{"title":"Chemical biology Books","description":"","products":[{"product_id":"physical-chemistry-for-the-life-sciences-9780198830108","title":"Physical Chemistry for the Life Sciences","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eA balanced presentation of the concepts of physical chemistry, and their applications to biology and biochemistry. Written to straddle the worlds of physical chemistry and the life sciences, it shows how the tools of physical chemistry can elucidate biological questions.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eFocus 1: Biochemical Thermodynamics: The First Law Focus 2: Biochemical Thermodynamics: The Second Law Focus 3: Water and Aqueous solutions Focus 4: Chemical equilibrium Focus 5: Ion and Electron Transport Focus 6: The Rates of Reactions Focus 7: Biochemical kinetics Focus 8: Atoms Focus 9: Molecules Focus 10: Macromolecules and self-assembly Focus 11: Biochemical spectroscopy Focus 12: Scattering techniques Focus 13: Gravimetric methods","brand":"Oxford University Press","offers":[{"title":"Default Title","offer_id":48732800942423,"sku":"9780198830108","price":137.74,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9780198830108.jpg?v=1791378727"},{"product_id":"ecotoxicology-9781108819732","title":"Ecotoxicology","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eEcotoxicology offers a comprehensive overview of the science underpinning the recognition and management of environmental contamination. It describes the toxicology of environmental contaminants, the methods used for assessing their toxicity and ecological impacts, and approaches employed to mitigate pollution and ecological health risks globally. Chapters cover the latest advances in research, including genomics, natural toxins, endocrine disruption and the toxicology of radioactive substances. The second half of the book focuses on applications, such as cradle-to-grave effects of selected industries, legal and economic approaches to environmental regulation, ecological risk assessment, and contaminated site remediation. With short capsules written by invited experts, numerous case studies from around the world and further reading lists, this textbook is designed for advanced undergraduate and graduate one-semester courses. It is also a valuable reference for graduate students and professionals. Online resources for instructors and students are also available.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePreamble; Preface; Part I. Approaches and Methods: 1. The history and emergence of ecotoxicology as a science Pamela Welbourn and Peter V. Hodson; 2. Measuring toxicity Peter V. Hodson and David A. Wright; 3. Contaminant uptake and bioaccumulation: mechanisms, kinetics and modelling Peter G. C. Campbell, Peter V. Hodson, Pamela M. Welbourn, David A. Wright; 4. Methods in ecotoxicology Peter. V. Hodson and David W. Wright; 5 Ecotoxicogenomics Valérie S. Langlois and Christopher J. Martyniuk; Part II. Toxicology of Individual Substances: 6. Metals and metalloids Peter G. C. Campbell, Pamela M. Welbourn and Christopher D. Metcalfe; 7. Organic compounds Christopher D. Metcalfe, David A. Wright, Peter V. Hodson; 8. Endocrine disrupting chemicals Christopher D. Metcalfe, Christopher J. Martyniuk, Valérie S. Langlois, and David A. Wright; 9. Natural toxins David A. Wright and Pamela M. Welbourn; 10. Ionising radiation Louise Winn; Part III. Complex Issues: 11. Complex issues, multiple stressors and lessons learned Pamela M. Welbourn, Peter G. C. Campbell, Peter V. Hodson and Christopher D. Metcalfe) 12. Regulatory toxicology and ecological risk assessment Peter V. Hodson, Pamela Welbourn and Peter G. C. Campbell; 13. Recovery of contaminated sites Pamela M. Welbourn and Peter V. Hodson; 14. Emerging concerns and future visions David A. Wright and Peter G. C. Campbell; Index.","brand":"Cambridge University Press","offers":[{"title":"Default Title","offer_id":48738335129943,"sku":"9781108819732","price":42.74,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781108819732.jpg?v=1723811941"},{"product_id":"natural-product-biosynthesis-chemical-logic-and-enzymatic-machinery-9781839165641","title":"Natural Product Biosynthesis: Chemical Logic and","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eAuthored by leading experts in the enzymology of natural product biosynthesis, this completely revised and updated edition provides a description of the types of natural products, the biosynthetic pathways that enable the production of these molecules, and an update on the discovery of novel products in the post-genomic era. Although some 500 000 – 600 000 natural products have been isolated and characterized over the past two centuries, there may be a 10-fold greater inventory awaiting immediate exploration based on biosynthetic gene cluster predictions. The approach of this book is to codify the chemical logic that underlies each natural product structural class as they are assembled from building blocks of primary metabolism.    This second edition integrates many new findings into the sets of principles of the first edition that parsed categories of natural product chemistries into the underlying enzymatic mechanisms and the catalytic machinery for building the varied and complex end product metabolites. New chapters include evaluation of a core set of thermodynamically activated but kinetically stable metabolites that power both primary and secondary metabolic pathways. Also, after decades of uncertainty about the existence of various pericyclase classes, a series of genome mining, heterologous expression, and enzymatic activity characterization have validated a plethora of pericyclases over the past decade. The several types of pericyclases are involved in biosynthetic complexity generation of almost every major category of natural products.    This text will serve as a reference point for chemists of every subdiscipline, including synthetic organic chemists and medicinal chemists. It will also be valuable to bioinformatic and computational biologists, pharmacognocists and chemical ecologists, and bioengineers and synthetic biologists.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eMajor Classes of Natural Product Scaffolds and Enzymatic Biosynthetic Machinery; The Chemical Logic for Major Reaction Types; Polyketide Natural Products; Peptide Natural Products I: RiPPs; Peptide Natural Products II: Nonribosomal Peptides; Isoprenoids\/Terpenes; Alkaloids I; Purine- and Pyrimidine-derived Natural Products; Phenylpropanoid Natural Product Biosynthesis; Alkaloids II: Indole Terpenes; Natural Product Oligosaccharides and Glycosides; Oxygenases, Thwarted Oxygenases, and Oxygen-dependent Halogenases; S-Adenosylmethionine; Pericyclases in Natural Product Biosynthesis; Natural Products Isolation and Characterization: Gene-independent Approaches; Natural Products in the Post Genomic Era","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48741984698711,"sku":"9781839165641","price":94.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781839165641.jpg?v=1720059562"},{"product_id":"the-genesis-machine-our-quest-to-rewrite-life-in-the-age-of-synthetic-biology-9781541797925","title":"The Genesis Machine: Our Quest to Rewrite Life in","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cp\u003eSynthetic biology is the technique that enables us not just to read and edit but also write DNA to program living biological structures as though they were tiny computers. Unlike cloning Dolly the sheep-which cut and copied existing genetic material-the future of synthetic biology might be something like an app store, where you could download and add new capabilities into any cell, microbe, plant, or animal.\u003cbr\u003e\u003cbr\u003eThis breakthrough science has the potential to mitigate, perhaps solve, humanity's immediate and longer-term existential challenges: climate change; the feeding, clothing, housing, and caring for billions of humans; fighting the next viral outbreak before it becomes a global pandemic; old age as a treatable pathology; bringing back extinct animals.\u003cbr\u003e\u003cbr\u003eIt could also be anarchic and socially destructive. With our governing structures created in an era before startling advances in technology, we are not prepared for a future in which life could be manipulated or programmed.\u003cbr\u003e\u003cbr\u003eAs futurist Amy Webb and synthetic biologist Andrew Hessel show in this book, within the next decade, we will need to make important decisions: whether to program novel viruses to fight diseases, what genetic privacy will look like, who will \"own\" living organisms, how companies should earn revenue from engineered cells, and how to contain a synthetic organism in a lab. \u003ci\u003eThe Genesis Machine?\u003c\/i\u003e provides the background for us to understand and grapple with these issues, and think through the religious, philosophical, and ethical implications for the future.\u003c\/p\u003e","brand":"PublicAffairs,U.S.","offers":[{"title":"Default Title","offer_id":48867549446487,"sku":"9781541797925","price":16.14,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781541797925.jpg?v=1722283822"},{"product_id":"chemistry-biochemistry-on-the-leading-edge-9781590334485","title":"Chemistry \u0026 Biochemistry on the Leading Edge","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886473556311,"sku":"9781590334485","price":88.79,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781590334485.jpg?v=1722540224"},{"product_id":"new-perspectives-in-chemistry-biochemistry-9781590334492","title":"New Perspectives in Chemistry \u0026 Biochemistry","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886473687383,"sku":"9781590334492","price":88.79,"currency_code":"GBP","in_stock":true}]},{"product_id":"studies-in-chemistry-biochemistry-9781590335673","title":"Studies in Chemistry \u0026 Biochemistry","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eScience can do much good for mankind or can cause a catastrophe for mankind if it is handled by terrorists, (even aircraft can be turned into weapons of destruction as we have seen on September 11 2001 in New York City and Washington DC) This volume deals with science for the sake of mankind. Chemical physics, which combines chemistry and physics, and biochemical physics, which combines chemistry, physics and biology, have been developing quite radically recently. This holds true for pure and applied science as well. Some examples of such success are given in this book. Included in this volume are papers from Russian scientists, scientists from the republics of the former USSR and papers from scientists in western countries.","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886476210519,"sku":"9781590335673","price":83.29,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781590335673.jpg?v=1791474403"},{"product_id":"focus-on-chemistry-biochemistry-9781590335963","title":"Focus on Chemistry \u0026 Biochemistry","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886477029719,"sku":"9781590335963","price":74.39,"currency_code":"GBP","in_stock":false}]},{"product_id":"new-developments-in-chemistry-biochemistry-9781590336533","title":"New Developments in Chemistry \u0026 Biochemistry","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eNew Developments in Chemistry \u0026amp; Biochemistry","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886479126871,"sku":"9781590336533","price":76.49,"currency_code":"GBP","in_stock":false}]},{"product_id":"international-perspectives-on-chemistry-biochemistry-research-9781590336885","title":"International Perspectives on Chemistry \u0026","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886479421783,"sku":"9781590336885","price":74.39,"currency_code":"GBP","in_stock":false}]},{"product_id":"biochemistry-chemistry-research-development-9781590336946","title":"Biochemistry \u0026 Chemistry: Research \u0026 Development","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886479618391,"sku":"9781590336946","price":81.59,"currency_code":"GBP","in_stock":false}]},{"product_id":"d-amino-acids-a-new-frontier-in-amino-acids-protein-research-practical-methods-protocols-9781600210754","title":"D-Amino Acids: A New Frontier in Amino Acids \u0026","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886583361879,"sku":"9781600210754","price":176.24,"currency_code":"GBP","in_stock":false}]},{"product_id":"amino-acid-receptor-research-9781604562835","title":"Amino Acid Receptor Research","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eAmino acid receptors and cell surface proteins that bind amino acids and trigger changes which influence the behaviour of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition. This book presents the latest research in the field.","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886632972631,"sku":"9781604562835","price":159.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781604562835.jpg?v=1791474577"},{"product_id":"inorganic-biochemistry-research-progress-9781604567083","title":"Inorganic Biochemistry: Research Progress","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886646866263,"sku":"9781604567083","price":149.99,"currency_code":"GBP","in_stock":false}]},{"product_id":"progress-in-chemistry-biochemistry-kinetics-thermodynamics-synthesis-properties-applications-volume-1-9781606923443","title":"Progress in Chemistry \u0026 Biochemistry: Kinetics,","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886690283863,"sku":"9781606923443","price":999.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781606923443.jpg?v=1722541196"},{"product_id":"success-in-chemistry-biochemistry-minds-flight-in-time-space-volume-4-a-festschrift-in-honor-of-the-75th-birthday-of-professor-gennady-e-zaikov-9781606923436","title":"Success in Chemistry \u0026 Biochemistry: Mind's","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThe given compilation is devoted to the anniversary of Professor Gennady E Zaikov. The compilation itself has been prepared by those scientists with whom G. E. Zaikov has worked during more than half a century of his scientific career.","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886690349399,"sku":"9781606923436","price":265.59,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781606923436.jpg?v=1722541195"},{"product_id":"kinetics-thermodynamics-for-chemistry-biochemistry-volume-two-9781606923528","title":"Kinetics \u0026 Thermodynamics for Chemistry \u0026","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886690513239,"sku":"9781606923528","price":143.24,"currency_code":"GBP","in_stock":false}]},{"product_id":"chemistry-biochemistry-from-pure-to-applied-science-a-festschrift-in-honor-of-the-75th-brithday-of-professor-gennady-e-zaikov-9781606923535","title":"Chemistry \u0026 Biochemistry: From Pure to Applied","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886691037527,"sku":"9781606923535","price":136.49,"currency_code":"GBP","in_stock":false}]},{"product_id":"organic-chemistry-biochemistry-biotechnology-renewable-resources-research-development-volume-1-today-tomorrow-9781620811559","title":"Organic Chemistry, Biochemistry, Biotechnology \u0026","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886945481047,"sku":"9781620811559","price":159.74,"currency_code":"GBP","in_stock":false}]},{"product_id":"organic-chemistry-biochemistry-biotechnology-renewable-resources-research-development-volume-2-tomorrow-perspectives-9781620811597","title":"Organic Chemistry, Biochemistry, Biotechnology \u0026","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48886945710423,"sku":"9781620811597","price":170.39,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781620811597.jpg?v=1722542296"},{"product_id":"an-introduction-to-drug-carriers-9781685071486","title":"An Introduction to Drug Carriers","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThe book An Introduction to Drug Carriers provides a broad overview of drug carriers. Drug carriers play medically important roles in delivering drugs to pinpointed regions in biological systems. The cell hosts most of the disorders related to diseases. Therefore, the cell is also considered the main target region for most drugs. Some of the cellular compartments, especially cell-based membranes, which are geometrically constructed with both hydrophobic and hydrophilic layers\/boundaries, often appear as barriers against vital candidate drugs' journey to the target regions. Besides, there are off-target structures that need to be avoided for drugs to get adsorbed. Otherwise, drugs may cause unbearable off-target binding originated toxicity, which would reduce the efficacy of the drugs. Appropriate choice of drug carriers may help specific drugs to get conjugated and be delivered to their optimal target structures. Biophysical and biochemical characterization of drug carriers concerning their role as vehicles to carry certain drugs may be obtained using engineering techniques. Manipulation in the cellular sites that cause disturbances in drug delivery is another biomedical option utilized to ensure smooth drug delivery. Various theoretical and experimental techniques are utilized to address all these issues related to drug carriers. The collected chapters written by experts in the field will help the subject matter be understood thoroughly.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePreface; Cell Systems as Biological Drug Carriers; Vesicles as Drug Carriers; A Significant Role of Various Polymers Conjugated with Folic Acid into Micelles as a Drug Carrier in Receptor-Targeted Drug Delivery for Breast Cancer; Emerging Applications of Drug Delivery Systems in Odontogenic Infections  An Overview; Nanotechnology of Cell Membrane and Drug Delivery; Current Trends in Applications of Nanosponges: A Multifaceted Drug Carrier System.","brand":"Nova Science Publishers Inc","offers":[{"title":"Default Title","offer_id":48887491363159,"sku":"9781685071486","price":113.59,"currency_code":"GBP","in_stock":false}]},{"product_id":"molybdenum-and-tungsten-enzymes-biochemistry-9781782620891","title":"Molybdenum and Tungsten Enzymes: Biochemistry","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThere has been enormous progress in our understanding of molybdenum and tungsten enzymes and relevant inorganic complexes of molybdenum and tungsten over the past twenty years. This set of three books provides a timely and comprehensive overview of the field and documents the latest research.  The first volume in the set focusses on the enzymes themselves, and discusses active sites and substrate channels of relevant proteins. The book begins with an introductory overview of the whole field. Chapters are contributed by world leaders and topics covered include pyranopterin cofactor biosynthesis and incorporation of the mature cofactor into apoprotein. Subsequent volumes cover the bioinorganic chemistry relevant to these enzymes and the full range of spectroscopic and theoretical methods that are used to investigate their physical and electronic structure and function.  This text will be a valuable reference to workers both inside and outside the field, including graduate students and young investigators interested in developing new research programs in this area.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePart I Molybdenum- and tungsten-containing enzymes; Abundance, ubiquity, and evolution of molybdoenzymes; Molybdenum cofactor biosynthesis; Bacterial molybdoenzymes; The prokaryotic Mo\/W-bisPGD enzyme family; Enzymes of the xanthine oxidase family; The sulfite oxidase family of Mo enzymes; Nitrogenase; Tungsten-containing enzymes; Part II Introduction and overview of synthetic Mo and W chemistry; Synthesis of mono- and bisdithiolene Mo and W model compounds; Pterin‐inspired Model Compounds of Molybdenum Enzymes; Synthesis of models for the xanthine oxidase family of enzymes; Electron transfer mechanisms in Mo and W compounds; Comparative kinetics of enzymes and models; Models of the metal clusters of nitrogenase; Part III Overview of spectroscopic and electronic studies of Mo and W enzymes; Spectroscopic and electronic structure studies of Mo model compounds and enzymes; Electron paramagnetic resonance studies of molybdenum enzymes; X-ray absorption spectroscopic studies of molybdenum enzymes; Electrochemistry of molybdenum and tungsten enzymes; Computational studies of molybdenum and tungsten enzymes; Nitrogen Fixation in Nitrogenase and Related Small-Molecule Models","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887690133847,"sku":"9781782620891","price":170.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782620891.jpg?v=1791476896"},{"product_id":"carbohydrate-chemistry-volume-41-9781782621218","title":"Carbohydrate Chemistry: Volume 41","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eWith the increase in volume, velocity and variety of information, researchers can find it difficult to keep up to date with the literature in the field. As the synthesis of novel carbohydrates and carbohydrate mimetics continues to be a major challenge for organic chemists, not least because of the increasingly interdisciplinary nature of carbohydrate science, Carbohydrate Chemistry Volume 41 will prove invaluable. Covering both chemical and biological science, this series collates modern carbohydrate research from theory to application and will be of great benefit to any researcher who wishes to learn about the latest developments in the carbohydrate field.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePreface; Design and synthesis of glycomimetics; Pyranose glycals in the generation of skeletal diversity; Recent developments in the stereoselective synthesis of deoxy glycosides; Lewis acid promoted anomerisation: recent developments and applications; Progress in the synthesis of mycothiol, its biosynthetic precursors and analogues; Synthetic receptors for molecular recognition of carbohydrates; Contribution of carbohydrate chemistry to assessment of the biological role of natural alpha-glycosides; Carbohydrate-carbohydrate interation: from hypothesis to confirmation","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887690559831,"sku":"9781782621218","price":314.95,"currency_code":"GBP","in_stock":true}]},{"product_id":"proteome-informatics-9781782624288","title":"Proteome Informatics","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThe field of proteomics has developed rapidly over the past decade nurturing the need for a detailed introduction to the various informatics topics that underpin the main liquid chromatography tandem mass spectrometry (LC-MS\/MS) protocols used for protein identification and quantitation. Proteins are a key component of any biological system, and monitoring proteins using LC-MS\/MS proteomics is becoming commonplace in a wide range of biological research areas. However, many researchers treat proteomics software tools as a black box, drawing conclusions from the output of such tools without considering the nuances and limitations of the algorithms on which such software is based. This book seeks to address this situation by bringing together world experts to provide clear explanations of the key algorithms, workflows and analysis frameworks, so that users of proteomics data can be confident that they are using appropriate tools in suitable ways.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTrade Review\u003c\/h2\u003eThis is a timely book for the proteomics researcher in guiding decision trees involved in the informatics pipelines of this rapidly developing field. The book does an excellent job in focusing on that part of the informatics discipline, both at the user interface and behind the scenes algorithms, that is of great importance to developing innovative and effective methods for protein interrogation. -- Taufika Islam Williams * Analytical and Bioanalytical Chemistry *\u003cbr\u003eBook’s topic: Proteomics, the comprehensive interrogation of proteins expressed by a living system, has enjoyed expeditious growth and development in recent years, as it brings together a range of informatics themes that fortify and support the everincreasing power of LC-MS\/MS platforms to tackle important biological questions. Proteins are the vehicles of change in living cells and understanding them is elemental to understanding molecular biology. The complexity of the proteomics workflow, from sample preparation to LC-MS\/MS to bioinformatics analyses, is such thatmore often than not, the intricacies and indeed shortcomings of the bioinformatics software are not carefully considered during data interpretation. This is an unwelcome prospect, given that comprehending the inner workings of living systems can be intimately tied to fluctuating patterns of protein expression,which can only be as thoroughly understood as the cumulative proteomics experiment allows. State-of-the-art sample preparation and LC-MS\/MS will only be as biologically informative as the informatics methods with which data are interrogated. Proteome informatics is described as the ever increasing collection of bioinformatics methodologies that can be exercised in the analysis of protein expression. The book Proteome informatics, edited byConradBessant and the 5th volume of the Royal Society of Chemistry on New Developments in Mass Spectrometry, describes the bioinformatics of proteome analyses in the very context of proteomics workflows. It is an opportune discussion by leading experts on the current state of this evolving discipline, highlighting the essential fund of knowledge that will enable the proteomics expert, who may or may not be well-versed in computer science or statistics, to exploit and construct algorithms that can effectively interrogate gigabytes of data, while keeping a sharp focus on the limitations of what such software can reasonably underscore about the system being studied.   Contents: This book is divided into four main sections, which follow an introductory chapter on proteome informatics. The first section describes protein identification and begins with manual de novo sequencing to more sophisticated de novo algorithms. The book steers into details of peptide spectrum matching by database search and the alternative spectral library search in use today. Despite the established advantages of the latter, the approach is only as good as the population of the library itself, which invariably limits the identification of experimental peptides and their post-translational modifications (PTMs). Discussion proceeds into peptide-spectrum match (PSM) scoring and validation, a lynchpin of proteome informatics which unequivocally dictates the “goodness of fit” in a given peptide (and subsequently protein) identification. Merits and demerits of common methods are briefly explored. This is proceeded by a chapter on protein grouping, which links identified peptides to identifying proteins. The section concludes with commentary on identification and positioning of the all-important PTMs. Indeed, the hundreds of in vivo PTMs (not to mention the many more possibilities of chemical modifications that may be artificially introduced into the system under investigation) are subject to change with changing cellular milieu, and hence are critical in a comprehensive proteomics study. The second section is dedicated to the quantification of proteins. Algorithms detailing MS1-based quantification are examined in its five components. The central point for such algorithms is the detection and quantification of peptidespecific signal patterns, called features. Peptide- and protein level identification are effected using precursor ion exact mass, charge state, and tandem MS. Chromatographic alignment fine-tunes all runs to a common retention time (RT) coordinate system such that corresponding features will display analogous RTs. -- Taufika Islam Williams * Analytical and Bioanalytical Chemistry - Review part 1 *\u003cbr\u003eInternal standard features are then used to derive normalization factors that correct for sample loading disparities and ionization variabilities. Protein-level differential analysis encompasses processes to quantify proteins via constituent peptide analyses, as well as approaches to determine protein regulation disparities across study samples. MS2-based quantification, which exploits abundance data of fragment ions in tandem MS spectra, is then discussed by drawing comparisons between spectral counting and reporter ion-based quantification. Discussion then veers into the bioinformatics support for selected reaction monitoring (SRM), the gold standard for accurate, unambiguous MS-based quantification. The section concludes with a chapter on dataindependent acquisition (DIA), which primarily differs from data-dependent acquisition (DDA) in that the window selection of the first mass analyzer is dynamic during DDA, whereas it is used to scan the entire spectrum during DIA. Data analysis can be tricky in DIA and the chapter does justice in surveying DIA theory, notable DIA methods employed today, and major considerations in data interrogation. The third section details the open source software landscape for bioinformatics in proteomics investigations. A key consideration is data formatting, given the breadth of academic and commercial software that is commonly exercised for proteomics data management. The section proceeds to discuss three major software platforms for proteomics data analysis pipelines: OpenMS (modular solution for proteomics and metabolomics), Galaxy (originally designed for the genomics research community), and R (programming language for statistical computing and graphics). Section 4 takes the reader into the broader territory of integrating proteomics data with that from other studies, particularly genomics and transcriptomics. Proteogenomics, the application of proteomics data to augment genome annotation, does not quite offer the sensitivities featured by RNA-Seq and does exhibit particular bioinformatics challenges. Nevertheless, a major advantage of this field is the successful interrogation of proteins whose exact sequences are missing from generic databases to which they are matched and whose function may have critical bearings on biological phenotype. The authors detail underlying theory, software platforms, data formats, current challenges, and future direction. The section, and indeed the book, concludes with a discussion of the union between proteomics and transcriptomics data or proteome informed by transcriptomics (PIT). While PIT data can be used for genome annotations, the power behind this approach lies in facilitating proteomic analyses in the absence of a reference genome, not to mention the pinpointing of sequence variation and examining such dynamic events as isoform switching. In PIT, the protein database is created from RNA-Seq data. The authors elaborate PIT applications and data management options.   Comparison with the existing literature: This book is distinctive in how it frames bioinformatics strictly in its relevance to designing a proteomics experiment. The authors draw upon only that portion of knowledge from key disciplines that intersect with proteomics to better construct sophisticated and robust informatics pipelines. In the last decade, a number of books have addressed bioinformatics as it relates to the rapidly developing field of proteomics, notably Bioinformatics for comparative proteomics edited by Cathy Wu and Chuming Chen (2010), Proteome bioinformatics edited by Simon Hubbard and Andrew Jones (2010), Bioinformatics of human proteomics edited by XiagdongWang (2013), Mass spectrometry data analysis in proteomics edited by Rune Matthiesen (2013), Bioinformatics: genomics and proteomics by Ruchi Singh (2015), Proteome bioinformatics edited by Shivakumar Keerthikumar and Suresh Mathivanan (2016), Exploring genomics, proteomics and bioinformatics by Charles Malkoff (2016), Modern proteomics—sample preparation, analysis and practical applications edited by Hamid Mirzaei and Martin Carrasco (2016), Protein bioinformatics edited by Cathy Wu, Cecilia Arighi and Karen Ross (2017). Some provide a bird’s eye view of informatics as applied to proteomics. Some delve deeper into PTMs, while others focus on database searching aspects, cancer research, human proteins, or the interplay between gene expression and protein expression. Yet others center on proteomics while discussing informatics as a part of the whole experiment or explore specific MS-based methods and data analysis strategies. This book presents the advantage of elaborating important bioinformatics details, both at the user interface and behind the scenes (i.e., software algorithms), that should be carefully considered by the proteomics scientist in experimental design to better understand and interpret the data.   Critical assessment: The book performs a thorough assessment of informatics processes and considerations in proteomics. Representative examples of informatics workflows are provided and discussed, but given the breadth of the subject, not all important bioinformatics software that is currently used in proteomics (i.e., Byonic™ by Protein Metrics) was able to receive attention. This is relevant because a detailed comparison of the inner workings of proteomics software in use today would better equip the proteomics researcher to build effective workflows, which is the major purpose of this book. Nevertheless, the discussions of examples that are provided do highlight the considerations of importance when selecting software and of course when using the software in the proteomics experiment. It must be mentioned that Bessant has put together a very useful body of work, harnessing the expertise of over 35 contributing authors to cover a number of very relevant topics in the informatics arena of proteomics science. Some topics are more in-depth than others perhaps not as thorough as they ought to be. There is unavoidable overlap with limited inter-chapter connections. The book would have benefited from additional chapters describing the integration of proteomics data with other metadata experiments (i.e., metabolomics, lipidomics) and the unique bioinformatics challenges they present. Mass spectrometry imaging (MSI), a rapidly emerging and developing field, is not covered in much detail in the context of this book. The particulars of open source software in proteomics, along with protein identification and quantification, are overall, quite helpful.   Readership recommendation: The target audience for this book includes scientists and doctoral students using proteomics science to understand biological systems. Given the interdisciplinary nature of proteomics, this book will be of benefit to and of interest to the bioanalytical chemist, biophysicist, biomedical engineer, biologist, and indeed the biostatistician. The book is constructed in such a manner that it includes enough introductory material for those new to proteome analysis, as well as enough depth and details for experts and specialists. No doubt, it offers a very useful fund of knowledge to the proteomics researcher.   Summary: Proteomics research is inherently multidisciplinary in its workflows, as it brings together concepts from chemistry, engineering, computer science, biochemistry, statistics, mathematics, and biology to understand protein expression. This is a timely book for the proteomics researcher in guiding decision trees involved in the informatics pipelines of this rapidly developing field. The book does an excellent job in focusing on that part of the informatics discipline, both at the user interface and behind the scenes algorithms, that is of great importance to developing innovative and effective methods for protein interrogation. Informatics is placed squarely within the framework of proteomics and this will be most beneficial indeed for the target audience. -- Taufika Islam Williams * Analytical and Bioanalytical Chemistry - Review part 2 *\u003cbr\u003eby Charles Malkoff (2016), Modern proteomics—sample preparation, analysis and practical applications edited by Hamid Mirzaei and Martin Carrasco (2016), Protein bioinformatics edited by Cathy Wu, Cecilia Arighi and Karen Ross (2017). Some provide a bird’s eye view of informatics as applied to proteomics. Some delve deeper into PTMs, while others focus on database searching aspects, cancer research, human proteins, or the interplay between gene expression and protein expression. Yet others center on proteomics while discussing informatics as a part of the whole experiment or explore specific MS-based methods and data analysis strategies. This book presents the advantage of elaborating important bioinformatics details, both at the user interface and behind the scenes (i.e., software algorithms), that should be carefully considered by the proteomics scientist in experimental design to better understand and interpret the data.   Critical assessment: The book performs a thorough assessment of informatics processes and considerations in proteomics. Representative examples of informatics workflows are provided and discussed, but given the breadth of the subject, not all important bioinformatics software that is currently used in proteomics (i.e., Byonic™ by Protein Metrics) was able to receive attention. This is relevant because a detailed comparison of the inner workings of proteomics software in use today would better equip the proteomics researcher to build effective workflows, which is the major purpose of this book. Nevertheless, the discussions of examples that are provided do highlight the considerations of importance when selecting software and of course when using the software in the proteomics experiment. It must be mentioned that Bessant has put together a very useful body of work, harnessing the expertise of over 35 contributing authors to cover a number of very relevant topics in the informatics arena of proteomics science. Some topics are more in-depth than others perhaps not as thorough as they ought to be. There is unavoidable overlap with limited inter-chapter connections. The book would have benefited from additional chapters describing the integration of proteomics data with other metadata experiments (i.e., metabolomics, lipidomics) and the unique bioinformatics challenges they present. Mass spectrometry imaging (MSI), a rapidly emerging and developing field, is not covered in much detail in the context of this book. The particulars of open source software in proteomics, along with protein identification and quantification, are overall, quite helpful. Readership recommendation: The target audience for this book includes scientists and doctoral students using proteomics science to understand biological systems. Given the interdisciplinary nature of proteomics, this book will be of benefit to and of interest to the bioanalytical chemist, biophysicist, biomedical engineer, biologist, and indeed the biostatistician. The book is constructed in such a manner that it includes enough introductory material for those new to proteome analysis, as well as enough depth and details for experts and specialists. No doubt, it offers a very useful fund of knowledge to the proteomics researcher. -- Taufika Islam Williams * Analytical and Bioanalytical Chemistry - Review part 3 *\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eIntroduction to Proteome Informatics; De Novo Sequencing; Peptide-Spectrum Matching; PSM Scoring and Validation; Protein Grouping; Identification and Localisation of Post Translational Modifications; Algorithms for MS1-Based Quantitation; Algorithms for MS2-Based Quantitation; Informatics Solutions for Selected Reaction Monitoring; Data Analysis for Data Independent Acquisition; Mining Proteomics Repositories; Data Formats of the Proteomics Standards Initiative; OpenMS; Using Galaxy for Proteomics; R for Proteomics; Proteogenomics: Proteomics for Genome Annotation; Proteomics Informed by Transcriptomics; Subject Index","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887691510103,"sku":"9781782624288","price":170.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782624288.jpg?v=1791476900"},{"product_id":"the-biological-chemistry-of-nickel-9781782624981","title":"The Biological Chemistry of Nickel","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eMetal ions play key roles in biology. Many are essential for catalysis, for electron transfer and for the fixation, sensing, and metabolism of gases. Others compete with those essential metal ions or have toxic or pharmacological effects.   This book is structured around the periodic table and focuses on the control of metal ions in cells. It addresses the molecular aspects of binding, transport and storage that ensure balanced levels of the essential elements. Organisms have also developed mechanisms to deal with the non-essential metal ions. However, through new uses and manufacturing processes, organisms are increasingly exposed to changing levels of both essential and non-essential ions in new chemical forms. They may not have developed defenses against some of these forms (such as nanoparticles).   Many diseases such as cancer, diabetes and neurodegeneration are associated with metal ion imbalance. There may be a deficiency of the essential metals, overload of either essential or non-essential metals or perturbation of the overall natural balance.   This book is the first to comprehensively survey the molecular nature of the overall natural balance of metal ions in nutrition, toxicology and pharmacology. It is written as an introduction to research for students and researchers in academia and industry and begins with a chapter by Professor R J P Williams FRS.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eIntroduction to the Biological Chemistry of Nickel; Oceanic Nickel Biogeochemistry and the Evolution of Nickel Use; Nickel Toxicity and Carcinogenesis; Nickel Binding Sites - Coordination Modes and Thermodynamics; Urease; Crystallographic Analyses of the Active Site Chemistry and Oxygen Sensitivity of [NiFe(Se)]-Hydrogenases; One-Carbon Chemistry of Nickel-Containing Carbon Monoxide Dehydrogenase and Acetyl-CoA Synthase; Biochemistry of Methyl-Coenzyme M Reductase; Reinventing the Wheel: The NiSOD Story; Nickel Glyoxalase I; Lactate Racemase and Its Niacin-Derived, Covalently-Tethered, Nickel Cofactor; Nickel in Microbial Physiology - from Single Proteins to Complex Trafficking Systems: Nickel Import\/Export; Nickel Regulation; Nickel Metallochaperones: Structure, Function, and Nickel-Binding Properties; Cross-Talk Between Nickel and Other Metals in Microbial Systems; Nickel and Virulence in Bacterial Pathogens; Application of Ni(II)-Binding Proteins","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887691837783,"sku":"9781782624981","price":160.55,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782624981.jpg?v=1791476902"},{"product_id":"chemical-diversity-of-plant-specialized-metabolites-a-biosynthetic-approach-9781837670451","title":"Chemical Diversity of Plant Specialized","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThe phytochemical constituents of plants fall into two main categories based on their role in basic metabolic processes: primary and secondary. Primary metabolites are involved in basic life functions and are similar in all living cells, whereas secondary metabolites are derived from subsidiary pathways. Although traditionally referred to as secondary metabolites, more recently these compounds have been termed ‘plant specialized metabolites’, as the exact biochemical boundary between primary and secondary metabolites has not been fully established.    Plant specialized metabolites are the main elements in the study and use of ‘medicinal’ plants and herbs, as well as in nutrition and food chemistry. In modern medicine, plant specialized metabolites provide many of the lead compounds in the production of medicines targeted at treating a broad variety of diseases. Such metabolites also play an important role in sessile plants to resist and withstand different biotic and abiotic stresses. Plant specialized metabolites are classified according to their chemical structures and this book will present the different classes in turn, while discussing their sources and distribution in plant families, their biosynthetic pathways, and their important and notable uses in phytochemistry and pharmacology.   Chemical Diversity of Plant Specialized Metabolites will be a useful guide and reference point for chemists and students in many disciplines including synthetic organic chemists, medicinal chemists, plant scientists, pharmacognosists, chemical ecologists, bioengineers, and synthetic biologists, in addition to those working in related fields.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eIntroduction;Carbohydrates and Glycosides;Acetate-malonate Pathway: Fatty Acids and Polyketides;Mevalonate and Methylerythritol Phosphate Pathway: Terpenoids and Steroids;Shikimic Acid Pathway: Phenols;Alkaloids;Essential Oils and Resins","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887969710423,"sku":"9781837670451","price":94.05,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781837670451.jpg?v=1791478242"},{"product_id":"methods-and-strategies-for-c-n-bond-formation-reactions-9781837671793","title":"Methods and Strategies for C–N Bond Formation","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eOrganic compounds containing amino groups are one of the most important classes of chemicals in both academia and industry. This class of materials is a very important structural motif in organic synthesis due to its widespread applications in natural products, agrochemicals, pharmaceuticals, and advanced materials.   This book is a concise overview of modern approaches to N-alkylation and N-arylation of primary, secondary and tertiary amines using alkylating and arylating reagents with amino sources found in both basic and applied chemical research. The work also discusses key examples of amine synthesis from a sustainable perspective, using deep eutectic solvents and the application of amines in different areas. It is an ideal reference for advanced and postgraduate students as well as academic and industrial chemists working in organic, natural product, catalytic, medicinal, and polymer chemistry.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eHistorical Background of the Synthetic Methods and Properties of Amines;Synthetic Methods for Alkyl Amines;Synthetic Methods for Primary Anilines;Synthetic Methods for Diarylamines and Triarylamine;Synthesis of Amines from a Sustainable Perspective in Deep Eutectic Solvents, and Application of Amines in Different Areas","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887970431319,"sku":"9781837671793","price":151.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781837671793.jpg?v=1791478243"},{"product_id":"microalgae-for-sustainable-products-the-green-synthetic-biology-platform-9781839165627","title":"Microalgae for Sustainable Products: The Green","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eMicroalgae are a diverse set of eukaryotic photosynthetic organisms with great potential for being used to produce various high-value molecules. Using synthetic biology to manipulate and control the metabolic processes of microalgae, scientists hope to find economical and sustainable alternatives for commercial production of high value biochemicals and other metabolites for diverse applications.    Highlighting the immense potential of microalgae as a renewable and sustainable source of commercially important, high-value biomolecules, this book covers the recent advances in the resources, tools, and techniques used for genetic engineering of microalgae. Also discussed are the legislative challenges associated with genetically engineered microalgae, their derived products and their uses, as well as socio-economic and environmental acceptance.  Written to be accessible to a wide audience, this book will be a useful reference to students and researchers from both academia and industry, as well as policy makers, for understanding the current status, trends and future possibilities of using microalgae for biotechnological applications.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eMicroalgae as a Renewable and Sustainable Source of High Value Metabolites;Recent Advances and Challenges in Establishing Commercial Scale Multi-product Microalgal Biorefineries;Understanding Metabolic Pathways and Their Network to Augment Microalgal Strain Performance for Industrially Important Metabolite Production;Advances in the Resources to Augment Microalgal Genetic Engineering: Omics-based Resources, Mutant Libraries, and High-throughput Screening Techniques;Recent Advances in Microalgal Genome Editing with Special Emphasis on CRISPR Mediated Modification Systems;Microalgae as a Sustainable Synthetic-biology Platform for the Production of Recombinant Proteins: Advantages, Bottlenecks and Case Studies;Genetic Engineering of Microalgae for Enhanced Photosynthetic Efficiency, CO2 Fixation, and Fuel-based Products;Genetic Engineering of Microalgae for Non-fuel, High-value Biochemicals of Industrial Significance;Use of Genetically Modified Algae: Consumption Safety Challenges, Current Legislations, and Socio-economic and Environmental Concerns;Microalgal Product Basket: Portfolio Positioning Across Food, Feed, and Fuel Segments with Industrial Growth Projections","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887996350807,"sku":"9781839165627","price":85.5,"currency_code":"GBP","in_stock":true}]},{"product_id":"the-chemical-biology-of-carbon-9781839168024","title":"The Chemical Biology of Carbon","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eBuilding upon the previous volumes, The Chemical Biology of Sulfur, The Chemical Biology of Phosphorus, and The Chemical Biology of Nitrogen, this book examines the organic chemistry of life, The Chemical Biology of Carbon. It examines chemical biology open to carbon-containing natural metabolites that allow both retrospective and predictive behaviours of both biosynthetic and degradative metabolism in primary and secondary pathways. This book also notes the centrality of a core set of heterocycles in metabolites and coenzyme forms of vitamins and how that chemistry enables life. The organic chemical fundamental considerations are always tied to specific metabolites and metabolic transformations. This context makes this volume not a classical organic or even bioorganic approach to organic chemistry in vivo but instead a unique analysis of how the rules and reactivities of organic chemistry underlie the organic chemistry of life. The Chemical Biology of Carbon is an ideal reference and guide for medicinal chemists, chemical biologists, organic chemists as well as postgraduate, graduate and advanced undergraduate students in these areas and related disciplines.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eIntroduction to Carbon Chemical Biology; Olefin and Alkyne Functional Groups; C–O Bond Formation and Reactivity: A Family of Related Functional Groups; Carbon–Sulfur Bonds: Adding to Functional Group Inventory; Carbon–Nitrogen Functional Groups; Purines and Pyrimidines: Essential Nitrogen Heterocycles; Carbacyclic Metabolites: Alicyclic and Aromatic Rings in Chemical Biology; Heterocycles-I; Heterocycles in Chemical Biology-II: Vitamins; Routes That Make and Break C–H and C–C Bonds In Vivo I: Carbanion Generation; Routes to Make and Break C–C Bonds II: Carbon Electrophiles; Carbon Radicals; Cascades vs Concerted Reactions; Glucose Chemical Biology; C–C Bonds in Biosynthesis: Squalene and the Sterol Biosynthetic Pathway; Chemical Biology of the Nitrogen Heterocycle Porphobilinogen in Tetrapyrrole Macrocycle Biosynthesis","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48887997595991,"sku":"9781839168024","price":170.05,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781839168024.jpg?v=1791478330"},{"product_id":"carbohydrate-chemistry-and-biochemistry-structure-and-mechanism-9781849733274","title":"Carbohydrate Chemistry and Biochemistry:","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThis fully updated and expanded second edition of a highly popular text book focuses on the structure and mechanism in carbohydrate chemistry and biochemistry.   Carbohydrates play important roles in biological systems as energy sources, as structural materials, and as informational structures (when they are often attached to proteins or lipids). Their chemical reactivity and conformational behaviour is governed by mechanistic and stereochemical rules, which apply as much to enzymic as to non-enzymic reactivity. The same principles of reactivity and conformation govern changes brought about in the process industries, such as pulp, paper and food.   Extensively referenced with citations and a detailed index, the book contains everything the reader needs to know to start a carbohydrate research project with one of the real strengths being the treatment and integration of the important physical-chemical principles and methods (though lead references only are given to the finer points of carbohydrate synthesis).   The book is suitable for both researchers who are new to the subject and those more established as well as a readership from diverse backgrounds and interests, including chemists, biochemists, food scientists and technologists involved with the processing of polysaccharides in the paper, textile, cosmetics, biofuels and other industries.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTrade Review\u003c\/h2\u003e\"...the book provides an excellent and authoritative reference resource for beginning and established researchers interested in structural and mechanistic aspects of carbohydrate (biochemistry)\"\u003cbr\u003e\"useful addition to the library of individuals with interests in theglycoscience field, as well as students wishing to learn moreabout this area.\"\u003cbr\u003e\"the overall view of the text is favorable, since it covers so many varied topics, some perhaps unfamiliar to even the most seasoned glycoscientists\"\u003cbr\u003e\"...this is an excellent treatment of carbohydrate chemistry.  It belongs in libraries and on the bookshelves of carbohydrate chemists and biochemists.\"\u003cbr\u003e\"..an invaluable companion and introduction to the primary literature of the field.\"\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eStructures of the open-chain forms of reducing sugars and related molecules. Mechanistic probes of sugar carbonyl group additions; Conformations of Sugar Rings and Glycosidic Linkages; Nucleophilic Substitution a the Anomeric Centre; Enzymic Glycoside Hydrolysis and Transglycosylation: Kinetics and Mechanism; Primary Structure and Conformation of Oligosaccharides and Polysaccharides; Heterolytic Reactions of OH Groups; Heterolytic Chemistry of the Carbon Chain; Glycosyl Transferases and Oligosaccharide and Polysaccharide Biosynthesis; Glycoconjugates: Biosynthesis and Properties; One-electron Chemistry of Carbohydrates; Appendix; Subject Index","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888116445527,"sku":"9781849733274","price":79.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781849733274.jpg?v=1791478888"},{"product_id":"comprehensive-biomarker-discovery-and-validation-for-clinical-application-9781849734226","title":"Comprehensive Biomarker Discovery and Validation","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eComprehensive Biomarker Discovery and Validation for Clinical Application provides the reader with an extensive introduction into all aspects of proteomics biomarker discovery, validation and development. It discusses the current status of science and technology, its limitations, bottlenecks as well as future development trends to improve the success rate of translating biomarker discovery into useful clinical tests. The most important feature of the book is to provide an overview of current technologies and the challenges encountered during biomarker discovery and validation, such as patient selection, sample handling, data processing, statistical analysis and registration and approval of validated biomarkers through European and US regulatory authorities. The authors introduce the reader to each of these topics in significant detail and provide examples or guidelines for best practice. There are prominent chapters included on biomarkers in translational and personalised medicine; an introduction to regulatory affairs and bring biomarkers to the market; biomarker discovery and the use of mass spectrometry based profiling platforms; MALDI imaging techniques in tissue-based biomarkers discovery and a clinical application study on the use of diagnostic assays for early diagnosis of heart failure using various proteomic methods. The book concludes with a final chapter on future trends in biomarker discovery and validation. The book targets a readership of industrial and academic researchers that are involved in biomarker discovery and validation or that manage biobanks, develop sample preparation methods, analytical profiling systems and bioinformatics tools. Common pitfalls and success stories in biomarker discovery are highlighted and guidelines for best practice are provided for the different parts of the procedure. The book will be an essential information resource for scientists working in the field.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eIntroduction to biomarker discovery and validation; Clinical context of proteomics biomarker discovery and validation, authority regulations; Biomarker discovery: Patient selection; Biomarker discovery: Experimental design and biobanking; Biomarker discovery: body fluids; Biomarker discovery: tissues; Biomarker discovery: mass spectrometry based profiling platforms; Biomarker discovery: array based profiling platforms; Biomarker discovery: data preprocessing for LC-MS data; Biomarker discovery: data preprocessing for Maldi imaging, and 2D electrophoresis and protein arrays data; Biomarker discovery: statistical analysis and validation; Biomarker validation: biomarker validation methods; Functional biomarker validation; Clinical application: case studies Clinical application: summary and future technology development trends","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888117920087,"sku":"9781849734226","price":151.99,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781849734226.jpg?v=1791478891"},{"product_id":"dna-conjugates-and-sensors-9781849734271","title":"DNA Conjugates and Sensors","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eApplications of nucleic acids have developed recently to provide solutions for biosensors, diagnostic tools and as platforms for the assembly of complex structures. These developments have been possible as their base sequence can be used to assemble precise structures following simple and predictable rules. Self-assembled DNA can then be amplified using polymerase chain reaction (PCR) and this ultimately enables the preparation of synthetic nucleic acids. Their use as molecular tools or DNA-conjugates has recently been enhanced by the addition of other groups including enzymes, fluorophores and small molecules. Written by leaders in the field, this volume describes the preparation and application of these DNA-conjugates. Several have been used as sensors (aptamers, riboswitches and nanostructures) based on the ability of nucleic acids to adopt specific structures in the presence of ligands, whilst others link reporter groups such as proteins or fluorophores to RNA or DNA for detection, single molecule studies, and increasing the sensitivity of PCR. The book is relevant to researchers in areas related to analytical chemistry, chemical biology, medicinal chemistry, molecular pharmacology, and structural and molecular biology.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eFluorophore-functionalised Locked Nucleic Acids (LNAs); Fluorophore Conjugates for Single Molecule Work; Small Molecule–Oligonucleotide Conjugates; Small Molecule–RNA Conjugates; Click Chemistry – a Versatile Method for Nucleic Acid Labelling, Cyclisation and Ligation; Therapeutic Applications of Nucleic Acid Aptamer Conjugates; pH Sensitive DNA Devices; Making Sense of Catalysis: The Potential of DNAzymes as Biosensors; Electrochemical Techniques as Powerful Readout Methods for Aptamer-based Biosensors; Oligonucleotide Conjugates for Detection of Specific Nucleic Acid Sequences; Nucleic Acid–Nanoparticle Conjugate Sensors for Use with Surface Enhanced Resonance Raman Scattering (SERRS); Covalent and Non-covalent Conjugates of Oligonucleotides as Artificial Restriction DNA Cutters","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888117985623,"sku":"9781849734271","price":146.29,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781849734271.jpg?v=1791478890"},{"product_id":"carbohydrate-chemistry-volume-38-9781849734394","title":"Carbohydrate Chemistry: Volume 38","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eIn this volume, glycochemistry and glycobiology have been combined to demonstrate the contribution of organic chemistry, modern analytics, biological and biochemical expertise to the increasingly important field of glycomincs. A polysaccharide immunomodulator with therapeutic implications, carbohydrate vaccines, new findings emphasizing the influence of carbohydrate decoration on the regulation of inflammatory response and new therapeutic approaches in the treatment of acute and chronic inflammatory diseases, recent approachesin the treatment of acute and chronic inflammatory diseases, recent progress on glycoengineering based on a glycosylation, and key aspects of the glycosylation changes associated with bladder cancer are amongst the subjects presented in this volume.   The contribution of glycochemistry to innovation in glycosciences is shown with chapters covering highly functionalized exo-glycals for the generation of molecular diversity in a chemoselective manner, imino sugar glycosidase inhibitors, carbasugars, multivalent glycoconjugates, including glycodendrimers, glyconanotubes, and glyconanoparticles, and their uses in medicinal chemistry, as well as artificial saccharide-based and saccharide functionalized gene delivery systems. Siderphores based on monosaccharides (which have proven effective for Gram-negative bacteria and mycobacteria), and the so-called smart materials, (which can modulate and control cell behaviour), complete the volume.   Volume 38 of Carbohydrate Chemistry - Chemical and Biological Apporaches contains contributions ranging from glycochemistry to glycobiology. This collection demonstrates in a meaningful way how the interdisciplinary approach of an international glyconetwork can advance the field of carbohydrate research in Europe and worldwide.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e1. Applications of glycobiology: biological and immunological effects of a chemically modified amylose-derivative; 2. Lipopolysaccharide structure and biological activity of Cystic fibrosis pathogens; 3. Synthesis of inner core lipopolysaccharide structures for the development of vaccines and antibiotics against Gram-negative bacterial infections; 4. Synthetic Glycopeptides in Vaccine Development and Antibody Epitope Mapping; 5. Posttranslational sialylation and its impact on leukocyte recruitment during inflammation; 6. Glycoengineering of protein-based therapeutics; 7. Exploring CDG diagnostic tools; 8. Bladder cancer: glycosylation insights; 9. Levansucrases of Pseudomonas bacteria: novel approaches for protein expression, assay of enzymes, fructooligosaccharides and heterooligofructans; 10. Recent advances on the application of NMR methods to study the conformation, dynamics and molecular recognition features of carbohydrates; 11. Glycosidase inhibitors: versatile tools in glycobiology; 12. An overview of key routes for the transformation of sugars into carbasugars and related compounds; 13. Multivalent glycoconjugates in Medicinal Chemistry; 14. Glycotransporters for gene delivery; 15. Furanose-based templates in the chemoselective generation of molecular diversity; 16. Synthesis of carbohydrate-based artificial siderophores and their biological applications; 17. Smart biomaterials: the contribution of glycoscience","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888118214999,"sku":"9781849734394","price":299.95,"currency_code":"GBP","in_stock":true}]},{"product_id":"carbohydrate-chemistry-chemical-and-biological-approaches-volume-39-9781849735872","title":"Carbohydrate Chemistry: Chemical and Biological","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eIn this volume, glycochemistry and glycobiology have been combined to demonstrate the contribution of organic chemistry, modern analytics, biological and biochemical expertise to the increasingly important field of glycomics. A polysaccharide immunomodulator with therapeutic implications, carbohydrate vaccines, new findings emphasizing the influence of carbohydrate decoration on the regulation of inflammatory response and new therapeutic approaches in the treatment of acute and chronic inflammatory diseases, recent progress on glycoengineering based on a glycosylation strategy to optimize protein drugs, congenital disorders of glycosylation, and key aspects of the glycosylation changes associated with bladder cancer are amongst the subjects presented in this volume. The contribution of glycochemistry to innovation in glycosciences is shown with chapters covering highly functionalized exo-glycals for the generation of molecular diversity in a chemoselective manner, imino sugar glycosidase inhibitors, carbasugars, multivalent glycoconjugates, including glycodendrimers, glyconanotubes, and glyconanoparticles, and their uses in medicinal chemistry, as well as artificial saccharide-based and saccharide-functionalized gene delivery systems. Siderophores based on monosaccharides (which have proven effective for Gram-negative bacteria and mycobacteria), and the so-called smart materials, (which can modulate and control cell behaviour), complete the volume. Volume 39 of Carbohydrate Chemistry - Chemical and Biological Approaches contains contributions ranging from glycochemistry to glycobiology. This volume demonstrates in a meaningful way how the interdisciplinary approach of an international glyconetwork can advance the field of carbohydrate research in Europe and worldwide.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eSynthetic Lipoarabinomannans as Inhibitors of Mycobaterial Growth; Epoxy carbohydrate derivatives and analogues as useful intermediates in the synthesis of glycosidase inhibitors; Recent design in the inhibition of glycosyltransferases; Beta-N-Acetylhexosaminidases: Group-specific inhibitors wanted...; Structure Determination of Lectins by X-ray Crystallography; Glycation: from molecules to life; Radical-mediated brominations at ring positions of carbohydrates - 35 years later; Glycosidases and diabetes type II: mode of action and therapeutic perspectives; Recent Advances in Enzymatic Synthesis of Heparin; Decoration of bacterial capsular polysaccharide. Their importance for vaccine development; Positive Attitude, Shape, Flexibility, Added-Value Accessoires or “Just Being Different”: How to Attract a Glycosidase; Surface Binding Sites in Carbohydrate Active Enzymes.","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888119001431,"sku":"9781849735872","price":314.95,"currency_code":"GBP","in_stock":true}]},{"product_id":"quantitative-proteomics-9781849738088","title":"Quantitative Proteomics","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eAs a component of post-genome science, the field of proteomics has assumed great prominence in recent years. Whereas quantitative analyses focussed initially on relative quantification, a greater emphasis is now placed on absolute quantification and consideration of proteome dynamics. Coverage of the topic of quantitative proteomics requires consideration both of the analytical fundamentals of quantitative mass spectrometry and the specific demands of the problem being addressed.   Quantitative Proteomics aims to outline the state of the art in mass spectrometry-based quantitative proteomics, describing recent advances and current limitations in the instrumentation used, together with the various methods employed for generating high quality data. Details on both strategies describing how stable isotope labelling can be applied and methods for performing quantitative analysis of proteins in a label-free manner are given. The utility of these strategies to understanding cellular protein dynamics are then exemplified with chapters looking at spatial proteomics, dynamics of protein function as determined by quantifying changes in protein post-translational modification and protein turnover. Finally, a key application of these techniques to biomarker discovery and validation is presented, together with the rapidly developing area of quantitative analysis of protein-based foodstuffs.   This exemplary book is essential reading for analytical and biological mass spectrometrists working in proteomics research, as well as those undertaking either fundamental or clinical-based investigations with an interest in understanding protein dynamics and\/or biomarker assessment.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTrade Review\u003c\/h2\u003e\"Quantitative Proteomics should not be regarded only as an updated reference book of cutting-edge bottom-up strategies for  quantitative proteomics. Its  reading makes us reflect on   the  enormous experimental progress made possible by  the recent developments magnificently summarized in  the 15  chapters in  this new volume of  the series New Developments in Mass  Spectrometry.\" -- Juan J. Calvete * Journal of Proteomics, Volume 108, 2014, Pages 494-496 *\u003cbr\u003eBio-molecular cycles are to say the least exceedingly complex. Although many cycles have already been defined, relatively little is known about the macromolecular workhorses that are embedded in the cells that actually do the work. It is only in the last two decades, with major advances in instrumentation, that insights into these complex mechanisms have been possible. Analysing a moving target is difficult at any time. When that target is the determination of protein composition as a function of the cell cycle, its age and its response to extracellular stimuli, the process becomes one of taking a snapshot in time. By definition this monitors the quantitative changes taking place over time and mass spectrometry is one of very few techniques capable of achieving this objective. Even with this very powerful tool, a very careful selection of appropriate strategies is called for, and this book describes those that have achieved at least a degree of success. The greatest limitation is that quantitative proteomics relies on the use of peptide surrogates as read-outs for the actual protein amount. Such simulations are not always reliable, a major fact recognised and emphasised throughout all chapters. With this in mind the editors have assembled authors with the necessary knowledge combined with an ability to explain current practices whilst simultaneously stating the limitations. Most authors also propose new ideas and possible extensions that may well apply in the future.      The book is divided into a description of the technology (two chapters); label-based protein quantification (three chapters); label-free protein quantification (three chapters); dynamic protein quantification (four chapters); and application of quantitative proteomics (three chapters). The division between labelled and label-free quantification is most useful. It allows for a rapid comparison between methods and easier selection of the most appropriate method. The challenge in any method is to determine the absolute protein quantification at any given time and then reproduce it. At the forefront of current methods are HPLC and electrospray MS. As always with this technology, a major issue is how to identify the most appropriate sample preparation method, an issue recognised by most authors.      The most intriguing chapters are the last two. It is encouraging to see a chapter on blood plasma. The blood processing industry is a key to human survival, is a massively important industry, and yet receives relatively little publicity. It is in effect largely hidden from public view. Non-communicable diseases account for 60 % of the world’s fatalities, and yet many could be detected by biomarkers if the technology were available—and quantitative proteomics offers the promise of inexpensive automated procedures on the millions of samples of blood taken daily. Similarly, in the chapter on food, application of similar methods offers the prospect of determining allergies in food, the new plague of allergic reaction now suffered by some 30 % of the western populace.      It is regrettable that this book is unlikely to be read by those responsible for allocation of research funding. Development of the described technology holds significant promise in delivering automated methods capable of early detection and therefore easier and cheaper treatment of many diseases. -- K. Jones, Chromatographia * Chromatographia (2015) 78:141–142 *\u003cbr\u003e\"the editors have assembled authors with the necessary knowledge combined with an ability to explain current practices whilst simultaneously stating the limitations. Most authors also propose new ideas and possible extensions that may well apply in the future.\" -- K. Jones * Chromatographia (2015) 78:141–142 *\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePractical Considerations and Current Limitations in Quantitative Mass Spectrometry-Based Proteomics; Targeted Proteomics Based on High Resolution Accurate Mass Spectrometry Measurement; Making Sense Out of the Proteome: The Utility of iTRAQ and TMT; Getting Absolute: Determining Absolute Protein Quantities via Selected Reaction Monitoring Mass Spectrometry; Proteomics Standards with Controllable Trueness - Absolute Quantification of Peptides, Phosphopeptides and Proteins Using ICP- and ESI-MS Label-Free Strategies for Protein Quantification; Overview and Implementation of Mass Spectrometry-Based Label-Free Quantitative Proteomics; MS1 Label-Free Quantification Using Ion Intensity Chromatograms in Skyline (Research and Clinical Applications); Label-Free Quantification of Proteins Using Data-Independent Acquisition; Spatial Proteomics: Practical Considerations for Data Acquisition and Analysis in Protein Subcellular Localisation Studies; Quantitative Analyses of Phosphotyrosine Cellular Signalling in Disease; Next Generation Proteomics: PTMs in Space and Time; Experimental and Analytical Approaches to Quantification of Protein Turnover on a Proteome-Wide Scale; Protein Quantification by MRM for Biomarker Validation; MRM-based Protein Quantification with Labelled Standards for Biomarker Discovery, Verification, and Validation in Human Plasma; Mass Spectrometry-Based Quantification of Proteins and Peptides in Food; Subject Index","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":48888120607063,"sku":"9781849738088","price":156.75,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781849738088.jpg?v=1791478898"},{"product_id":"biochemistry-9780198833871","title":"Biochemistry","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eVery Short Introductions\u003cb\u003e: Brilliant, Sharp, Inspiring \u003c\/b\u003eFrom the simplest bacteria to humans, all living things are composed of cells of one type or another, all of which have fundamentally the same chemistry. This chemistry must provide mechanisms that allow cells to interact with the external world, a means to power the cell, machinery to carry out varied processes within the cell, a structure within which everything runs, and also governance through a web of interlocking chemical reactions. Biochemistry is the study of those reactions, the molecules that are created, manipulated, and destroyed as a result of them, and the massive macromolecules (such as DNA, cytoskeletons, proteins and carbohydrates) that form the chemical machinery and structures on which these biochemical reactions take place. It didn''t take long for an understanding of the chemistry of life to turn into a desire to manipulate it. Drugs and therapies all aim to modify biochemical processes for good or ill: Penicillin, derived from mould, stops bacteria making their cell walls. Aspirin, with its origins in willow bark, inhibits enzymes involved in inflammatory responses. A few nanograms of botulinum toxin (botox), can kill by preventing the release of neurotransmitters from the ends of nerves and so leads to paralysis and death, or give a wrinkle free forehead (if administered in very tiny quantities).This Very Short Introduction discusses the key concepts of biochemistry, as well as the historical figures in the field and the molecules they studied, before considering the current science and innovations in the field, and the interaction between biochemistry, biotechnology, and synthetic biology. ABOUT THE SERIES: The Very Short Introductions series from Oxford University Press contains hundreds of titles in almost every subject area. These pocket-sized books are the perfect way to get ahead in a new subject quickly. Our expert authors combine facts, analysis, perspective, new ideas, and enthusiasm to make interesting and challenging topics highly readable.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePreface 1: The roots of biochemistry 2: Water, lipids and carbohydrates 3: Proteins: Nature's nano-machines 4: Nucleic acids: Life's blueprints 5: Powering a cell: Bioenergetics 6: Manufacturing and maintaining DNA 7: Following biochemistry within the cell 8: Biotechnology and synthetic biology Further reading References\u003c\/b\u003e","brand":"Oxford University Press","offers":[{"title":"Default Title","offer_id":49083400356183,"sku":"9780198833871","price":9.49,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9780198833871.jpg?v=1725548820"},{"product_id":"drug-transporters-volume-1-role-and-importance-in-adme-and-drug-development-9781782620693","title":"Drug Transporters: Volume 1: Role and Importance","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eUnderstanding and quantifying the effects of membrane transporters within the human body is essential for modulating drug safety and drug efficacy. In this first volume on Drug Transporters, the current knowledge and techniques in the transporter sciences and their relations to drug metabolism and pharmacokinetics are comprehensively reviewed. The second volume of the book is specifically dedicated to emerging science and technologies, highlighting potential areas for future advances within the drug transporter field.   The topics covered in both volumes ensure that all relevant aspects of transporters are described across the drug development process, from in silico models and preclinical tools through to the potential impact of transporters in the clinic. Contributions are included from expert leaders in the field, at-the-bench industrial scientists, renowned academics and international regulators. Case studies and emerging developments are highlighted, together with the merits and limitations of the available methods and tools, and extensive references to reviews on specific in-depth topics are also included for those wishing to pursue their knowledge further.    As such, this text serves as an essential handbook of information for postgraduate students, academics, industrial scientists and regulators who wish to understand the role of transporters in absorption, distribution, metabolism, and excretion processes. In addition, it is also a useful reference tool on the models and calculations necessary to predict their effect on human pharmacokinetics and pharmacodynamics.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eOverview of drug transporter families and their role in drug development; Liver transporters and their involvement in the hepatocellular uptake and export systems of organic anions; Intestinal transporters; Kidney transporters; CNS transporters; Lung transporters; The use of in vitro and in silico systems for investigating transporter interactions; The use of transgenic and knockout in vivo systems for investigating transporter interactions; Modelling and simulation of transporter interactions; Clinical Drug-Drug Interactions: An industrial Pharmaceutical Perspective; Regulatory requirements,  Labelling and Drug Transporters; Recent Advances and Emerging Technologies; Bioinformatics; Regulation of transporters; Transporter Pharmacogenomics; Transporter Imaging; Transporters and Proteomics","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":49084339749207,"sku":"9781782620693","price":170.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782620693.jpg?v=1791476895"},{"product_id":"allosterism-in-drug-discovery-9781782624592","title":"Allosterism in Drug Discovery","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eAlthough the concept of allosterism has been known for over half a century, its application in drug discovery has exploded in recent years. The emergence of novel technologies that enable molecular-level ligand-receptor interactions to be studied in studied in unprecedented detail has driven this trend. This book, written by the leaders in this young research area, describes the latest developments in allosterism for drug discovery.   Bringing together research in a diverse range of scientific disciplines, Allosterism in Drug Discovery is a key reference for academics and industrialists interested in understanding allosteric interactions. The book provides an in-depth review of research using small molecules as chemical probes and drug candidates that interact allosterically with proteins of relevance to life sciences and human disease. Knowledge of these interactions can then be applied in the discovery of the novel therapeutics of the future.   This book will be useful for people working in all disciplines associated with drug discovery in academia or industry, as well as postgraduate students who may be working in the design of allosteric modulators.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eModulation of Biological Targets: Why Use Allosteric Ligands?; Identifying and Quantifying Allosteric Drug Function; Targeting Catalytic and Non-catalytic Functions of Protein Kinases; Molecular Biology Techniques Applied to GPCR Allosteric and Biased Ligands; Examining Allosterism in a Dimeric GPCR Context; A Unifying Approach to the Duality of \"Energetic\" Versus \"Conformational\" Formulations of Allosteric Coupling: Mechanistic Implications on GPCR Allostery; mGluR2 Positive Allosteric Modulators; Muscarinic Receptors Allosteric Modulation; Positive Allosteric Modulators of Opioid Receptors; mGluR7 allostery: up and down modulation; Allosteric Modulators of Adenosine, P2Y and P2X Receptors; Positive Allosteric Modulators of G Protein-Coupled Receptors that Act via Covalent Mechanisms of Action; mGluR4 PET ligands as enablers of target biology understanding; Mechanism of action of a GluN2C- and GluN2D-selective NMDA receptor positive allosteric modulator; Development of AMPA Receptor Modulators as Cognition Enhancers; Allosteric modulation of the neuronal nicotinic acetylcholine receptor; Allosteric Binding in the Serotonin Transporter – Pharmacology, Structure, Function and Potential Use as a Novel Drug Target; Allosteric Inhibition of Abl Kinase; Allosteric Modulators of Heat Shock Protein 90 (HSP90); A look forward;","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":49084340797783,"sku":"9781782624592","price":170.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782624592.jpg?v=1791476901"},{"product_id":"carbohydrate-chemistry-volume-42-9781782625384","title":"Carbohydrate Chemistry: Volume 42","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eWith the increase in volume, velocity and variety of information, researchers can find it difficult to keep up to date with the literature in their field. This invaluable volume contains analysed, evaluated and distilled information on the latest in carbohydrate research. The discovery and synthesis of novel carbohydrates and mimetics with diverse applications continues to be a major challenge for carbohydrate chemists. The understanding of the structure and function of carbohydrates and glycoconjugates remains vital in medicine and molecular biology.   This volume collates modern carbohydrate research from theory to application and demonstrates the importance of carbohydrates in new lead generation. It is of benefit to any researcher who wishes to learn about the latest developments in the carbohydrate field.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eContemporary glycoconjugation chemistry; Advances in applications of NMR methods to uncover the conformation and recognition features of glycans; Recent advances in Kdo-glycoside synthesis; Predictable and highly efficient preparation of carbohydrate-based vaccines: Squaric acid chemistry is the way to go; Synthetic Approaches to Cyclodextrins and Their Analogues; Bacterial lipopolysaccharides covalently bound to hopanoids: key molecules that favour the life of Bradyrhizobia in stressful environments; Giant dsDNA viruses taste for sugars; Glycosteroids: a specific type of glycolipids with self assembly properties; Recent examples of novel synthetic approaches to diverse amino-sugars; FimH Antagonists – Solubility vs. Oral Availability; Ferrier rearrangement. An update on recent developments; Recent advances in the synthesis of iminosugars. An insight into the cascade addition of Grignard reagents to halonitriles\/cyclization;","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":49084340830551,"sku":"9781782625384","price":314.95,"currency_code":"GBP","in_stock":true}]},{"product_id":"molybdenum-and-tungsten-enzymes-bioinorganic-chemistry-9781782628774","title":"Molybdenum and Tungsten Enzymes: Bioinorganic","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThere has been enormous progress in our understanding of molybdenum and tungsten enzymes and relevant inorganic complexes of molybdenum and tungsten over the past twenty years. This set of three books provides a timely and comprehensive overview of the field and documents the latest research.    Building on the first volume that focussed on biochemistry aspects, the second volume in the set focusses on the inorganic complexes that model the structures and reactivity of the active sites of each major group of molybdenum and tungsten enzymes. Special attention is given to synthetic strategies, reaction mechanism and chemical kinetics of these systems. The introductory chapter provides a useful overview and places the topic of the book into a wider context.    This text will be a valuable reference to workers both inside and outside the field, including graduate students and young investigators interested in developing new research programs in this area.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003ePart I Molybdenum- and tungsten-containing enzymes; Abundance, ubiquity, and evolution of molybdoenzymes; Molybdenum cofactor biosynthesis; Bacterial molybdoenzymes; The prokaryotic Mo\/W-bisPGD enzyme family; Enzymes of the xanthine oxidase family; The sulfite oxidase family of Mo enzymes; Nitrogenase; Tungsten-containing enzymes; Part II Introduction and overview of synthetic Mo and W chemistry; Synthesis of mono- and bisdithiolene Mo and W model compounds; Pterin‐inspired Model Compounds of Molybdenum Enzymes; Synthesis of models for the xanthine oxidase family of enzymes; Electron transfer mechanisms in Mo and W compounds; Comparative kinetics of enzymes and models; Models of the metal clusters of nitrogenase; Part III Overview of spectroscopic and electronic studies of Mo and W enzymes; Spectroscopic and electronic structure studies of Mo model compounds and enzymes; Electron paramagnetic resonance studies of molybdenum enzymes; X-ray absorption spectroscopic studies of molybdenum enzymes; Electrochemistry of molybdenum and tungsten enzymes; Computational studies of molybdenum and tungsten enzymes; Nitrogen Fixation in Nitrogenase and Related Small-Molecule Models","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":49084341387607,"sku":"9781782628774","price":151.05,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781782628774.jpg?v=1791476907"},{"product_id":"venoms-to-drugs-venom-as-a-source-for-the-development-of-human-therapeutics-9781849736633","title":"Venoms to Drugs: Venom as a Source for the","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThe pharmaceutical industry has become increasingly interested in biologics from animal venoms as a potential source for therapeutic agents in recent years, with a particularly emphasis on peptides. To date six drugs derived from venom peptides or proteins have been approved by the FDA, with nine further agents currently being investigated in clinical trials. In addition to these drugs in approved or advanced stages of development, many more peptides and proteins are being studied in varying stages of preclinical development. This unique book provides an up to date and comprehensive account of the potential of peptides and proteins from animal venoms as possible therapeutics. Topics covered include chemistry and structural biology of animal venoms, proteomic and transcriptomic approaches to drug discovery, bioassays, high-throughput screens and target identification, and reptile, scorpion, spider and cone snail venoms as a platform for drug development. Case studies are used to illustrate methods and successes and highlight issues surrounding administration and other important lessons that have been learnt from the development of approved therapeutics based on venoms. The first text to focus on this fascinating area and bridging an important gap, this book provides the reader with essential and current knowledge on this fast-developing area. Venoms to Drugs will find wide readership with researchers working in academia and industry working in all medicinal and pharmaceutical areas.\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTrade Review\u003c\/h2\u003eBelonging to the RSC’s Drug Discovery series, Venoms to Drugs is a welcome addition to the bookshelf designed to guide the reader through the opportunities and challenges to be found in Nature’s treasure chest in the efforts to develop new therapeutic solutions to human maladies. Venoms have evolved to assist numerous animals with matters of defence or in catching prey—if you’ve been stung by a bee you’ll have felt the power of a venom at work—and here we explore a little-tapped natural resource which could help provide the chemical foundations for the next big painkiller, antihypertensive or anti-inflammatory. Turning venom, consisting of a cocktail of toxins, from a potentially deadly secretion into a relatively safe, efficacious medicine is not  simple. This book does not shy away from this fact, but embraces the problems and examines methods afforded by recent  scientific advances through which the many challenges may be overcome. The book begins by introducing the drug-development opportunities provided by these natural resources, with an overview of the evolution of venoms across species and how many venom toxins retain a similar basic template upon which to pin their more specific functional flourishes for various targets and effects. We are given a detailed introduction to the obstacles met when turning these natural products into medicines, from the problems of retaining functionality to producing stable formulations. What stands out here in particular is that there are groups of animals whose venoms remain completely unexplored in terms of their therapeutic potential, and thus the scene is set for the rest  of the book. The structure of the book is logical and the contents detailed, well-written and informative throughout. Chapters on approaches to drug discovery, taking into account advantages provided by recent technological advances, are followed by an examination of venoms as lead compounds from various animal orders in four further chapters. Later on, Chapters 9 and 10 describe the development of analgesic drugs and anti-inflammatory\/autoimmune compounds from some extraordinary sea creatures, demonstrating good examples of the possibilities that may be found. The technical detail in the writing has not been lost or brushed over, which makes the book all-the-better as a useful resource. One aspect that is particularly good is the inclusion of case studies, to demonstrate how a carefully nurtured project can bear fruit. As always, there are chemical puzzles to solve, pharmacological mechanisms to pick apart and regulatory hurdles to jump, but from deadly cone-snail venom used to paralyse its prey comes the analgesic ziconatide, and from pit viper venom comes the ACE inhibitor captopril—one wonders what next might be found from a jellyfish’s tentacles or a spider’s jaws. If there is a sting in the tail in this particular story, then it is certainly to be extracted, analysed and put to good use! This book is, of course, targeted towards chemists as is clear from the detail and style throughout, but others with an interest in this subject (pharmacologists, electrophysiologists, formulation scientists and their kin) will certainly find this a useful, interesting and perhaps even thought-provoking resource to have at hand. -- Neil C. Henny, Liverpool John Moores University * Chromatographia (2015) 78:1507-1508 *\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eVenomous animals: evolution and ecology; Chemistry and structural biology of animal venoms; Venoms-based drug discovery: proteomic and transcriptomic approaches; Venoms-based drug discovery: bioassays, high-throughput screens, and target identification; Reptile venoms as a platform for drug development; Cone snail venoms as a platform for drug development; Scorpion venoms as a platform for drug development; Spider-venom peptides as a platform for drug development; Case study 1: development of the analgesic drugs Prialt® and Xen2174; Case study 2: development of exenatide for treatment of type 2 diabetes; Case study 3: development of ShK for the treatment of autoimmune diseases; Development of venom natriuretic peptides for treating congestive heart failure; Engineering venom peptides to improve their stability and bioavailability; Manufacturing of venom-derived therapeutic peptides; Venoms to drugs: prospects and pitfalls","brand":"Royal Society of Chemistry","offers":[{"title":"Default Title","offer_id":49084554871127,"sku":"9781849736633","price":160.55,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781849736633.jpg?v=1791478896"},{"product_id":"genomic-and-epigenomic-biomarkers-of-toxicology-and-disease-9781119807674","title":"Genomic and Epigenomic Biomarkers of Toxicology","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eGenomic and Epigenomic Biomarkers of Toxicology and Disease\u003c\/b\u003e \u003cp\u003e\u003cb\u003eThe latest developments in biomarker research applicable to toxicology and medicine\u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eResearch on genomic and epigenomic biomarkers is developing rapidly with cutting-edge studies scattered throughout the academic literature, making the status of ongoing scientific activity in this area difficult to ascertain.  \u003c\/p\u003e\u003cp\u003e\u003ci\u003eGenomic and Epigenomic Biomarkers of Toxicology and Disease: Clinical and Therapeutic Actions\u003c\/i\u003e delivers a comprehensive and authoritative compilation of up-to-date developments in the application of genomic and epigenomic biomarkers to toxicology, disease prevention, cancer detection, therapeutics, gene therapy, and other areas. With contributions from a collection of internationally recognized investigators, this edited volume offers unique insights into current trends and future directions of research in the discussed areas.  \u003c\/p\u003e\u003cp\u003e Combining state-of-the-art information on genomic and epigenom\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e\u003cp\u003eDedication ix\u003c\/p\u003e \u003cp\u003ePreface xi\u003c\/p\u003e \u003cp\u003eAcknowledgements xiii\u003c\/p\u003e \u003cp\u003eList of Contributors xv\u003c\/p\u003e \u003cp\u003e1 Genomic and Epigenomic Biomarkers for Predictive Toxicity and Disease 1\u003cbr\u003e \u003ci\u003eSaura C. Sahu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2 MicroRNAs as Non-invasive Biomarkers of Toxicity and Chemical Hazard: Genomic and Epigenomic Biomarkers of Toxicology and Disease 7\u003cbr\u003e \u003ci\u003eGail M. Nelson and Brian N. Chorley\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3 EV (Extracellular Vesicle)-associated miRNAs as Biomarkers of Toxicity 37\u003cbr\u003e \u003ci\u003eRyuichi Ono, Yusuke Yoshioka, Yusuke Furukawa, Mie Naruse, Makiko Kuwagata, Takahiro Ochiya, Satoshi Kitajima, and Yoko Hirabayashi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4 Circulating miRNAs as Biomarkers of Toxic Heavy Metal Exposure 63\u003cbr\u003e \u003ci\u003eAlexandra N. Nail, Ana P. Ferragut Cardoso, Mayukh Banerjee, and J. Christopher States\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5 MicroRNA Biomarkers of Malignant Mesothelioma 89\u003cbr\u003e \u003ci\u003eLijin Zhu, Fangfang Zhang, Min Zhang, Hailing Xia, Xiuyuan Yuan, and Yanan Gao\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6 Role of Non-coding RNAs in Innate Immune Responses Perturbed by Environmental Arsenic Exposure 101\u003cbr\u003e \u003ci\u003eLiz Saavedra Perez and Benjamin L. King\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7 Transcriptomics: Applications in Toxicology and Medicine 133\u003cbr\u003e \u003ci\u003ePius Joseph Copyrighted Material\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8 Network Biology for Biomarker Discovery and Therapy in Cancer 163\u003cbr\u003e \u003ci\u003eAsim Bikas Das\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9 Epigenetic Biomarkers: Link to Maternal Exposure and Offspring Health Outcomes 185\u003cbr\u003e \u003ci\u003eJairus Pulczinski, Moira Mccormick, Yuchen Sun, Musa Watfa, Robert YS Cheng, and Wan-Yee Tang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10 The Role of Dynamic Epigenetic Changes in Modulating Homeostasis after Exposure to Low-dose Environmental Chemicals 213\u003cbr\u003e \u003ci\u003eChongli Yuan, Jennifer L. Freeman, Junkai Xie, and Han Zhao\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11 Emerging Non-invasive Molecular Biomarkers for Early Cancer Detection 229\u003cbr\u003e \u003ci\u003eJacob Sobota, Yingxue Zhang, Eid Alshammari,and Zhe Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12 Aberrant DNA Methylation of Tumor Suppressor Genes and Oncogenes as Cancer Biomarkers 251\u003cbr\u003e \u003ci\u003eEid Alshammari, Yingxue Zhang, Jacob Sobota, and Zhe Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13 SMYD Protein Family as Promising Biomarkers for Cancer Diagnosis and Prognosis 273\u003cbr\u003e \u003ci\u003eYingxue Zhang, Eid Alshammari, Jacob Sobota, and Zhe Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14 Toward Precision Medicine: Epigenetic Alterations in Human Melanoma 309\u003cbr\u003e \u003ci\u003eCarmen Elena Condrat, Elena Codruta Dobrica, Sanda Maria Cretoiu, and Dragos Cretoiu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15 Currents Trends and Future Perspectives in Our Epigenetic Signatures: What a Diet Can Trigger 333\u003cbr\u003e \u003ci\u003eElena-Codruța Dobrică, Mihnea-Alexandru Găman, Matei-Alexandru Cozma, and Sanda Maria Cretoiu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16 Genetic and Epigenetic Biomarkers of Organophosphate Compounds, Dialkyl Phosphate Exposure, and Their Relation to Biological Effects 363\u003cbr\u003e \u003ci\u003eDavid S. Hernández-Toledano and Libia Vega\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17 Genetic, Epigenetic, and Anatomical Factors in Agenesis and Development of Female Reproductive Tract 383\u003cbr\u003e \u003ci\u003eTadaaki Nakajima, Tomomi Sato, and Taisen Iguchi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18 Cause or Consequence: Epigenomic DNA Methylation Changes in Arsenic- Mediated in Vitro Transformation of Human Prostate Cells 395\u003cbr\u003e \u003ci\u003eB. Alex Merrick, Dhiral P. Phadke, Ruchir R. Shah, Deepak Mav, and Erik J. Tokar\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19 Epigenetic Regulation of Sex Determination and Toxicity in Nonmammalian Vertebrates 415\u003cbr\u003e \u003ci\u003eGenki Yamagishi, Taisen Iguchi, and Shinichi Miyagawa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20 Characterization of Genomic and Epigenomic Biomarkers of Nanoparticle Toxicity Using the Zebrafish Model System 449\u003cbr\u003e \u003ci\u003eAthira Sairanthry Suku, Parayanthala Valappil Mohanan, and Jennifer L. Freeman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIndex 477\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49371826717015,"sku":"9781119807674","price":153.0,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119807674.jpg?v=1730154714"},{"product_id":"advanced-chemical-biology-chemical-dissection-and-reprogramming-of-biological-systems-9783527347339","title":"Advanced Chemical Biology: Chemical Dissection","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eAdvanced Chemical Biology\u003c\/b\u003e \u003cp\u003e\u003cb\u003eThe modern approach to teaching chemical biology\u003c\/b\u003e \u003c\/p\u003e\u003cp\u003e\u003ci\u003eAdvanced Chemical Biology\u003c\/i\u003e is organized around the central dogma of life, progressing from genes to proteins and higher-order cellular structures, including core application areas such as imaging, chemical genetics, activity-based protein profiling, and natural product discovery and biosynthesis. Advanced topics and applications in, e. g., microbiology, developmental biology, and neurobiology, are covered in separate sections.  \u003c\/p\u003e\u003cp\u003e\tEvery chapter is homogeneous in style and layout, consisting of a short historical introduction followed by a description of the underlying concepts and a selection of recent examples of how the concept has been turned into practice. The subdivision of the contents into core and supplemental chapters enables a flexible use in teaching, both for a one-semester and a two-semester course. \u003c\/p\u003e\u003cp\u003e\tWritten by authors and editors coming from the leading scientific institutions that have developed the concepts and technologies for this discipline, \u003ci\u003eAdvanced Chemical Biology\u003c\/i\u003e includes specific information on topics like: \u003c\/p\u003e\u003cul\u003e\n\u003cli\u003eDNA function, synthesis and engineering, chemical approaches to genome integrity, and RNA function, synthesis, and probing\u003c\/li\u003e\n\u003cli\u003eChemical approaches to transcription and RNA regulation in vivo, chemical biology of genome engineering, and peptide\/protein synthesis and engineering\u003c\/li\u003e\n\u003cli\u003eDirected evolution for chemical biology, chemical biology of cellular metabolism, chemical biology of lipids, and protein post-translational modifications\u003c\/li\u003e\n\u003cli\u003eChemical glycobiology, chemical and enzymatic modification of proteins, genetic code expansion, bio-orthogonal chemistry, and cellular imaging\u003c\/li\u003e\n\u003c\/ul\u003e \u003cp\u003eWith its broad scope and focus on turning concepts into applications, \u003ci\u003eAdvanced Chemical Biology\u003c\/i\u003e is an excellent starting point for anyone entering the field and looking for a guide to the wide range of available methods and strategies that chemical biology has to offer. \u003c\/p\u003e\u003cp\u003e\u003cb\u003eWith a Foreword by Nobel Laureate Carolyn Bertozzi.\u003c\/b\u003e\u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTrade Review\u003c\/h2\u003eInteressante Richtung des Lehrbuches, stärker aus chemischer Perspektive betrachtet. Erweitert dadurch den Blickwinkel aufs Fach gerade für Wissenschaftler die stärker aus der biologischen Richtung kommen.\u003cbr\u003e Prof. Dr. David Kostner, Hochschule München,  Biotechnologie (11\/2023)\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003eCORE TOPICS\u003cbr\u003e Introduction\u003cbr\u003e DNA function, synthesis and engineering\u003cbr\u003e Chemical approaches to genome integrity and engineering\u003cbr\u003e RNA function, synthesis and engineering\u003cbr\u003e Chemical approaches to transcription and RNA regulation in vivo\u003cbr\u003e Peptide synthesis and engineering\u003cbr\u003e Protein engineering and semisynthesis\u003cbr\u003e Biomolecular structure determination\u003cbr\u003e Biomolecular structure prediction and design\u003cbr\u003e Directed Evolution\u003cbr\u003e Cellular metabolism\u003cbr\u003e Membrane biology and lipid signaling\u003cbr\u003e Posttranslational modifications\u003cbr\u003e Chemical glycobiology\u003cbr\u003e Bioconjugation\u003cbr\u003e Genetic code expansion\u003cbr\u003e Bioorthogonal chemistry\u003cbr\u003e Cellular imaging\u003cbr\u003e In vivo imaging\u003cbr\u003e Natural product biosynthesis\u003cbr\u003e Natural product discovery\u003cbr\u003e Activity-based protein profiling\u003cbr\u003e Chemical genetics\u003cbr\u003e Development of small molecule probes and therapeutics\u003cbr\u003e SUPPLEMENTAL TOPICS\u003cbr\u003e Metals in biology\u003cbr\u003e Chemical redox-biology\u003cbr\u003e Chemical microbiology\u003cbr\u003e Chemical mammalian cell biology\u003cbr\u003e Chemical developmental biology\u003cbr\u003e Chemical immunology\u003cbr\u003e Chemical neurobiology\u003cbr\u003e Chemical plant biology\u003cbr\u003e Chemical virology\u003cbr\u003e Chemical parasitology","brand":"Wiley-VCH Verlag GmbH","offers":[{"title":"Default Title","offer_id":49372701819223,"sku":"9783527347339","price":90.0,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9783527347339.jpg?v=1730163868"},{"product_id":"riboregulator-design-and-analysis-9781071624203","title":"Riboregulator Design and Analysis","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eThis collection explores the latest advances in riboregulators, such as RNA-only systems and ribonucleoprotein systems, and provides detailed techniques to study, evolve, and design them. Beginning with a set of chapters focused on the design and application of small RNA (sRNA) regulator systems, the book continues with sections on techniques to create switchable riboregulator systems known as riboswitches, technologies that leverage RNA-guided CRISPR-Cas systems to edit the epigenome, control gene expression, and create diagnostics, as well as computational and experimental techniques to investigate the sequence-structure-function relationship of RNA systems that can both advance fundamental understanding and rational design of riboregulators. Written for the highly successful \u003ci\u003eMethods in Molecular Biology\u003c\/i\u003e series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e\u003cp\u003e\u003cb\u003e1. RNP-Based Control Systems for Genetic Circuits in Synthetic Biology Beyond CRISPR\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Trevor. R Simmons, Andrew D. Ellington, and Lydia M. Contreras\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e2. Computational Design of RNA Toehold-Mediated Translation Activators\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Kaiyue Wu, Zhaoqing Yan, and Alexander A. Green\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e3. Design of RNA-Based Translational Repressors\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Seongho Hong, Dongwon Park, Soma Chaudhary, Griffin McCutcheon, Alexander A. Green, and Jongmin Kim\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e4. Design of Ribocomputing Devices for Complex Cellular Logic\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Griffin McCutcheon, Soma Chaudhary, Seongho Hong, Dongwon Park, Jongmin Kim, and Alexander A. Green\u003c\/p\u003e   \u003cp\u003e\u003c\/p\u003e  \u003cp\u003e\u003cb\u003e5. Computational Design of Small Transcription Activating RNAs (STARs)\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Baiyang Liu and James Chappell\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e6. Design and Assembly of Multi-Level Transcriptional and Translational Regulators for Stringent Control of Gene Expression\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            F. Veronica Greco, Thea Irvine, Claire S. Grierson, and Thomas E. Gorochowski\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e7. Model-Based Design of Synthetic Antisense RNA for Predictable Gene Repression\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Tae Seok Moon\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e8. Design of a Toolbox of RNA Thermometers\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Shaunak Sen, Abhilash Patel, and Krishan Kumar Gola\u003c\/p\u003e   \u003cp\u003e\u003c\/p\u003e  \u003cp\u003e\u003cb\u003e9. Development of Synthetic Riboswitches to Guide the Evolution of Metabolite Production in Microorganisms\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Minsun Kim, Sungho Jang, and Gyoo Yeol Jung\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e10. \u003c\/b\u003e\u003cb\u003eEfficient Method to Identify Synthetic Riboswitches Using RNA-Based Capture-SELEX Combined with In Vivo Screening\u003c\/b\u003e\u003c\/p\u003e              Janice Kramat and Beatrix Suess\u003cp\u003e\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e11. RNA Design Principles for Riboswitches that Regulate RNase P-Mediated tRNA Processing\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Anna Ender, Peter Stadler, Mario Mörl, and Sven Findeiß\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e12. Design, Characterization, and Application of Targeted Gene Activation in Bacteria Using a Modular CRISPRa System\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Maria Claudia Villegas Kcam and James Chappell\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e13. Reprogramming TracrRNAs for In Vitro RNA Detection and In Vivo Transcriptional Recording\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Chunlei Jiao and Chase L. Beisel\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e14. Harnessing CRISPR-Cas9 for Epigenetic Engineering\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Rosa S. Guerra-Resendez and Isaac B. Hilton\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e15. RNA Structure Prediction, Analysis, and Design: An Introduction to Web-Based Tools\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Raphael Angelo I. Zambrano, Carmen Hernandez-Perez, and Melissa K. Takahashi\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cb\u003e16. Single-Molecule FRET Studies of RNA Structural Rearrangements and RNA-RNA Interactions\u003c\/b\u003e\u003cp\u003e\u003c\/p\u003e  \u003cp\u003e            Ewelina M. Małecka, Boyang Hua, and Sarah A. Woodson\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e\u003cb\u003e17. Cotranscriptional RNA Chemical Probing\u003c\/b\u003e\u003c\/p\u003e  \u003cp\u003e            Courtney E. Szyjka and Eric J. Strobel\u003c\/p\u003e","brand":"Springer-Verlag New York Inc.","offers":[{"title":"Default Title","offer_id":49406772379991,"sku":"9781071624203","price":999.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781071624203.jpg?v=1730497057"},{"product_id":"multiblock-data-fusion-in-statistics-and-machine-learning-9781119600961","title":"Multiblock Data Fusion in Statistics and Machine","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eMultiblock Data Fusion in Statistics and Machine Learning\u003c\/b\u003e \u003cp\u003e\u003cb\u003eExplore the advantages and shortcomings of various forms of multiblock analysis, and the relationships between them, with this expert guide \u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eArising out of fusion problems that exist in a variety of fields in the natural and life sciences, the methods available to fuse multiple data sets have expanded dramatically in recent years. Older methods, rooted in psychometrics and chemometrics, also exist.  \u003c\/p\u003e\u003cp\u003e\u003ci\u003eMultiblock Data Fusion in Statistics and Machine Learning: Applications in the Natural and Life Sciences\u003c\/i\u003e is a detailed overview of all relevant multiblock data analysis methods for fusing multiple data sets. It focuses on methods based on components and latent variables, including both well-known and lesser-known methods with potential applications in different types of problems.  \u003c\/p\u003e\u003cp\u003e Many of the included methods are illustrated by practical examples and are accompanied by a freely available R-package. T\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e\u003cp\u003eForeword xiii\u003c\/p\u003e \u003cp\u003ePreface xv\u003c\/p\u003e \u003cp\u003eList of Figures xvii\u003c\/p\u003e \u003cp\u003eList of Tables xxxi\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart I Introductory Concepts and Theory 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction 3\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1.1 Scope of the Book 3\u003c\/p\u003e \u003cp\u003e1.2 Potential Audience 4\u003c\/p\u003e \u003cp\u003e1.3 Types of Data and Analyses 5\u003c\/p\u003e \u003cp\u003e1.3.1 Supervised and Unsupervised Analyses 5\u003c\/p\u003e \u003cp\u003e1.3.2 High-, Mid- and Low-level Fusion 5\u003c\/p\u003e \u003cp\u003e1.3.3 Dimension Reduction 7\u003c\/p\u003e \u003cp\u003e1.3.4 Indirect Versus Direct Data 8\u003c\/p\u003e \u003cp\u003e1.3.5 Heterogeneous Fusion 8\u003c\/p\u003e \u003cp\u003e1.4 Examples 8\u003c\/p\u003e \u003cp\u003e1.4.1 Metabolomics 8\u003c\/p\u003e \u003cp\u003e1.4.2 Genomics 11\u003c\/p\u003e \u003cp\u003e1.4.3 Systems Biology 13\u003c\/p\u003e \u003cp\u003e1.4.4 Chemistry 13\u003c\/p\u003e \u003cp\u003e1.4.5 Sensory Science 15\u003c\/p\u003e \u003cp\u003e1.5 Goals of Analyses 16\u003c\/p\u003e \u003cp\u003e1.6 Some History 17\u003c\/p\u003e \u003cp\u003e1.7 Fundamental Choices 17\u003c\/p\u003e \u003cp\u003e1.8 Common and Distinct Components 19\u003c\/p\u003e \u003cp\u003e1.9 Overview and Links 20\u003c\/p\u003e \u003cp\u003e1.10 Notation and Terminology 21\u003c\/p\u003e \u003cp\u003e1.11 Abbreviations 22\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Basic Theory and Concepts 25\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e2.i General Introduction 25\u003c\/p\u003e \u003cp\u003e2.1 Component Models 25\u003c\/p\u003e \u003cp\u003e2.1.1 General Idea of Component Models 25\u003c\/p\u003e \u003cp\u003e2.1.2 Principal Component Analysis 26\u003c\/p\u003e \u003cp\u003e2.1.3 Sparse PCA 30\u003c\/p\u003e \u003cp\u003e2.1.4 Principal Component Regression 31\u003c\/p\u003e \u003cp\u003e2.1.5 Partial Least Squares 32\u003c\/p\u003e \u003cp\u003e2.1.6 Sparse PLS 36\u003c\/p\u003e \u003cp\u003e2.1.7 Principal Covariates Regression 37\u003c\/p\u003e \u003cp\u003e2.1.8 Redundancy Analysis 38\u003c\/p\u003e \u003cp\u003e2.1.9 Comparing PLS, PCovR and RDA 38\u003c\/p\u003e \u003cp\u003e2.1.10 Generalised Canonical Correlation Analysis 38\u003c\/p\u003e \u003cp\u003e2.1.11 Simultaneous Component Analysis 39\u003c\/p\u003e \u003cp\u003e2.2 Properties of Data 39\u003c\/p\u003e \u003cp\u003e2.2.1 Data Theory 39\u003c\/p\u003e \u003cp\u003e2.2.2 Scale-types 42\u003c\/p\u003e \u003cp\u003e2.3 Estimation Methods 44\u003c\/p\u003e \u003cp\u003e2.3.1 Least-squares Estimation 44\u003c\/p\u003e \u003cp\u003e2.3.2 Maximum-likelihood Estimation 45\u003c\/p\u003e \u003cp\u003e2.3.3 Eigenvalue Decomposition-based Methods 47\u003c\/p\u003e \u003cp\u003e2.3.4 Covariance or Correlation-based Estimation Methods 47\u003c\/p\u003e \u003cp\u003e2.3.5 Sequential Versus Simultaneous Methods 48\u003c\/p\u003e \u003cp\u003e2.3.6 Homogeneous Versus Heterogeneous Fusion 50\u003c\/p\u003e \u003cp\u003e2.4 Within- and Between-block Variation 52\u003c\/p\u003e \u003cp\u003e2.4.1 Definition and Example 52\u003c\/p\u003e \u003cp\u003e2.4.2 MAXBET Solution 54\u003c\/p\u003e \u003cp\u003e2.4.3 MAXNEAR Solution 54\u003c\/p\u003e \u003cp\u003e2.4.4 PLS2 Solution 55\u003c\/p\u003e \u003cp\u003e2.4.5 CCA Solution 55\u003c\/p\u003e \u003cp\u003e2.4.6 Comparing the Solutions 56\u003c\/p\u003e \u003cp\u003e2.4.7 PLS, RDA and CCA Revisited 56\u003c\/p\u003e \u003cp\u003e2.5 Framework for Common and Distinct Components 60\u003c\/p\u003e \u003cp\u003e2.6 Preprocessing 63\u003c\/p\u003e \u003cp\u003e2.7 Validation 64\u003c\/p\u003e \u003cp\u003e2.7.1 Outliers 64\u003c\/p\u003e \u003cp\u003e2.7.1.1 Residuals 64\u003c\/p\u003e \u003cp\u003e2.7.1.2 Leverage 66\u003c\/p\u003e \u003cp\u003e2.7.2 Model Fit 67\u003c\/p\u003e \u003cp\u003e2.7.3 Bias-variance Trade-off 69\u003c\/p\u003e \u003cp\u003e2.7.4 Test Set Validation 70\u003c\/p\u003e \u003cp\u003e2.7.5 Cross-validation 72\u003c\/p\u003e \u003cp\u003e2.7.6 Permutation Testing 75\u003c\/p\u003e \u003cp\u003e2.7.7 Jackknife and Bootstrap 76\u003c\/p\u003e \u003cp\u003e2.7.8 Hyper-parameters and Penalties 77\u003c\/p\u003e \u003cp\u003e2.8 Appendix 78\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Structure of Multiblock Data 87\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e3.i General Introduction 87\u003c\/p\u003e \u003cp\u003e3.1 Taxonomy 87\u003c\/p\u003e \u003cp\u003e3.2 Skeleton of a Multiblock Data Set 87\u003c\/p\u003e \u003cp\u003e3.2.1 Shared Sample Mode 88\u003c\/p\u003e \u003cp\u003e3.2.2 Shared Variable Mode 88\u003c\/p\u003e \u003cp\u003e3.2.3 Shared Variable or Sample Mode 88\u003c\/p\u003e \u003cp\u003e3.2.4 Shared Variable and Sample Mode 89\u003c\/p\u003e \u003cp\u003e3.3 Topology of a Multiblock Data Set 90\u003c\/p\u003e \u003cp\u003e3.3.1 Unsupervised Analysis 90\u003c\/p\u003e \u003cp\u003e3.3.2 Supervised Analysis 93\u003c\/p\u003e \u003cp\u003e3.4 Linking Structures 95\u003c\/p\u003e \u003cp\u003e3.4.1 Linking Structure for Unsupervised Analysis 95\u003c\/p\u003e \u003cp\u003e3.4.2 Linking Structures for Supervised Analysis 96\u003c\/p\u003e \u003cp\u003e3.5 Summary 98\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Matrix Correlations 99\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e4.i General Introduction 99\u003c\/p\u003e \u003cp\u003e4.1 Definition 99\u003c\/p\u003e \u003cp\u003e4.2 Most Used Matrix Correlations 101\u003c\/p\u003e \u003cp\u003e4.2.1 Inner Product Correlation 101\u003c\/p\u003e \u003cp\u003e4.2.2 GCD coefficient 101\u003c\/p\u003e \u003cp\u003e4.2.3 RV-coefficient 102\u003c\/p\u003e \u003cp\u003e4.2.4 SMI-coefficient 102\u003c\/p\u003e \u003cp\u003e4.3 Generic Framework of Matrix Correlations 104\u003c\/p\u003e \u003cp\u003e4.4 Generalised Matrix Correlations 105\u003c\/p\u003e \u003cp\u003e4.4.1 Generalised RV-coefficient 105\u003c\/p\u003e \u003cp\u003e4.4.2 Generalised Association Coefficient 106\u003c\/p\u003e \u003cp\u003e4.5 Partial Matrix Correlations 108\u003c\/p\u003e \u003cp\u003e4.6 Conclusions and Recommendations 110\u003c\/p\u003e \u003cp\u003e4.7 Open Issues 111\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II Selected Methods for Unsupervised and Supervised Topologies 113\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Unsupervised Methods 115\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e5.i General Introduction 115\u003c\/p\u003e \u003cp\u003e5.ii Relations to the General Framework 115\u003c\/p\u003e \u003cp\u003e5.1 Shared Variable Mode 117\u003c\/p\u003e \u003cp\u003e5.1.1 Only Common Variation 117\u003c\/p\u003e \u003cp\u003e5.1.1.1 Simultaneous Component Analysis 117\u003c\/p\u003e \u003cp\u003e5.1.1.2 Clustering and SCA 123\u003c\/p\u003e \u003cp\u003e5.1.1.3 Multigroup Data Analysis 125\u003c\/p\u003e \u003cp\u003e5.1.2 Common, Local, and Distinct Variation 126\u003c\/p\u003e \u003cp\u003e5.1.2.1 Distinct and Common Components 127\u003c\/p\u003e \u003cp\u003e5.1.2.2 Multivariate Curve Resolution 130\u003c\/p\u003e \u003cp\u003e5.2 Shared Sample Mode 133\u003c\/p\u003e \u003cp\u003e5.2.1 Only Common Variation 133\u003c\/p\u003e \u003cp\u003e5.2.1.1 SUM-PCA 133\u003c\/p\u003e \u003cp\u003e5.2.1.2 Multiple Factor Analysis and STATIS 135\u003c\/p\u003e \u003cp\u003e5.2.1.3 Generalised Canonical Analysis 136\u003c\/p\u003e \u003cp\u003e5.2.1.4 Regularised Generalised Canonical Correlation Analysis 139\u003c\/p\u003e \u003cp\u003e5.2.1.5 Exponential Family SCA 140\u003c\/p\u003e \u003cp\u003e5.2.1.6 Optimal-scaling 143\u003c\/p\u003e \u003cp\u003e5.2.2 Common, Local, and Distinct Variation 146\u003c\/p\u003e \u003cp\u003e5.2.2.1 Joint and Individual Variation Explained 146\u003c\/p\u003e \u003cp\u003e5.2.2.2 Distinct and Common Components 147\u003c\/p\u003e \u003cp\u003e5.2.2.3 PCA-GCA 148\u003c\/p\u003e \u003cp\u003e5.2.2.4 Advanced Coupled Matrix and Tensor Factorisation 153\u003c\/p\u003e \u003cp\u003e5.2.2.5 Penalised-ESCA 156\u003c\/p\u003e \u003cp\u003e5.2.2.6 Multivariate Curve Resolution 158\u003c\/p\u003e \u003cp\u003e5.3 Generic Framework 159\u003c\/p\u003e \u003cp\u003e5.3.1 Framework for Simultaneous Unsupervised Methods 159\u003c\/p\u003e \u003cp\u003e5.3.1.1 Description of the Framework 159\u003c\/p\u003e \u003cp\u003e5.3.1.2 Framework Applied to Simultaneous Unsupervised Data Analysis Methods 161\u003c\/p\u003e \u003cp\u003e5.3.1.3 Framework of Common\/Distinct Applied to Simultaneous Unsupervised Multiblock Data Analysis Methods 161\u003c\/p\u003e \u003cp\u003e5.4 Conclusions and Recommendations 162\u003c\/p\u003e \u003cp\u003e5.5 Open Issues 164\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 ASCA and Extensions 167\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.i General Introduction 167\u003c\/p\u003e \u003cp\u003e6.ii Relations to the General Framework 167\u003c\/p\u003e \u003cp\u003e6.1 ANOVA-Simultaneous Component Analysis 168\u003c\/p\u003e \u003cp\u003e6.1.1 The ASCA Method 168\u003c\/p\u003e \u003cp\u003e6.1.2 Validation of ASCA 176\u003c\/p\u003e \u003cp\u003e6.1.2.1 Permutation Testing 176\u003c\/p\u003e \u003cp\u003e6.1.2.2 Back-projection 178\u003c\/p\u003e \u003cp\u003e6.1.2.3 Confidence Ellipsoids 178\u003c\/p\u003e \u003cp\u003e6.1.3 The ASCA+ and LiMM-PCA Methods 181\u003c\/p\u003e \u003cp\u003e6.2 Multilevel-SCA 182\u003c\/p\u003e \u003cp\u003e6.3 Penalised-ASCA 183\u003c\/p\u003e \u003cp\u003e6.4 Conclusions and Recommendations 185\u003c\/p\u003e \u003cp\u003e6.5 Open Issues 186\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Supervised Methods 187\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e7.i General Introduction 187\u003c\/p\u003e \u003cp\u003e7.ii Relations to the General Framework 187\u003c\/p\u003e \u003cp\u003e7.1 Multiblock Regression: General Perspectives 188\u003c\/p\u003e \u003cp\u003e7.1.1 Model and Assumptions 188\u003c\/p\u003e \u003cp\u003e7.1.2 Different Challenges and Aims 188\u003c\/p\u003e \u003cp\u003e7.2 Multiblock PLS Regression 190\u003c\/p\u003e \u003cp\u003e7.2.1 Standard Multiblock PLS Regression 190\u003c\/p\u003e \u003cp\u003e7.2.2 MB-PLS Used for Classification 194\u003c\/p\u003e \u003cp\u003e7.2.3 Sparse Multiblock PLS Regression (sMB-PLS) 196\u003c\/p\u003e \u003cp\u003e7.3 The Family of SO-PLS Regression Methods (Sequential and Orthogonalised PLS Regression) 199\u003c\/p\u003e \u003cp\u003e7.3.1 The SO-PLS Method 199\u003c\/p\u003e \u003cp\u003e7.3.2 Order of Blocks 202\u003c\/p\u003e \u003cp\u003e7.3.3 Interpretation Tools 202\u003c\/p\u003e \u003cp\u003e7.3.4 Restricted PLS Components and their Application in SO-PLS 203\u003c\/p\u003e \u003cp\u003e7.3.5 Validation and Component Selection 204\u003c\/p\u003e \u003cp\u003e7.3.6 Relations to ANOVA 205\u003c\/p\u003e \u003cp\u003e7.3.7 Extensions of SO-PLS to Handle Interactions Between Blocks 212\u003c\/p\u003e \u003cp\u003e7.3.8 Further Applications of SO-PLS 215\u003c\/p\u003e \u003cp\u003e7.3.9 Relations Between SO-PLS and ASCA 215\u003c\/p\u003e \u003cp\u003e7.4 Parallel and Orthogonalised PLS (PO-PLS) Regression 217\u003c\/p\u003e \u003cp\u003e7.5 Response Oriented Sequential Alternation 222\u003c\/p\u003e \u003cp\u003e7.5.1 The ROSA Method 222\u003c\/p\u003e \u003cp\u003e7.5.2 Validation 225\u003c\/p\u003e \u003cp\u003e7.5.3 Interpretation 225\u003c\/p\u003e \u003cp\u003e7.6 Conclusions and Recommendations 228\u003c\/p\u003e \u003cp\u003e7.7 Open Issues 229\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III Methods for Complex Multiblock Structures 231\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Complex Block Structures; with Focus on L-Shape Relations 233\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e8.i General Introduction 233\u003c\/p\u003e \u003cp\u003e8.ii Relations to the General Framework 234\u003c\/p\u003e \u003cp\u003e8.1 Analysis of L-shape Data: General Perspectives 235\u003c\/p\u003e \u003cp\u003e8.2 Sequential Procedures for L-shape Data Based on PLS\/PCR and ANOVA 236\u003c\/p\u003e \u003cp\u003e8.2.1 Interpretation of X1, Quantitative X2-data, Horizontal Axis First 236\u003c\/p\u003e \u003cp\u003e8.2.2 Interpretation of X1, Categorical X2-data, Horizontal Axis First 238\u003c\/p\u003e \u003cp\u003e8.2.3 Analysis of Segments\/Clusters of X1 Data 240\u003c\/p\u003e \u003cp\u003e8.3 The L-PLS Method for Joint Estimation of Blocks in L-shape Data 246\u003c\/p\u003e \u003cp\u003e8.3.1 The Original L-PLS Method, Endo-L-PLS 247\u003c\/p\u003e \u003cp\u003e8.3.2 Exo- Versus Endo-L-PLS 250\u003c\/p\u003e \u003cp\u003e8.4 Modifications of the Original L-PLS Idea 252\u003c\/p\u003e \u003cp\u003e8.4.1 Weighting Information from X3 and X1 in L-PLS Using a Parameter \u003ci\u003eα\u003c\/i\u003e252\u003c\/p\u003e \u003cp\u003e8.4.2 Three-blocks Bifocal PLS 253\u003c\/p\u003e \u003cp\u003e8.5 Alternative L-shape Data Analysis Methods 254\u003c\/p\u003e \u003cp\u003e8.5.1 Principal Component Analysis with External Information 254\u003c\/p\u003e \u003cp\u003e8.5.2 A Simple PCA Based Procedure for Using Unlabelled Data in Calibration 255\u003c\/p\u003e \u003cp\u003e8.5.3 Multivariate Curve Resolution for Incomplete Data 256\u003c\/p\u003e \u003cp\u003e8.5.4 An Alternative Approach in Consumer Science Based on Correlations Between X3 and X1 257\u003c\/p\u003e \u003cp\u003e8.6 Domino PLS and More Complex Data Structures 258\u003c\/p\u003e \u003cp\u003e8.7 Conclusions and Recommendations 258\u003c\/p\u003e \u003cp\u003e8.8 Open Issues 260\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart IV Alternative Methods for Unsupervised and Supervised Topologies 261\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Alternative Unsupervised Methods 263\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e9.i General Introduction 263\u003c\/p\u003e \u003cp\u003e9.ii Relationship to the General Framework 263\u003c\/p\u003e \u003cp\u003e9.1 Shared Variable Mode 263\u003c\/p\u003e \u003cp\u003e9.2 Shared Sample Mode 265\u003c\/p\u003e \u003cp\u003e9.2.1 Only Common Variation 265\u003c\/p\u003e \u003cp\u003e9.2.1.1 DIABLO 265\u003c\/p\u003e \u003cp\u003e9.2.1.2 Generalised Coupled Tensor Factorisation 266\u003c\/p\u003e \u003cp\u003e9.2.1.3 Representation Matrices 267\u003c\/p\u003e \u003cp\u003e9.2.1.4 Extended PCA 272\u003c\/p\u003e \u003cp\u003e9.2.2 Common, Local, and Distinct Variation 273\u003c\/p\u003e \u003cp\u003e9.2.2.1 Generalised SVD 273\u003c\/p\u003e \u003cp\u003e9.2.2.2 Structural Learning and Integrative Decomposition 273\u003c\/p\u003e \u003cp\u003e9.2.2.3 Bayesian Inter-battery Factor Analysis 275\u003c\/p\u003e \u003cp\u003e9.2.2.4 Group Factor Analysis 276\u003c\/p\u003e \u003cp\u003e9.2.2.5 OnPLS 277\u003c\/p\u003e \u003cp\u003e9.2.2.6 Generalised Association Study 278\u003c\/p\u003e \u003cp\u003e9.2.2.7 Multi-Omics Factor Analysis 278\u003c\/p\u003e \u003cp\u003e9.3 Two Shared Modes and Only Common Variation 281\u003c\/p\u003e \u003cp\u003e9.3.1 Generalised Procrustes Analysis 282\u003c\/p\u003e \u003cp\u003e9.3.2 Three-way Methods 282\u003c\/p\u003e \u003cp\u003e9.4 Conclusions and Recommendations 283\u003c\/p\u003e \u003cp\u003e9.4.1 Open Issues 284\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Alternative Supervised Methods 287\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e10.i General Introduction 287\u003c\/p\u003e \u003cp\u003e10.ii Relations to the General Framework 287\u003c\/p\u003e \u003cp\u003e10.1 Model and Focus 288\u003c\/p\u003e \u003cp\u003e10.2 Extension of PCovR 288\u003c\/p\u003e \u003cp\u003e10.2.1 Sparse Multiblock Principal Covariates Regression, Sparse PCovR 288\u003c\/p\u003e \u003cp\u003e10.2.2 Multiway Multiblock Covariates Regression 289\u003c\/p\u003e \u003cp\u003e10.3 Multiblock Redundancy Analysis 292\u003c\/p\u003e \u003cp\u003e10.3.1 Standard Multiblock Redundancy Analysis 292\u003c\/p\u003e \u003cp\u003e10.3.2 Sparse Multiblock Redundancy Analysis 294\u003c\/p\u003e \u003cp\u003e10.4 Miscellaneous Multiblock Regression Methods 295\u003c\/p\u003e \u003cp\u003e10.4.1 Multiblock Variance Partitioning 296\u003c\/p\u003e \u003cp\u003e10.4.2 Network Induced Supervised Learning 296\u003c\/p\u003e \u003cp\u003e10.4.3 Common Dimensions for Multiblock Regression 298\u003c\/p\u003e \u003cp\u003e10.5 Modifications and Extensions of the SO-PLS Method 298\u003c\/p\u003e \u003cp\u003e10.5.1 Extensions of SO-PLS to Three-Way Data 298\u003c\/p\u003e \u003cp\u003e10.5.2 Variable Selection for SO-PLS 299\u003c\/p\u003e \u003cp\u003e10.5.3 More Complicated Error Structure for SO-PLS 299\u003c\/p\u003e \u003cp\u003e10.5.4 SO-PLS Used for Path Modelling 300\u003c\/p\u003e \u003cp\u003e10.6 Methods for Data Sets Split Along the Sample Mode, Multigroup Methods 304\u003c\/p\u003e \u003cp\u003e10.6.1 Multigroup PLS Regression 304\u003c\/p\u003e \u003cp\u003e10.6.2 Clustering of Observations in Multiblock Regression 306\u003c\/p\u003e \u003cp\u003e10.6.3 Domain-Invariant PLS, DI-PLS 307\u003c\/p\u003e \u003cp\u003e10.7 Conclusions and Recommendations 308\u003c\/p\u003e \u003cp\u003e10.8 Open Issues 309\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart V Software 311\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Algorithms and Software 313\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e11.1 Multiblock Software 313\u003c\/p\u003e \u003cp\u003e11.2 R package multiblock 313\u003c\/p\u003e \u003cp\u003e11.3 Installing and Starting the Package 314\u003c\/p\u003e \u003cp\u003e11.4 Data Handling 314\u003c\/p\u003e \u003cp\u003e11.4.1 Read From File 314\u003c\/p\u003e \u003cp\u003e11.4.2 Data Pre-processing 315\u003c\/p\u003e \u003cp\u003e11.4.3 Re-coding Categorical Data 316\u003c\/p\u003e \u003cp\u003e11.4.4 Data Structures for Multiblock Analysis 317\u003c\/p\u003e \u003cp\u003e11.4.4.1 Create List of Blocks 317\u003c\/p\u003e \u003cp\u003e11.4.4.2 Create data.frame of Blocks 317\u003c\/p\u003e \u003cp\u003e11.5 Basic Methods 318\u003c\/p\u003e \u003cp\u003e11.5.1 Prepare Data 319\u003c\/p\u003e \u003cp\u003e11.5.2 Modelling 319\u003c\/p\u003e \u003cp\u003e11.5.3 Common Output Elements Across Methods 319\u003c\/p\u003e \u003cp\u003e11.5.4 Scores and Loadings 320\u003c\/p\u003e \u003cp\u003e11.6 Unsupervised Methods 321\u003c\/p\u003e \u003cp\u003e11.6.1 Formatting Data for Unsupervised Data Analysis 321\u003c\/p\u003e \u003cp\u003e11.6.2 Method Interfaces 322\u003c\/p\u003e \u003cp\u003e11.6.3 Shared Sample Mode Analyses 322\u003c\/p\u003e \u003cp\u003e11.6.4 Shared Variable Mode 322\u003c\/p\u003e \u003cp\u003e11.6.5 Common Output Elements Across Methods 323\u003c\/p\u003e \u003cp\u003e11.6.6 Scores and Loadings 324\u003c\/p\u003e \u003cp\u003e11.6.7 Plot From Imported Package 325\u003c\/p\u003e \u003cp\u003e11.7 ANOVA Simultaneous Component Analysis 325\u003c\/p\u003e \u003cp\u003e11.7.1 Formula Interface 325\u003c\/p\u003e \u003cp\u003e11.7.2 Simulated Data 325\u003c\/p\u003e \u003cp\u003e11.7.3 ASCA Modelling 325\u003c\/p\u003e \u003cp\u003e11.7.4 ASCA Scores 326\u003c\/p\u003e \u003cp\u003e11.7.5 ASCA Loadings 326\u003c\/p\u003e \u003cp\u003e11.8 Supervised Methods 327\u003c\/p\u003e \u003cp\u003e11.8.1 Formatting Data for Supervised Analyses 327\u003c\/p\u003e \u003cp\u003e11.8.2 Multiblock Partial Least Squares 328\u003c\/p\u003e \u003cp\u003e11.8.2.1 MB-PLS Modelling 328\u003c\/p\u003e \u003cp\u003e11.8.2.2 MB-PLS Summaries and Plotting 328\u003c\/p\u003e \u003cp\u003e11.8.3 Sparse Multiblock Partial Least Squares 328\u003c\/p\u003e \u003cp\u003e11.8.3.1 Sparse MB-PLS Modelling 328\u003c\/p\u003e \u003cp\u003e11.8.3.2 Sparse MB-PLS Plotting 329\u003c\/p\u003e \u003cp\u003e11.8.4 Sequential and Orthogonalised Partial Least Squares 330\u003c\/p\u003e \u003cp\u003e11.8.4.1 SO-PLS Modelling 330\u003c\/p\u003e \u003cp\u003e11.8.4.2 Måge Plot 331\u003c\/p\u003e \u003cp\u003e11.8.4.3 SO-PLS Loadings 332\u003c\/p\u003e \u003cp\u003e11.8.4.4 SO-PLS Scores 333\u003c\/p\u003e \u003cp\u003e11.8.4.5 SO-PLS Prediction 334\u003c\/p\u003e \u003cp\u003e11.8.4.6 SO-PLS Validation 334\u003c\/p\u003e \u003cp\u003e11.8.4.7 Principal Components of Predictions 336\u003c\/p\u003e \u003cp\u003e11.8.4.8 CVANOVA 336\u003c\/p\u003e \u003cp\u003e11.8.5 Parallel and Orthogonalised Partial Least Squares 337\u003c\/p\u003e \u003cp\u003e11.8.5.1 PO-PLS Modelling 337\u003c\/p\u003e \u003cp\u003e11.8.5.2 PO-PLS Scores and Loadings 338\u003c\/p\u003e \u003cp\u003e11.8.6 Response Optimal Sequential Alternation 339\u003c\/p\u003e \u003cp\u003e11.8.6.1 ROSA Modelling 339\u003c\/p\u003e \u003cp\u003e11.8.6.2 ROSA Loadings 340\u003c\/p\u003e \u003cp\u003e11.8.6.3 ROSA Scores 340\u003c\/p\u003e \u003cp\u003e11.8.6.4 ROSA Prediction 340\u003c\/p\u003e \u003cp\u003e11.8.6.5 ROSA Validation 341\u003c\/p\u003e \u003cp\u003e11.8.6.6 ROSA Image Plots 342\u003c\/p\u003e \u003cp\u003e11.8.7 Multiblock Redundancy Analysis 343\u003c\/p\u003e \u003cp\u003e11.8.7.1 MB-RDA Modelling 343\u003c\/p\u003e \u003cp\u003e11.8.7.2 MB-RDA Loadings and Scores 343\u003c\/p\u003e \u003cp\u003e11.9 Complex Data Structures 344\u003c\/p\u003e \u003cp\u003e11.9.1 L-PLS 344\u003c\/p\u003e \u003cp\u003e11.9.1.1 Simulated L-shaped Data 344\u003c\/p\u003e \u003cp\u003e11.9.1.2 Exo-L-PLS 344\u003c\/p\u003e \u003cp\u003e11.9.1.3 Endo-L-PLS 344\u003c\/p\u003e \u003cp\u003e11.9.1.4 L-PLS Cross-validation 345\u003c\/p\u003e \u003cp\u003e11.9.2 SO-PLS-PM 345\u003c\/p\u003e \u003cp\u003e11.9.2.1 Single SO-PLS-PM Model 346\u003c\/p\u003e \u003cp\u003e11.9.2.2 Multiple Paths in an SO-PLS-PM Model 346\u003c\/p\u003e \u003cp\u003e11.10 Software Packages 347\u003c\/p\u003e \u003cp\u003e11.10.1 R Packages 347\u003c\/p\u003e \u003cp\u003e11.10.2 MATLAB Toolboxes 348\u003c\/p\u003e \u003cp\u003e11.10.3 Python 349\u003c\/p\u003e \u003cp\u003e11.10.4 Commercial Software 349\u003ci\u003e                \u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eReferences 351\u003c\/p\u003e \u003cp\u003eIndex 373\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407096488279,"sku":"9781119600961","price":118.76,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119600961.jpg?v=1730498163"},{"product_id":"data-analysis-and-chemometrics-for-metabolomics-9781119639381","title":"Data Analysis and Chemometrics for Metabolomics","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003eUnderstand new modes of analysing metabolomic data Metabolomics is the study of metabolites, small molecules and chemical substrates within cells or larger structures which collectively make up the metabolome. The field of metabolomics stands to benefit enormously from chemometrics, an approach which brings advanced statistical techniques to bear on data of this kind. Data Analysis and Chemometrics for Metabolomics constitutes an accessible introduction to chemometric techniques and their applications in the field of metabolomics. Thoroughly and accessibly written by a leading expert in chemometrics, and printed in full-colour, it brings robust data analysis into conversation with the metabolomic field to the immense benefit of practitioners. Data Analysis and Chemometrics for Metabolomics readers will also find: Statistical insights into the nature of metabolomic hypothesis testing, validation, and more All metabolomics data sets from the book on a companion website Case studies from","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407106056535,"sku":"9781119639381","price":99.0,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119639381.jpg?v=1730498196"},{"product_id":"dna-origami-9781119682547","title":"DNA Origami","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eDNA ORIGAMI\u003c\/b\u003e  \u003cp\u003e\u003cb\u003eDiscover the impact and multidisciplinary applications of this subfield of DNA nanotechnology \u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eDNA origami refers to the technique of assembling single-stranded DNA template molecules into target two- and three-dimensional shapes at the nanoscale. This is accomplished by annealing templates with hundreds of DNA strands and then binding them through the specific base-pairing of complementary bases. The inherent properties of these DNA moleculesmolecular recognition, self-assembly, programmability, and structural predictabilityhas given rise to intriguing applications from drug delivery systems to uses in circuitry in plasmonic devices. \u003c\/p\u003e\u003cp\u003eThe first book to examine this important subfield, \u003ci\u003eDNA Origami \u003c\/i\u003ebrings together leading experts from all fields to explain the current state and future directions of this cutting-edge avenue of study. The book begins by providing a detailed examination of structural design and assembly systems and their applicatio\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e\u003cp\u003eList of Contributors xiii\u003c\/p\u003e \u003cp\u003ePreface xvii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 DNA Origami Technology: Achievements in the Initial 10 Years 1\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMasayuki Endo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.1.1 DNA Nanotechnology Before the Emergence of DNA Origami 3\u003c\/p\u003e \u003cp\u003e1.2 Two- Dimensional DNA Origami 3\u003c\/p\u003e \u003cp\u003e1.3 Programmed Arrangement of Multiple DNA Origami Components 6\u003c\/p\u003e \u003cp\u003e1.4 Three- Dimensional DNA Origami Structures 9\u003c\/p\u003e \u003cp\u003e1.5 Modification and Functionalization of 2D DNA Origami Structures 11\u003c\/p\u003e \u003cp\u003e1.5.1 Selective Placement of Functional Nanomaterials 11\u003c\/p\u003e \u003cp\u003e1.5.2 Selective Placement of Functional Molecules and Proteins via Ligands 13\u003c\/p\u003e \u003cp\u003e1.5.3 Distance- Controlled Enzyme Reactions and Photoreactions 13\u003c\/p\u003e \u003cp\u003e1.6 Single- Molecule Detection and Sensing using DNA Origami Structures 14\u003c\/p\u003e \u003cp\u003e1.6.1 Single- Molecule RNA Detection 14\u003c\/p\u003e \u003cp\u003e1.6.2 Single- Molecule Detection of Chemical Reactions 14\u003c\/p\u003e \u003cp\u003e1.6.3 Single- Molecule Detection using Mechanical DNA Origami 14\u003c\/p\u003e \u003cp\u003e1.6.4 Single- Molecule Sensing using Mechanical DNA Origami 14\u003c\/p\u003e \u003cp\u003e1.7 Application to Single Biomolecule AFM Imaging 16\u003c\/p\u003e \u003cp\u003e1.7.1 High- Speed AFM- Based Observation of Biomolecules 16\u003c\/p\u003e \u003cp\u003e1.7.2 Visualization of DNA Structural Changes in the DNA Nanospace 18\u003c\/p\u003e \u003cp\u003e1.7.3 Visualization of the Reaction Events of Enzymes and Proteins in the DNA Nanospace 18\u003c\/p\u003e \u003cp\u003e1.8 Single- Molecule Fluorescence Studies 19\u003c\/p\u003e \u003cp\u003e1.8.1 Nanoscopic Ruler for Single- Molecule Imaging 19\u003c\/p\u003e \u003cp\u003e1.8.2 Kinetics of Binding and Unbinding Events and DNA- PAINT 21\u003c\/p\u003e \u003cp\u003e1.8.3 DNA Barcode Imaged by DNA- PAINT 21\u003c\/p\u003e \u003cp\u003e1.9 DNA Molecular Machines 22\u003c\/p\u003e \u003cp\u003e1.9.1 DNA Assembly Line Constructed on the DNA Origami 22\u003c\/p\u003e \u003cp\u003e1.9.2 DNA Spider System Constructed on the DNA Origami 22\u003c\/p\u003e \u003cp\u003e1.9.3 DNA Motor System Constructed on the DNA Origami 24\u003c\/p\u003e \u003cp\u003e1.10 Selective Incorporation of Nanomaterials and the Applications 24\u003c\/p\u003e \u003cp\u003e1.10.1 DNA Origami Plasmonic Structure with Chirality 24\u003c\/p\u003e \u003cp\u003e1.10.2 Surface- Enhanced Fluorescence by Gold Nanoparticles and DNA Origami Structure 26\u003c\/p\u003e \u003cp\u003e1.10.3 Placement of DNA Origami onto a Fabricated Solid Surface 26\u003c\/p\u003e \u003cp\u003e1.11 Dynamic DNA Origami Structures Responsive to External Stimuli 27\u003c\/p\u003e \u003cp\u003e1.11.1 DNA Origami Structures Responsive to External Stimuli 27\u003c\/p\u003e \u003cp\u003e1.11.2 Stimuli- Responsive DNA Origami Plasmonic Structures 27\u003c\/p\u003e \u003cp\u003e1.11.3 Photo- Controlled DNA Origami Plasmonic Structures 27\u003c\/p\u003e \u003cp\u003e1.12 Conjugation of DNA Origami to Lipid 29\u003c\/p\u003e \u003cp\u003e1.12.1 DNA Origami Channel with Gating 29\u003c\/p\u003e \u003cp\u003e1.12.2 DNA Origami Templated Synthesis of Liposomes 29\u003c\/p\u003e \u003cp\u003e1.13 DNA Origami for Biological Applications 29\u003c\/p\u003e \u003cp\u003e1.13.1 Introduction of DNA Origami into Cells and Functional Expression 29\u003c\/p\u003e \u003cp\u003e1.13.2 Drug Release Using the Properties Characteristic for DNA Origami 31\u003c\/p\u003e \u003cp\u003e1.13.3 DNA Origami Structures Coated with Lipids and Polymers 32\u003c\/p\u003e \u003cp\u003e1.13.4 Nanorobot with Dynamic Mechanism 32\u003c\/p\u003e \u003cp\u003e1.13.5 Nanorobot Targeting Tumor In Vivo 32\u003c\/p\u003e \u003cp\u003e1.14 Conclusions 33\u003c\/p\u003e \u003cp\u003eReferences 34\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Wireframe DNA Origami and Its Application as Tools for Molecular Force Generation 41\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMarco Lolaico and Björn Högberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 41\u003c\/p\u003e \u003cp\u003e2.2 Pre- Origami Wireframe DNA Nanostructures 42\u003c\/p\u003e \u003cp\u003e2.3 Hierarchical DNA Origami Wireframe 43\u003c\/p\u003e \u003cp\u003e2.4 Entire DNA Origami Design 45\u003c\/p\u003e \u003cp\u003e2.5 DNA Origami Wireframe as Tools for Molecular Force Application 50\u003c\/p\u003e \u003cp\u003e2.5.1 Introduction 50\u003c\/p\u003e \u003cp\u003e2.5.2 Results and Discussion 51\u003c\/p\u003e \u003cp\u003e2.6 Conclusions 54\u003c\/p\u003e \u003cp\u003e2.6.1 Materials and Methods 54\u003c\/p\u003e \u003cp\u003eReferences 55\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Capturing Structural Switching and Self- Assembly Events Using High- Speed Atomic Force Microscopy 59\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eYuki Suzuki\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 59\u003c\/p\u003e \u003cp\u003e3.2 DNA Origami Nanomachines 60\u003c\/p\u003e \u003cp\u003e3.3 Ion- Responsive Mechanical DNA Origami Devices 60\u003c\/p\u003e \u003cp\u003e3.4 Photoresponsive Devices 62\u003c\/p\u003e \u003cp\u003e3.5 Two- Dimensional Self- Assembly Processes 64\u003c\/p\u003e \u003cp\u003e3.6 Sequential Self- Assembly 66\u003c\/p\u003e \u003cp\u003e3.7 Photostimulated Assembly and Disassembly 67\u003c\/p\u003e \u003cp\u003e3.8 Conclusions and Perspectives 69\u003c\/p\u003e \u003cp\u003eReferences 69\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Advancement of Computer- Aided Design Software and Simulation Tools for Nucleic Acid Nanostructures and DNA Origami 75\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eIbuki Kawamata\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 75\u003c\/p\u003e \u003cp\u003e4.2 General- Purpose Software 76\u003c\/p\u003e \u003cp\u003e4.3 Software for Designing Small DNA Nanostructures 78\u003c\/p\u003e \u003cp\u003e4.4 Software for Designing DNA Origami 81\u003c\/p\u003e \u003cp\u003e4.5 Software for Designing RNA Nanostructures 84\u003c\/p\u003e \u003cp\u003e4.6 Software for Designing Base Sequence 84\u003c\/p\u003e \u003cp\u003e4.7 Software for Simulating Nucleic Acid Nanostructures 85\u003c\/p\u003e \u003cp\u003e4.8 Summary and Future Perspective 86\u003c\/p\u003e \u003cp\u003eReferences 87\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Dynamic and Mechanical Applications of DNA Nanostructures in Biophysics 101\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMelika Shahhosseini, Anjelica Kucinic, Peter Beshay, Wolfgang Pfeifer, and Carlos Castro\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 101\u003c\/p\u003e \u003cp\u003e5.1.1 What Makes DNA a Good Material for Dynamic Applications 101\u003c\/p\u003e \u003cp\u003e5.1.2 Rupture Forces 103\u003c\/p\u003e \u003cp\u003e5.2 Applications 105\u003c\/p\u003e \u003cp\u003e5.2.1 Force Spectroscopy 105\u003c\/p\u003e \u003cp\u003e5.2.1.1 Utilizing the Stiffness of DNA for Force Spectroscopy 105\u003c\/p\u003e \u003cp\u003e5.2.1.2 Applications that Utilize Rupture Forces 107\u003c\/p\u003e \u003cp\u003e5.2.2 DNA Devices that Probe and Control DNA–DNA Interactions 108\u003c\/p\u003e \u003cp\u003e5.2.2.1 Detection 108\u003c\/p\u003e \u003cp\u003e5.2.2.2 Modulation 111\u003c\/p\u003e \u003cp\u003e5.2.3 DNA Devices that Respond to Biomolecules 111\u003c\/p\u003e \u003cp\u003e5.2.4 DNA Devices to Study Biological Molecular Motors 116\u003c\/p\u003e \u003cp\u003e5.2.5 DNA Walkers 116\u003c\/p\u003e \u003cp\u003e5.2.6 DNA Computing 119\u003c\/p\u003e \u003cp\u003e5.3 Tools for Quantifying DNA Devices and their Functions 120\u003c\/p\u003e \u003cp\u003e5.4 Modeling and Analysis 123\u003c\/p\u003e \u003cp\u003e5.5 Conclusion 124\u003c\/p\u003e \u003cp\u003eReferences 124\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Plasmonic Nanostructures Assembled by DNA Origami 135\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eSergio Kogikoski, Jr, Anushree Dutta, and Ilko Bald\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 135\u003c\/p\u003e \u003cp\u003e6.2 Optical Properties of the DNA Origami- Based Plasmonic Nanostructures 135\u003c\/p\u003e \u003cp\u003e6.3 Nanoparticle Functionalization with DNA 138\u003c\/p\u003e \u003cp\u003e6.4 DNA Origami- Based Plasmonic Assemblies 140\u003c\/p\u003e \u003cp\u003e6.5 Surface- Enhanced Raman Scattering (SERS) and Other Plasmonic Effects 143\u003c\/p\u003e \u003cp\u003e6.6 Conclusion 152\u003c\/p\u003e \u003cp\u003eAcknowledgments 152\u003c\/p\u003e \u003cp\u003eReferences 152\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Assembly of Nanoparticle Superlattices Using DNA Origami as a Template 155\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eSofia Julin, Petteri Piskunen, Mauri A. Kostiainen, and Veikko Linko\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 155\u003c\/p\u003e \u003cp\u003e7.2 Gold Nanoparticles 156\u003c\/p\u003e \u003cp\u003e7.2.1 Oligonucleotide- Modified AuNPs 156\u003c\/p\u003e \u003cp\u003e7.2.2 Cationic AuNPs 158\u003c\/p\u003e \u003cp\u003e7.3 Formation of DNA Origami- Assisted Superlattices 158\u003c\/p\u003e \u003cp\u003e7.3.1 Superlattices Formed by Oligonucleotide- Functionalized AuNPs 159\u003c\/p\u003e \u003cp\u003e7.3.2 Superlattice Formed by Cationic AuNPs 160\u003c\/p\u003e \u003cp\u003e7.4 Characterization of Assemblies 160\u003c\/p\u003e \u003cp\u003e7.4.1 Electron Microscopy 161\u003c\/p\u003e \u003cp\u003e7.4.2 Small- Angle X- ray Scattering 161\u003c\/p\u003e \u003cp\u003e7.5 Conclusions and Future Perspectives 162\u003c\/p\u003e \u003cp\u003eAcknowledgments 164\u003c\/p\u003e \u003cp\u003eReferences 164\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Mechanics of DNA Origami Nanoassemblies 167\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eDeepak Karna, Jiahao Ji, and Hanbin Mao\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 167\u003c\/p\u003e \u003cp\u003e8.2 Analytical Tools to Investigate Mechanical Properties of Nanoassemblies 168\u003c\/p\u003e \u003cp\u003e8.2.1 Optical Tweezers 168\u003c\/p\u003e \u003cp\u003e8.2.2 Magnetic Tweezers 169\u003c\/p\u003e \u003cp\u003e8.2.3 Atomic Force Microscopy (AFM) 169\u003c\/p\u003e \u003cp\u003e8.3 Mechanical Strength of DNA Origami Structures 171\u003c\/p\u003e \u003cp\u003e8.4 Applications of Origami Nanostructures by Exploiting their Mechanical Strength 173\u003c\/p\u003e \u003cp\u003e8.5 Mechanochemical Properties of DNA Origami 175\u003c\/p\u003e \u003cp\u003e8.6 Conclusions 177\u003c\/p\u003e \u003cp\u003eReferences 177\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 3D DNA Origami as Single- Molecule Biophysical Tools for Dissecting Molecular Motor Functions 181\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMitsuhiro Iwaki\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 181\u003c\/p\u003e \u003cp\u003e9.2 DNA Origami Nanospring 181\u003c\/p\u003e \u003cp\u003e9.2.1 Design of DNA Origami Nanospring 181\u003c\/p\u003e \u003cp\u003e9.2.2 Nanospring Mechanical Properties 182\u003c\/p\u003e \u003cp\u003e9.2.3 Application to a Myosin VI Processive Motor 183\u003c\/p\u003e \u003cp\u003e9.3 DNA Origami Thick Filament Mimicking Muscle Structure 187\u003c\/p\u003e \u003cp\u003e9.3.1 Mystery of Muscle Contraction 187\u003c\/p\u003e \u003cp\u003e9.3.2 Design of a DNA Origami- Based Thick Filament 188\u003c\/p\u003e \u003cp\u003e9.3.3 High- speed AFM Observation of Force Generation by Myosin 189\u003c\/p\u003e \u003cp\u003e9.3.4 High- Speed Darkfield Imaging of Force Generation by Myosin 189\u003c\/p\u003e \u003cp\u003e9.4 Perspective 193\u003c\/p\u003e \u003cp\u003eReferences 193\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Switchable DNA Origami Nanostructures and Their Applications 197\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJianbang Wang, Michael P. O’Hagan, Verena Wulf, and Itamar Willner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 197\u003c\/p\u003e \u003cp\u003e10.2 Switchable Machines Constructed from DNA Origami Scaffolds 198\u003c\/p\u003e \u003cp\u003e10.2.1 Chemical Triggers for Origami Scaffolds 198\u003c\/p\u003e \u003cp\u003e10.2.1.1 Triggering Origami Devices with Strand Displacement Reactions 198\u003c\/p\u003e \u003cp\u003e10.2.1.2 Triggering Origami with Ion Concentration 200\u003c\/p\u003e \u003cp\u003e10.2.1.3 Triggering Origami with Molecular Species 202\u003c\/p\u003e \u003cp\u003e10.2.2 Physical Triggers for Origami Scaffolds 204\u003c\/p\u003e \u003cp\u003e10.2.2.1 Triggering Origami with Temperature 204\u003c\/p\u003e \u003cp\u003e10.2.2.2 Triggering Origami with Electric Fields 206\u003c\/p\u003e \u003cp\u003e10.2.2.3 Triggering Origami with Magnetic Fields 206\u003c\/p\u003e \u003cp\u003e10.2.2.4 Triggering Origami with Light 208\u003c\/p\u003e \u003cp\u003e10.3 DNA Origami Scaffolds for Defined Mechanical Operations 210\u003c\/p\u003e \u003cp\u003e10.3.1 Origami Scaffolds that Dictate the Motility of Elements 212\u003c\/p\u003e \u003cp\u003e10.3.2 Engineering Mechanical Functions of Origami Tiles 218\u003c\/p\u003e \u003cp\u003e10.4 Switchable Interconnected 2D Origami Assemblies 218\u003c\/p\u003e \u003cp\u003e10.5 Dynamic Triggered Switching of Origami for Controlled Release 223\u003c\/p\u003e \u003cp\u003e10.6 Switchable Plasmonic Phenomena with DNA Origami Scaffolds 227\u003c\/p\u003e \u003cp\u003e10.7 Origami- Guided Organization of Nanoparticles and Proteins 234\u003c\/p\u003e \u003cp\u003e10.8 Conclusions and Perspectives 238\u003c\/p\u003e \u003cp\u003eReferences 239\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 The Effect of DNA Boundaries on Enzymatic Reactions 241\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRichard Kosinski and Barbara Saccà\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 241\u003c\/p\u003e \u003cp\u003e11.2 DNA- Scaffolded Single Enzymes 242\u003c\/p\u003e \u003cp\u003e11.3 DNA- Scaffolded Enzyme Cascades 247\u003c\/p\u003e \u003cp\u003e11.4 On the Proximity Model and Other Hypotheses 250\u003c\/p\u003e \u003cp\u003e11.5 Conclusions 254\u003c\/p\u003e \u003cp\u003eAcknowledgments 256\u003c\/p\u003e \u003cp\u003eReferences 256\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 The Methods to Assemble Functional Proteins on DNA Scaffold and their Applications 261\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eEiji Nakata, Shiwei Zhang, Huyen Dinh, Peng Lin, and Takashi Morii\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 261\u003c\/p\u003e \u003cp\u003e12.2 Overview of the Methods for Arranging Proteins on DNA Scaffolds 262\u003c\/p\u003e \u003cp\u003e12.2.1 Reversible Conjugation between Protein and DNA 263\u003c\/p\u003e \u003cp\u003e12.2.1.1 Biotin- Avidin 264\u003c\/p\u003e \u003cp\u003e12.2.1.2 Antibody- Antigen 264\u003c\/p\u003e \u003cp\u003e12.2.1.3 Ni- NTA- Hexahistidine 266\u003c\/p\u003e \u003cp\u003e12.2.1.4 Aptamers 266\u003c\/p\u003e \u003cp\u003e12.2.1.5 Apo- Protein Reconstitution by the Prosthetic Group 266\u003c\/p\u003e \u003cp\u003e12.2.2 Irreversible Conjugation between Protein and DNA 266\u003c\/p\u003e \u003cp\u003e12.2.2.1 Chemical Crosslinking of Protein and DNA via Cross- Linker 267\u003c\/p\u003e \u003cp\u003e12.2.2.2 Crosslinking of Genetically Fused Protein with Chemically Modified DNA 267\u003c\/p\u003e \u003cp\u003e12.2.2.3 Covalent Conjugation of Genetically Modified Proteins to Unmodified DNA 269\u003c\/p\u003e \u003cp\u003e12.2.2.4 Applications of the Enzyme Assembled DNA Scaffolds 269\u003c\/p\u003e \u003cp\u003e12.3 DNA- Binding Adaptor for Assembling Proteins on DNA Scaffold and its Application 270\u003c\/p\u003e \u003cp\u003e12.3.1 DNA- Binding Adaptor for Reversible Assembly of Proteins via Noncovalent Interactions 270\u003c\/p\u003e \u003cp\u003e12.3.2 Modular Adaptors for Covalent Conjugation of Genetically Modified Proteins to Chemically Modified DNA 272\u003c\/p\u003e \u003cp\u003e12.3.3 Application of DNA- Binding Adaptors for Assembling Proteins on DNA Scaffolds 275\u003c\/p\u003e \u003cp\u003e12.3.3.1 Assembling Protein of Interest on DNA Scaffold in Cell 275\u003c\/p\u003e \u003cp\u003e12.3.3.2 Enzymatic Reaction System on a DNA Scaffold 275\u003c\/p\u003e \u003cp\u003e12.4 Summary 278\u003c\/p\u003e \u003cp\u003eReferences 278\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 DNA Origami for Synthetic Biology: An Integrated Gene Logic- Chip 281\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eHisashi Tadakuma\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 281\u003c\/p\u003e \u003cp\u003e13.2 Biomolecule Integration on DNA Nanostructure 281\u003c\/p\u003e \u003cp\u003e13.2.1 Nature Uses “Reaction Field” to Overcome the Cross- Talk Problem 281\u003c\/p\u003e \u003cp\u003e13.2.2 Synthetic Biology Approach 282\u003c\/p\u003e \u003cp\u003e13.2.3 DNA–Protein Complex 282\u003c\/p\u003e \u003cp\u003e13.2.4 Enzymatic Reaction on DNA Origami for Low- Molecular- Weight Substrate 284\u003c\/p\u003e \u003cp\u003e13.3 Gene Expression Control Using DNA Nanostructure 285\u003c\/p\u003e \u003cp\u003e13.3.1 Enzymatic Reaction on DNA Origami for High- Molecular- Weight Substrate 285\u003c\/p\u003e \u003cp\u003e13.3.2 Resolving Synthetic Biology Limitation by DNA Origami- Based Nano- Chip 286\u003c\/p\u003e \u003cp\u003e13.3.3 Unique Characters of the Nano- Chip 288\u003c\/p\u003e \u003cp\u003e13.3.4 Limitation of the Nano- Chip 292\u003c\/p\u003e \u003cp\u003e13.4 Summary and Perspective 292\u003c\/p\u003e \u003cp\u003eAcknowledgments 293\u003c\/p\u003e \u003cp\u003eReferences 293\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 DNA Origami for Molecular Robotics 297\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAkinori Kuzuya\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 DNA Origami as a Stage for DNA Walkers and Robotic Arms 297\u003c\/p\u003e \u003cp\u003e14.2 Nanomechanical DNA Origami 298\u003c\/p\u003e \u003cp\u003e14.3 DNA Origami Used in Combination with Molecular Motors 300\u003c\/p\u003e \u003cp\u003e14.4 Future Perspective 301\u003c\/p\u003e \u003cp\u003eReferences 303\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 DNA origami Nanotechnology for the Visualization, Analysis, and Control of Molecular Events with Nanoscale Precision 305\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eXiwen Xing and Masayuki Endo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction 305\u003c\/p\u003e \u003cp\u003e15.2 Designing of DNA Origami Frames for the Direct Observation of DNA Conformational Changes 308\u003c\/p\u003e \u003cp\u003e15.3 Direct Observation of DNA Structural Changes in the DNA Origami Frame 308\u003c\/p\u003e \u003cp\u003e15.3.1 G- Quadruplex Formation and Disruption 308\u003c\/p\u003e \u003cp\u003e15.3.2 G- Quadruplex Formation by the Assembly of Four DNA Strands 309\u003c\/p\u003e \u003cp\u003e15.3.3 Light- Induced Hybridization and Dehybridization of the Photoswitchable DNA Strands 309\u003c\/p\u003e \u003cp\u003e15.3.4 Direct Observation of B–Z Transition in the Equilibrium State 312\u003c\/p\u003e \u003cp\u003e15.3.5 Topological Control of G- Quadruplex and I- Motif Formation in the dsDNA 314\u003c\/p\u003e \u003cp\u003e15.4 Direct Observation and Regulation of Enzyme Reactions in the DNA Origami Frame 315\u003c\/p\u003e \u003cp\u003e15.4.1 Direct Observation and Regulation of Cre- Mediated DNA Recombination in the DNA Origami Frame 315\u003c\/p\u003e \u003cp\u003e15.4.2 Holiday- Junction Resolution Mediated by DNA Resolvase 317\u003c\/p\u003e \u003cp\u003e15.4.3 DNA Oxidation in the DNA Demethylation Process Mediated by TET Enzyme 317\u003c\/p\u003e \u003cp\u003e15.4.4 Searching and Recognition of Target Sites by using Photoresponsive Transcription Factor GAL 4 319\u003c\/p\u003e \u003cp\u003e15.5 Direct Observation of a Mobile DNA Nanomachine using DNA Origami 321\u003c\/p\u003e \u003cp\u003e15.5.1 A DNA Linear Motor System Created on a DNA Origami System 321\u003c\/p\u003e \u003cp\u003e15.5.2 Single- Molecule Operation of DNA Motor by using Programmed Instructions 321\u003c\/p\u003e \u003cp\u003e15.5.3 Photo- Controlled DNA Motor System Constructed on DNA Origami 324\u003c\/p\u003e \u003cp\u003e15.5.4 Photo- Controlled DNA Rotator System Constructed on DNA Origami 324\u003c\/p\u003e \u003cp\u003e15.6 Limitations of AFM Imaging and Comparison with other Imaging Techniques 326\u003c\/p\u003e \u003cp\u003e15.7 Conclusions and Perspectives 326\u003c\/p\u003e \u003cp\u003eReferences 327\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Stability and Stabilization of DNA Nanostructures in Biomedical Applications 333\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eSoumya Chandrasekhar, Praneetha Sundar Prakash, and Thorsten- Lars Schmidt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Threats for DNA Nanostructures 333\u003c\/p\u003e \u003cp\u003e16.1.1 Errors from Nanostructure Synthesis 334\u003c\/p\u003e \u003cp\u003e16.1.1.1 Missing Strands 334\u003c\/p\u003e \u003cp\u003e16.1.1.2 Oligonucleotide Synthesis Errors 335\u003c\/p\u003e \u003cp\u003e16.1.2 Denaturation of DNA Duplexes 336\u003c\/p\u003e \u003cp\u003e16.1.2.1 Melting 336\u003c\/p\u003e \u003cp\u003e16.1.2.2 The Role of Cations 336\u003c\/p\u003e \u003cp\u003e16.1.2.3 Influence of pH on Duplex Stability 337\u003c\/p\u003e \u003cp\u003e16.1.3 Backbone Cleavage 337\u003c\/p\u003e \u003cp\u003e16.1.3.1 Acid- Induced Depurination 337\u003c\/p\u003e \u003cp\u003e16.1.3.2 Base- Induced Cleavage of RNA 338\u003c\/p\u003e \u003cp\u003e16.1.3.3 Enzymatic Digest 338\u003c\/p\u003e \u003cp\u003e16.1.4 Chemical Damage at the Nucleobases 339\u003c\/p\u003e \u003cp\u003e16.1.4.1 Ultraviolet Radiation 339\u003c\/p\u003e \u003cp\u003e16.1.4.2 Radiative and Oxidative DNA Damage 340\u003c\/p\u003e \u003cp\u003e16.1.4.3 Deamination 340\u003c\/p\u003e \u003cp\u003e16.1.5 DNA Structures for Biological Applications 341\u003c\/p\u003e \u003cp\u003e16.1.5.1 Bioimaging 341\u003c\/p\u003e \u003cp\u003e16.1.5.2 Biosensing 341\u003c\/p\u003e \u003cp\u003e16.1.5.3 Computing 341\u003c\/p\u003e \u003cp\u003e16.1.5.4 Single- Molecule Biophysics and Mechanobiology 343\u003c\/p\u003e \u003cp\u003e16.1.5.5 Drug Delivery and Gene Therapy 343\u003c\/p\u003e \u003cp\u003e16.1.6 In vitro and In vivo Degradation and Clearance of DNA Structures 343\u003c\/p\u003e \u003cp\u003e16.1.6.1 Common in vitro and in vivo Stability Assays 344\u003c\/p\u003e \u003cp\u003e16.1.6.2 Degradation of DN in in vitro and in vivo 344\u003c\/p\u003e \u003cp\u003e16.1.6.3 Low Mg\u003csup\u003e2+\u003c\/sup\u003e Conditions \u003ci\u003e346\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1.6.4 Presence of Nucleases 346\u003c\/p\u003e \u003cp\u003e16.1.6.5 Cellular Uptake and Clearance of DNs 347\u003c\/p\u003e \u003cp\u003e16.1.6.6 Immune Response 348\u003c\/p\u003e \u003cp\u003e16.2 Strategies to Protect DNA Origami Structures 349\u003c\/p\u003e \u003cp\u003e16.2.1 Stabilization by Design 349\u003c\/p\u003e \u003cp\u003e16.2.2 Stabilization by Covalent Strategies 351\u003c\/p\u003e \u003cp\u003e16.2.2.1 Enzymatic Ligation 351\u003c\/p\u003e \u003cp\u003e16.2.2.2 Chemical Crosslinking 352\u003c\/p\u003e \u003cp\u003e16.2.2.3 Photo Crosslinking 354\u003c\/p\u003e \u003cp\u003e16.2.2.4 Base Analogues and Backbone Modification 356\u003c\/p\u003e \u003cp\u003e16.2.3 Stabilization by Non- Covalent Strategies and Additives 356\u003c\/p\u003e \u003cp\u003e16.2.3.1 Inorganic Materials 356\u003c\/p\u003e \u003cp\u003e16.2.3.2 Proteins 358\u003c\/p\u003e \u003cp\u003e16.2.3.3 Polymer, Peptides, and Polycation Coatings 358\u003c\/p\u003e \u003cp\u003eReferences 362\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 DNA Nanostructures for Cancer Diagnosis and Therapy 379\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eZhe Li and Yonggang Ke\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Introduction 379\u003c\/p\u003e \u003cp\u003e17.2 DNA Nanostructure- Based Diagnostics 380\u003c\/p\u003e \u003cp\u003e17.2.1 Nucleic Acid Detection 380\u003c\/p\u003e \u003cp\u003e17.2.2 Protein and Exosome Detection 382\u003c\/p\u003e \u003cp\u003e17.2.3 Tumor Cell Detection 384\u003c\/p\u003e \u003cp\u003e17.2.4 Imaging 385\u003c\/p\u003e \u003cp\u003e17.3 DNA Nanostructure- Based Drug Delivery 386\u003c\/p\u003e \u003cp\u003e17.3.1 Small Molecules 386\u003c\/p\u003e \u003cp\u003e17.3.1.1 Doxorubicin 386\u003c\/p\u003e \u003cp\u003e17.3.1.2 Platinum- Based Drugs 387\u003c\/p\u003e \u003cp\u003e17.3.2 Biologics 389\u003c\/p\u003e \u003cp\u003e17.3.2.1 CpG 389\u003c\/p\u003e \u003cp\u003e17.3.2.2 RNA 390\u003c\/p\u003e \u003cp\u003e17.3.2.3 Protein 392\u003c\/p\u003e \u003cp\u003e17.3.3 Inorganic Nanoparticles 393\u003c\/p\u003e \u003cp\u003e17.4 Challenges and Prospects 394\u003c\/p\u003e \u003cp\u003e17.4.1 Stability 394\u003c\/p\u003e \u003cp\u003e17.4.1.1 Nucleases 395\u003c\/p\u003e \u003cp\u003e17.4.1.2 Mg\u003csup\u003e2+\u003c\/sup\u003e 395\u003c\/p\u003e \u003cp\u003e17.4.1.3 Shape and Superstructure of DNA Nanostructures 396\u003c\/p\u003e \u003cp\u003e17.4.2 Drug Loading Efficiency 396\u003c\/p\u003e \u003cp\u003e17.4.3 Drug releasing efficiency 397\u003c\/p\u003e \u003cp\u003e17.4.4 Cell Internalization 398\u003c\/p\u003e \u003cp\u003eReferences 400\u003c\/p\u003e \u003cp\u003eIndex 411\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407119491415,"sku":"9781119682547","price":146.66,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119682547.jpg?v=1730498247"},{"product_id":"carbon-monoxide-in-drug-discovery-9781119783404","title":"Carbon Monoxide in Drug Discovery","description":"\u003ch2\u003eBook Synopsis\u003c\/h2\u003e\u003cb\u003eCARBON MONOXIDE IN DRUG DISCOVERY\u003c\/b\u003e  \u003cp\u003e\u003cb\u003eAn insightful reference for the latest physiological and therapeutic studies of carbon monoxide\u003c\/b\u003e \u003c\/p\u003e\u003cp\u003eIn \u003ci\u003eCarbon Monoxide in Drug Discovery: Basics, Pharmacology, and Therapeutic Potential,\u003c\/i\u003e a team of distinguished authors delivers foundational knowledge, the latest research, and remaining challenges regarding the physiological roles and therapeutic efficacy of carbon monoxide (CO). The editors have included a broad selection of resources from leading experts in the field that discuss the background and physiological roles of CO, a variety of delivery forms including CO prodrugs using benign carriers, CO sensing, therapeutic applications, and clinical trials. \u003c\/p\u003e\u003cp\u003eOrganized by topic to allow each chapter to be read individually, the book covers a wide range of topics, from physiological and patho-physiological mechanisms at the molecular level to clinical applications for multiple disease processes. \u003c\/p\u003e\u003cp\u003eThe editors of \u003ci\u003eCarbon Monoxid\u003cbr\u003e\u003cbr\u003e\u003ch2\u003eTable of Contents\u003c\/h2\u003e\u003c\/i\u003e\u003c\/p\u003e\u003cp\u003eList of Contributors viii\u003c\/p\u003e \u003cp\u003ePreface: Carbon Monoxide: Promises and Challenges in Its Pharmaceutical Development xii\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection I General Background and Physiological Actions 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1 Endogenous CO Production in Sickness and in Health 3\u003cbr\u003e \u003ci\u003eLadie Kimberly De La Cruz and Binghe Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2 Molecular Mechanisms of Actions for CO: An Overview 27\u003cbr\u003e \u003ci\u003eRodrigo W. Alves de Souza, Leo E. Otterbein, and Nils Schallner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3 Pharmacokinetic Characteristics of Carbon Monoxide 44\u003cbr\u003e \u003ci\u003eXiaoxiao Yang, Mingjia Wang, Chalet Tan, Wen Lu, and Binghe Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4 Carbon Monoxide and Energy Metabolism 88\u003cbr\u003e \u003ci\u003eDaniela Dias-Pedroso, Nuno Soares, and Helena L.A. Vieira\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5 Role of CO in Circadian Clock 97\u003cbr\u003e \u003ci\u003eHiroaki Kitagishi and Ikuko Sagami\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6 Carbon Monoxide and Mitochondria 108\u003cbr\u003e \u003ci\u003eClaude A. Piantadosi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7 Carbon Monoxide, Oxygen, and Pseudohypoxia 118\u003cbr\u003e \u003ci\u003eGrace E. Otterbein, Michael S. Tift, and Ghee Rye Lee\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8 Nitric Oxide in Human Physiology: Production, Regulation, and Interaction\u003c\/p\u003e \u003cp\u003ewith Carbon Monoxide Signaling 136\u003cbr\u003e \u003ci\u003eMaryam K. Mohammed and Brian S. Zuckerbraun\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9 When Carbon Monoxide Meets Hydrogen Sulfide 160\u003cbr\u003e \u003ci\u003eRui Wang Copyrighted Material\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10 Biliverdin and Bilirubin as Parallel Products of CO Formation: Not Just Bystanders 175\u003cbr\u003e \u003ci\u003eLibor Vitek\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection II Delivery Forms 195\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e11 Delivery Systems and Noncarrier Formulations 197\u003cbr\u003e \u003ci\u003eJames Byrne, Christoph Steiger, Jakob Wollborn, and Giovanni Traverso\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12 Metal-Based Carbon Monoxide-Releasing Molecules (CO-RMs) as Pharmacologically Active Therapeutics 203\u003cbr\u003e \u003ci\u003eRoberta Foresti, Djamal Eddine Benrahla, Shruti Mohan, and Roberto Motterlini\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13 Organic CO Donors that Rely on Photolysis for CO Release 223\u003cbr\u003e \u003ci\u003eYi Liao\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14 Organic Carbon Monoxide Prodrugs that Release CO Under Physiological Conditions 232\u003cbr\u003e \u003ci\u003eZhengnan Yuan and Binghe Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15 Targeted Delivery of Carbon Monoxide 259\u003cbr\u003e \u003ci\u003eLisa M. Berreau\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16 Anesthesia-Related Carbon Monoxide Exposure 286\u003cbr\u003e \u003ci\u003eRichard J. Levy\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17 Natural Products that Generate Carbon Monoxide: Chemistry and Nutritional Implications 302\u003cbr\u003e \u003ci\u003eLadie Kimberly De La Cruz and Binghe Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection III Carbon Monoxide Sensing and Scavenging 319\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e18 Fluorescent Probes for Intracellular Carbon Monoxide Detection 321\u003cbr\u003e \u003ci\u003eRyan R. Walvoord, Morgan R. Schneider, and Brian W. Michel\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection IV Therapeutic Applications 345\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e19 CO in Solid Organ Transplantation 347\u003cbr\u003e \u003ci\u003eRoberta Foresti, Roberto Motterlini, and Stephan Immenschuh\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20 Carbon Monoxide in Lung Injury and Disease 360\u003cbr\u003e \u003ci\u003eStefan W. Ryter\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21 Carbon Monoxide in Acute Brain Injury and Brain Protection 377\u003cbr\u003e \u003ci\u003eAlexandra Mazur, Madison Fangman, Rani Ashouri, Hannah Pamplin, Shruti Patel, and Sylvain Doré\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22 CO as a Protective Mediator of Liver Injury: The Role of PERK in HO-1\/ CO-Mediated Maintenance of Cellular Homeostasis in the Liver 385\u003cbr\u003e \u003ci\u003eYeonsoo Joe, Jeongmin Park, Mihyang Do, Stefan W. Ryter, Young-Joon Surh, Uh-Hyun Kim, and Hun Taeg Chung\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e23 CO and Cancer 401\u003cbr\u003e \u003ci\u003eJames N. Arnold and Joanne E. Anstee\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e24 CO and Diabetes 423\u003cbr\u003e \u003ci\u003eRebecca P. Chow and Hongjun Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e25 Carbon Monoxide and Acute Kidney Injury 434\u003cbr\u003e \u003ci\u003eMark de Caestecker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e26 CO as an Antiplatelet Agent: An Energy Metabolism Perspective 453\u003cbr\u003e \u003ci\u003ePatrycja Kaczara, Kamil Przyborowski, Roberto Motterlini, and Stefan Chlopicki\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e27 CO in Gastrointestinal Physiology and Protection 466\u003cbr\u003e \u003ci\u003eKatarzyna Magierowska and Marcin Magierowski\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e28 Carbon Monoxide and Sickle Cell Disease 482\u003cbr\u003e \u003ci\u003eEdward Gomperts, John Belcher, Howard Levy, and Greg Vercellotti\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e29 CO and Pain Management 497\u003cbr\u003e \u003ci\u003eOlga Pol\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e30 Clinical Trials of Low-Dose Carbon Monoxide 511\u003cbr\u003e \u003ci\u003eEdward Gomperts, Andrew Gomperts, and Howard Levy\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIndex 528\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407150391639,"sku":"9781119783404","price":170.1,"currency_code":"GBP","in_stock":false}]},{"product_id":"anthropology-of-violent-death-9781119806363","title":"Anthropology of Violent Death","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eAbout the editors, xiii\u003c\/p\u003e \u003cp\u003eAbout the contributors, xv\u003c\/p\u003e \u003cp\u003eForeword, xix\u003c\/p\u003e \u003cp\u003ePreface, xxiii\u003c\/p\u003e \u003cp\u003eSeries preface, xxvii\u003c\/p\u003e \u003cp\u003eAcknowledgments, xxix\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 The anthropology of violent death and the treatment of the bodies: an introduction, 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRoberto C. Parra and Douglas H. Ubelaker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 The posthumous dignity of dead persons, 1\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAntoon De Baets\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction: generations and posthumous dignity, 15\u003c\/p\u003e \u003cp\u003e2.2 The dead and posthumous dignity, 17\u003c\/p\u003e \u003cp\u003e2.3 Evidence for posthumous dignity, 18\u003c\/p\u003e \u003cp\u003e2.4 Duties flowing from posthumous dignity, 19\u003c\/p\u003e \u003cp\u003e2.5 The nature of posthumous dignity, 23\u003c\/p\u003e \u003cp\u003e2.6 Semantic debates about posthumous dignity, 25\u003c\/p\u003e \u003cp\u003e2.7 Breaches of posthumous dignity, 26\u003c\/p\u003e \u003cp\u003e2.8 Restoration of posthumous dignity, 28\u003c\/p\u003e \u003cp\u003e2.9 Conclusion: the impact of posthumous dignity, 31\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Continuing bonds and social memory: absence--presence, 39\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAvril Maddrell\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 What are continuing bonds and how are they experienced and expressed?, 39\u003c\/p\u003e \u003cp\u003e3.2 Continuing bonds and the well-being of mourners, 43\u003c\/p\u003e \u003cp\u003e3.3 Implications for professional service providers, 46\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 The archaeology of disappearance, 49\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAlfredo González-Ruibal\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction, 49\u003c\/p\u003e \u003cp\u003e4.2 Disappearance and power: concealment, dispersal, and virtualization, 51\u003c\/p\u003e \u003cp\u003e4.3 Material disappearance, human disappearance, 55\u003c\/p\u003e \u003cp\u003e4.4 The disappearance of disappearance, 58\u003c\/p\u003e \u003cp\u003e4.5 Concluding Remarks, 62\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Bioarchaeology of violent death, 67\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAnna Osterholtz, Debra Martin and Ryan Harrod\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction and background, 67\u003c\/p\u003e \u003cp\u003e5.2 Categories of group-level violent death, 70\u003c\/p\u003e \u003cp\u003e5.2.1 Bioarchaeology of Massacres, 70\u003c\/p\u003e \u003cp\u003e5.3 Case studies illustrating integrative approaches to massacres in the past, 70\u003c\/p\u003e \u003cp\u003e5.4 Differentiating between kratophanous violence and ritualized death, 77\u003c\/p\u003e \u003cp\u003e5.5 Conclusions, 81\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Destruction, mass violence, and human remains: Dealing with dead bodies as a \"total social phenomenon\", 91\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eÉlisabeth Anstett\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction, 91\u003c\/p\u003e \u003cp\u003e6.2 Understanding the forms taken by the Forensic Turn, and its effects, 93\u003c\/p\u003e \u003cp\u003e6.3 Understanding the genealogy of professional practices of disinterment, 98\u003c\/p\u003e \u003cp\u003e6.4 The blind spots of a total social phenomenon of great complexity, 102\u003c\/p\u003e \u003cp\u003e6.5 Conclusion, 103\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Kill, kill again and destroy: when death is not enough, 109\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eRoberto C. Parra, Digna M. Vigo-Corea and Pierre Perich\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction, 109\u003c\/p\u003e \u003cp\u003e7.2 Dehumanizing, 111\u003c\/p\u003e \u003cp\u003e7.3 When death is not enough, 114\u003c\/p\u003e \u003cp\u003e7.4 Dismembering\/mutilating: the perspective from culture, 121\u003c\/p\u003e \u003cp\u003e7.5 Conclusions, 126\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Mourning violent deaths and disappearances, 133\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAntonius C. G. M. Robben\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction, 133\u003c\/p\u003e \u003cp\u003e8.2 The conflictive mourning of the dead and missing after the First World War, 134\u003c\/p\u003e \u003cp\u003e8.3 Enduring bonds of the living, the dead, and the disappeared in Argentina, 138\u003c\/p\u003e \u003cp\u003e8.4 Oscillatory mourning of the dead and the disappeared by the bereaved, 142\u003c\/p\u003e \u003cp\u003e8.5 Conclusion, 147\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Whose humanitarianism, whose forensic anthropology?, 153\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJaymelee J. Kim and Adam Rosenblatt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction, 153\u003c\/p\u003e \u003cp\u003e9.2 Positionality of the authors, 155\u003c\/p\u003e \u003cp\u003e9.3 Reconceptualizing violent deaths, 156\u003c\/p\u003e \u003cp\u003e9.4 The dead as articipants in forensic anthropology, 158\u003c\/p\u003e \u003cp\u003e9.5 What's missing from human rights, 166\u003c\/p\u003e \u003cp\u003e9.6 The continued expansion of forensic anthropology, 169\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Battlefields and killed in action: tombs of the unknown soldier and commemoration, 177\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eLaura Wittman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction, 177\u003c\/p\u003e \u003cp\u003e10.2 Tomb of the unknown soldier, 178\u003c\/p\u003e \u003cp\u003e10.3 Mutilated victory, 182\u003c\/p\u003e \u003cp\u003e10.4 As an Epilogue, 190\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Mass grave protection and missing persons, 197\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eMelanie Klinkner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction, 197\u003c\/p\u003e \u003cp\u003e11.2 Missing persons in mass graves: a worldwide phenomenon, 198\u003c\/p\u003e \u003cp\u003e11.3 The legal framework for mass grave protection, 201\u003c\/p\u003e \u003cp\u003e11.4 Practicalities of protection, 208\u003c\/p\u003e \u003cp\u003e11.5 Protection on a global scale, 210\u003c\/p\u003e \u003cp\u003e11.6 Conclusion: the need to do better, 213\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Respect for the dead under international law and Islamic law in armed conflicts, 219\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eAhmed Al-Dawoody and Alexandra Ortiz Signoret\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction, 219\u003c\/p\u003e \u003cp\u003e12.2 The Legal Framework, 220\u003c\/p\u003e \u003cp\u003e12.3 Search for, Collect, and Evacuate the Dead without Adverse Distinction, 221\u003c\/p\u003e \u003cp\u003e12.4 Identification and Recording of Information on the Dead, 224\u003c\/p\u003e \u003cp\u003e12.5 Respecting the Dead and Dignified Treatment, 226\u003c\/p\u003e \u003cp\u003e12.6 Respectful Disposal of the Dead, 229\u003c\/p\u003e \u003cp\u003e12.7 Gravesites and Other Locations of Mortal Remains, 233\u003c\/p\u003e \u003cp\u003e12.8 Exhumations, 234\u003c\/p\u003e \u003cp\u003e12.9 Return of Human Remains and Personal Effects of the Dead, 236\u003c\/p\u003e \u003cp\u003e12.10 Conclusion, 239\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Unmaking forgotten mass graves and honorable burial: engaging with the spanish civil war legacy, 251\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eFrancisco Ferrándiz\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Overture, 251\u003c\/p\u003e \u003cp\u003e13.2 On Funerary Militarism, 252\u003c\/p\u003e \u003cp\u003e13.3 Franco's Militarist Imprint Under Siege, 256\u003c\/p\u003e \u003cp\u003e13.4 Unmaking the Generalissimo's Burial, 262\u003c\/p\u003e \u003cp\u003e13.5 Military disassemblage, 269\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Dealing with bad death in post-conflict societies: forensic devices, burials of exhumed remains, and mourning processes in Peru, 277\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eValérie Robin-Azevedo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Models for dealing with death: morphologies of \"good death\" and \"bad death\", 277\u003c\/p\u003e \u003cp\u003e14.2 Contexts of mass violence through the lens of bad death, 278\u003c\/p\u003e \u003cp\u003e14.3 Transitional justice, the forensic turn, and the \"dignified burial\": can we reverse bad death?, 280\u003c\/p\u003e \u003cp\u003e14.4 From the necropolitics to the necrogovernamentality of the Peruvian state, 281\u003c\/p\u003e \u003cp\u003e14.5 Exhumation of mass graves and the reactivation of bad death in the Andes, 284\u003c\/p\u003e \u003cp\u003e14.6 The task of identification or the process of rehumanization of ill-treated bodies, 287\u003c\/p\u003e \u003cp\u003e14.7 The uncertain dates and stretched time of bad death, 291\u003c\/p\u003e \u003cp\u003e14.8 Body substitutes in the absence of any trace of remains, 293\u003c\/p\u003e \u003cp\u003e14.9 Conclusion, 295\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Migrant death and the ethics of visual documentation in forensic anthropology, 303\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eKrista E. Latham, Alyson J. O'Daniel and Tanya Ramos\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction, 303\u003c\/p\u003e \u003cp\u003e15.2 Disciplinary ethics and social change: contextualizingforensic anthropology practices, 304\u003c\/p\u003e \u003cp\u003e15.3 Methods and scope, 309\u003c\/p\u003e \u003cp\u003e15.4 Making the case for a more socially aware practice of forensic anthropology, 318\u003c\/p\u003e \u003cp\u003e15.5 Closing, 320\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Bedeviling binaries: an integrated and dialectical approach to forensicanthropology in northern Uganda, 327\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eTricia Redeker Hepner and Dawnie W. Steadman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction, 327\u003c\/p\u003e \u003cp\u003e16.2 Restless spirits and human remains in Acholiland, Uganda, 329\u003c\/p\u003e \u003cp\u003e16.3 The integrated approach, 336\u003c\/p\u003e \u003cp\u003e16.4 To excavate or not to excavate?, 340\u003c\/p\u003e \u003cp\u003e16.5 Conclusion: from binary to dialectical relationships, 344\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Guiding principles for the dignified management of the dead in humanitarian emergencies and to prevent them from becoming missing persons, 351\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eStephen Cordner and Morris Tidball-Binz\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Why the need for these principles?, 351\u003c\/p\u003e \u003cp\u003e17.2 To whom are the guiding principles addressed?, 354\u003c\/p\u003e \u003cp\u003e17.3 Setting the scene, 355\u003c\/p\u003e \u003cp\u003e17.4 The preamble to the Guiding Principles, 360\u003c\/p\u003e \u003cp\u003e17.5 The Guiding Principles, 362\u003c\/p\u003e \u003cp\u003e17.6 The process of producing the Guiding Principles, 369\u003c\/p\u003e \u003cp\u003e17.7 Conclusions, 369\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Epilog: Anthropology of violent death and forensic humanitarian action, 375\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eDouglas H. Ubelaker and Roberto C. Parra\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Humanity and its less violent reactions?, 375\u003c\/p\u003e \u003cp\u003e18.2 Anthropology applied to forensic sciences and the notion of anthropology of violent death in the humanitarian context, 377\u003c\/p\u003e \u003cp\u003eNote 382\u003c\/p\u003e \u003cp\u003eReferences 383\u003c\/p\u003e \u003cp\u003eIndex, 385\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407158518103,"sku":"9781119806363","price":117.0,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119806363.jpg?v=1730498376"},{"product_id":"a-guide-to-virology-for-engineers-and-applied-scientists-9781119853138","title":"A Guide to Virology for Engineers and Applied","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003ePreface xvii\u003c\/p\u003e \u003cp\u003eAbout the Authors xix\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart I Introduction to Viruses 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Overview of Molecular Biology 3\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eContributing Author: Sarah Forster\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Cell Basics 4\u003c\/p\u003e \u003cp\u003e1.1.1 Cytoplasm 5\u003c\/p\u003e \u003cp\u003e1.1.2 Ribosomes 5\u003c\/p\u003e \u003cp\u003e1.1.3 Nucleus 6\u003c\/p\u003e \u003cp\u003e1.2 Cell Replication 6\u003c\/p\u003e \u003cp\u003e1.2.1 Nucleic Acids 6\u003c\/p\u003e \u003cp\u003e1.2.2 DNA Replication 7\u003c\/p\u003e \u003cp\u003e1.2.3 RNA Structure and Role 9\u003c\/p\u003e \u003cp\u003e1.2.4 Protein Synthesis 9\u003c\/p\u003e \u003cp\u003e1.3 Cellular Transport 11\u003c\/p\u003e \u003cp\u003e1.3.1 Plasma Membrane 11\u003c\/p\u003e \u003cp\u003e1.3.2 Cell Signaling 11\u003c\/p\u003e \u003cp\u003e1.4 Immune Defense 12\u003c\/p\u003e \u003cp\u003e1.4.1 Innate Immunity 12\u003c\/p\u003e \u003cp\u003e1.4.2 Adaptive Immunity 13\u003c\/p\u003e \u003cp\u003e1.4.2.1 Humoral Immunity 13\u003c\/p\u003e \u003cp\u003e1.4.2.2 Cellular Immunity 14\u003c\/p\u003e \u003cp\u003e1.5 Applications 14\u003c\/p\u003e \u003cp\u003e1.6 Chapter Summary 16\u003c\/p\u003e \u003cp\u003e1.7 Problems 16\u003c\/p\u003e \u003cp\u003eReferences 16\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Basics of Virology 19\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e2.1 Viral Basics and Terminology 19\u003c\/p\u003e \u003cp\u003e2.2 Viral Life Cycle 21\u003c\/p\u003e \u003cp\u003e2.2.1 Attachment (Connection) 21\u003c\/p\u003e \u003cp\u003e2.2.2 Penetration (Entry) 22\u003c\/p\u003e \u003cp\u003e2.2.3 Uncoating 22\u003c\/p\u003e \u003cp\u003e2.2.4 Replication 23\u003c\/p\u003e \u003cp\u003e2.2.5 Assembly 23\u003c\/p\u003e \u003cp\u003e2.2.6 Maturation and Release 23\u003c\/p\u003e \u003cp\u003e2.3 Virus Structure and Classification 24\u003c\/p\u003e \u003cp\u003e2.3.1 DNA Viruses 25\u003c\/p\u003e \u003cp\u003e2.3.2 RNA Viruses 25\u003c\/p\u003e \u003cp\u003e2.3.3 Reverse Transcription Viruses (Retroviruses) 27\u003c\/p\u003e \u003cp\u003e2.4 Viruses in Context of the Tree of Life 27\u003c\/p\u003e \u003cp\u003e2.5 Viral Genetics 28\u003c\/p\u003e \u003cp\u003e2.5.1 Antigenic Shift 28\u003c\/p\u003e \u003cp\u003e2.5.2 Antigenic Drift 29\u003c\/p\u003e \u003cp\u003e2.5.3 Phenotypic Mixing 29\u003c\/p\u003e \u003cp\u003e2.5.4 Complementation 29\u003c\/p\u003e \u003cp\u003e2.6 Applications 29\u003c\/p\u003e \u003cp\u003e2.7 Chapter Summary 31\u003c\/p\u003e \u003cp\u003e2.8 Problems 31\u003c\/p\u003e \u003cp\u003eReferences 32\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Pandemics, Epidemics, and Outbreaks 33\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e3.1 Human Viral Diseases 34\u003c\/p\u003e \u003cp\u003e3.2 Ebola and Marburg Viruses 35\u003c\/p\u003e \u003cp\u003e3.2.1 Symptoms 36\u003c\/p\u003e \u003cp\u003e3.2.2 Diagnosis 37\u003c\/p\u003e \u003cp\u003e3.2.3 Prevention and Treatment 37\u003c\/p\u003e \u003cp\u003e3.3 Human Immunodeficiency Disease (HIV) 38\u003c\/p\u003e \u003cp\u003e3.3.1 HIV Symptoms 39\u003c\/p\u003e \u003cp\u003e3.3.1.1 Stage 1: Acute Infection 39\u003c\/p\u003e \u003cp\u003e3.3.1.2 Stage 2: Chronic HIV Infection (Latent Phase) 39\u003c\/p\u003e \u003cp\u003e3.3.1.3 Stage 3: Acquired Immunodeficiency Syndrome (AIDS) 39\u003c\/p\u003e \u003cp\u003e3.3.2 Diagnosis 40\u003c\/p\u003e \u003cp\u003e3.3.3 HIV Prevention and Treatment 40\u003c\/p\u003e \u003cp\u003e3.4 Influenza 41\u003c\/p\u003e \u003cp\u003e3.4.1 Influenza Symptoms 41\u003c\/p\u003e \u003cp\u003e3.4.2 Influenza Diagnosis 42\u003c\/p\u003e \u003cp\u003e3.4.3 Influenza Prevention and Treatment 42\u003c\/p\u003e \u003cp\u003e3.4.4 Influenza Pandemics 43\u003c\/p\u003e \u003cp\u003e3.5 Coronaviruses 44\u003c\/p\u003e \u003cp\u003e3.5.1 Symptoms 45\u003c\/p\u003e \u003cp\u003e3.5.1.1 Typical Acute Symptoms 45\u003c\/p\u003e \u003cp\u003e3.5.1.2 Post-COVID Conditions 46\u003c\/p\u003e \u003cp\u003e3.5.1.3 COVID-19 Multiorgan System Effects (MIS) 46\u003c\/p\u003e \u003cp\u003e3.5.2 COVID-19 Diagnosis 47\u003c\/p\u003e \u003cp\u003e3.5.3 COVID-19 Prevention and treatment 48\u003c\/p\u003e \u003cp\u003e3.6 Current and Emerging Viral Threats 48\u003c\/p\u003e \u003cp\u003e3.7 Applications 51\u003c\/p\u003e \u003cp\u003e3.8 Chapter Summary 52\u003c\/p\u003e \u003cp\u003e3.9 Problems 53\u003c\/p\u003e \u003cp\u003eReferences 53\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Virus Prevention, Diagnosis, and Treatment 57\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e4.1 Vaccination Successes and Challenges 58\u003c\/p\u003e \u003cp\u003e4.2 Current Vaccine Technology 59\u003c\/p\u003e \u003cp\u003e4.2.1 Live-attenuated vaccines 60\u003c\/p\u003e \u003cp\u003e4.2.2 Inactivated vaccines 61\u003c\/p\u003e \u003cp\u003e4.2.3 Recombinant Subunit Vaccines 61\u003c\/p\u003e \u003cp\u003e4.2.4 Viral Vector Vaccines 62\u003c\/p\u003e \u003cp\u003e4.2.5 Messenger RNA (mRNA) Vaccines 62\u003c\/p\u003e \u003cp\u003e4.3 U.S.-Approved Vaccines and Requirements 63\u003c\/p\u003e \u003cp\u003e4.3.1 Commercially Available Viral Vaccines 63\u003c\/p\u003e \u003cp\u003e4.3.2 Vaccination Requirements 63\u003c\/p\u003e \u003cp\u003e4.4 Viral Testing and Diagnosis 64\u003c\/p\u003e \u003cp\u003e4.4.1 Viral Testing 65\u003c\/p\u003e \u003cp\u003e4.4.2 Antibody Testing 66\u003c\/p\u003e \u003cp\u003e4.5 Antiviral Treatment Options 66\u003c\/p\u003e \u003cp\u003e4.5.1 HIV 67\u003c\/p\u003e \u003cp\u003e4.5.1.1 Nucleoside Reverse Transcriptase Inhibitors (NRTIs) 67\u003c\/p\u003e \u003cp\u003e4.5.1.2 Non-nucleoside Reverse Transcriptase Inhibitors (NNRTIs) 67\u003c\/p\u003e \u003cp\u003e4.5.1.3 Protease Inhibitors (PIs) 67\u003c\/p\u003e \u003cp\u003e4.5.1.4 Fusion Inhibitors (FIs) 67\u003c\/p\u003e \u003cp\u003e4.5.1.5 Integrase Strand Transfer Inhibitors (INSTIs) 67\u003c\/p\u003e \u003cp\u003e4.5.1.6 CCR5 Antagonists 67\u003c\/p\u003e \u003cp\u003e4.5.1.7 Attachment Inhibitors 68\u003c\/p\u003e \u003cp\u003e4.5.1.8 Post-Attachment Inhibitors 68\u003c\/p\u003e \u003cp\u003e4.5.1.9 Pharmacokinetic Enhancers 68\u003c\/p\u003e \u003cp\u003e4.5.2 Influenza 68\u003c\/p\u003e \u003cp\u003e4.5.3 Hepatitis C virus (HCV) 68\u003c\/p\u003e \u003cp\u003e4.5.4 Other Treatment Options 69\u003c\/p\u003e \u003cp\u003e4.6 Applications 70\u003c\/p\u003e \u003cp\u003e4.7 Chapter Summary 71\u003c\/p\u003e \u003cp\u003e4.8 Problems 72\u003c\/p\u003e \u003cp\u003eReferences 72\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Safety Protocols and Personal Protection Equipment 75\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eContributing Author: Emma Parente\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Regulations and Oversight of Safety Protocols 76\u003c\/p\u003e \u003cp\u003e5.2 Protective and Safety Systems 76\u003c\/p\u003e \u003cp\u003e5.2.1 Personal Protective Devices and Practices 76\u003c\/p\u003e \u003cp\u003e5.2.2 Antimicrobial Suppression And Eradication 77\u003c\/p\u003e \u003cp\u003e5.3 Disinfection Categories and Procedures 78\u003c\/p\u003e \u003cp\u003e5.4 Occupational Health and Safety Administration Hazmat Regulations 79\u003c\/p\u003e \u003cp\u003e5.4.1 HAZMAT Level A Protection 80\u003c\/p\u003e \u003cp\u003e5.4.2 HAZMAT Level B Protection 81\u003c\/p\u003e \u003cp\u003e5.4.3 Level C Protection 82\u003c\/p\u003e \u003cp\u003e5.4.4 Level D Protection 83\u003c\/p\u003e \u003cp\u003e5.5 Bio Level Safety and Security 83\u003c\/p\u003e \u003cp\u003e5.6 COVID-Related Safety Precautions 84\u003c\/p\u003e \u003cp\u003e5.6.1 Personal Protective Equipment 84\u003c\/p\u003e \u003cp\u003e5.6.2 Transmission Control 85\u003c\/p\u003e \u003cp\u003e5.7 Applications 85\u003c\/p\u003e \u003cp\u003e5.8 Summary 87\u003c\/p\u003e \u003cp\u003e5.9 Problems 87\u003c\/p\u003e \u003cp\u003eReferences 88\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Epidemiology and Virus Transmission 91\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e6.1 Overview of Epidemiology 92\u003c\/p\u003e \u003cp\u003e6.2 Government Agencies’ Contributions to Public Health 94\u003c\/p\u003e \u003cp\u003e6.2.1 The Role of the Centers for Disease Control and Prevention (CDC) 94\u003c\/p\u003e \u003cp\u003e6.2.2 The World Health Organization (WHO): Successes and Challenges 95\u003c\/p\u003e \u003cp\u003e6.3 Epidemiologic Study Design 96\u003c\/p\u003e \u003cp\u003e6.3.1 Outbreak Case Example 98\u003c\/p\u003e \u003cp\u003e6.3.2 Clinical Trials 99\u003c\/p\u003e \u003cp\u003e6.4 Virus Transmission 100\u003c\/p\u003e \u003cp\u003e6.4.1 Modes of Transmission 101\u003c\/p\u003e \u003cp\u003e6.5 Applications 102\u003c\/p\u003e \u003cp\u003e6.6 Chapter Summary 104\u003c\/p\u003e \u003cp\u003e6.7 Problems 105\u003c\/p\u003e \u003cp\u003eReferences 105\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II Practical and Technical Considerations 109\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Engineering Principles and Fundamentals 111\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eContributing Author: Vishal Bhatty\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 History of Engineering 112\u003c\/p\u003e \u003cp\u003e7.2 Problem Solving: The Engineering Approach 113\u003c\/p\u003e \u003cp\u003e7.2.1 Problem-Solving Methodology 114\u003c\/p\u003e \u003cp\u003e7.2.2 Engineering and Scientific Sources 115\u003c\/p\u003e \u003cp\u003e7.3 Units and Conversion Constants 115\u003c\/p\u003e \u003cp\u003e7.3.1 The Metric System 115\u003c\/p\u003e \u003cp\u003e7.3.2 The SI System 117\u003c\/p\u003e \u003cp\u003e7.4 Dimensional Analysis 117\u003c\/p\u003e \u003cp\u003e7.5 Process Variables 119\u003c\/p\u003e \u003cp\u003e7.6 The Conservation Laws 121\u003c\/p\u003e \u003cp\u003e7.7 Thermodynamics and Kinetics 125\u003c\/p\u003e \u003cp\u003e7.8 Applications 126\u003c\/p\u003e \u003cp\u003e7.9 Chapter Summary 130\u003c\/p\u003e \u003cp\u003e7.10 Problems 130\u003c\/p\u003e \u003cp\u003eReferences 131\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Legal and Regulatory Considerations 133\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e8.1 The Regulatory System 134\u003c\/p\u003e \u003cp\u003e8.1.1 Laws, Regulations, Plans and policy: The Differences 135\u003c\/p\u003e \u003cp\u003e8.1.2 Policies and Plans 137\u003c\/p\u003e \u003cp\u003e8.2 The Role of Individual States 138\u003c\/p\u003e \u003cp\u003e8.3 Key Government Agencies 140\u003c\/p\u003e \u003cp\u003e8.3.1 Environmental Protection Agency (EPA) 140\u003c\/p\u003e \u003cp\u003e8.3.2 Centers for Disease Control and Prevention (CDC) 141\u003c\/p\u003e \u003cp\u003e8.3.3 Food and Drug Administration (FDA) 141\u003c\/p\u003e \u003cp\u003e8.3.4 Occupational Health and Safety Administration (OSHA) 141\u003c\/p\u003e \u003cp\u003e8.3.5 Legal Considerations during a Public Health Crisis 142\u003c\/p\u003e \u003cp\u003e8.4 Public Health Emergency Declarations 143\u003c\/p\u003e \u003cp\u003e8.5 Key Environmental Acts 145\u003c\/p\u003e \u003cp\u003e8.6 The Clean Air Act 145\u003c\/p\u003e \u003cp\u003e8.7 Regulation of Toxic Substances 147\u003c\/p\u003e \u003cp\u003e8.7.1 Toxic Water Pollutants: Control and Classification 150\u003c\/p\u003e \u003cp\u003e8.7.2 Drinking Water 150\u003c\/p\u003e \u003cp\u003e8.7.3 Surface Water Treatment Rules (SWTR) 151\u003c\/p\u003e \u003cp\u003e8.8 Regulations Governing Infectious Diseases 153\u003c\/p\u003e \u003cp\u003e8.8.1 Vaccination Laws 155\u003c\/p\u003e \u003cp\u003e8.8.2 State Healthcare Worker and Patient Vaccination Laws 155\u003c\/p\u003e \u003cp\u003e8.8.3 State-Mandated Childhood Vaccinations 155\u003c\/p\u003e \u003cp\u003e8.9 Applications 155\u003c\/p\u003e \u003cp\u003e8.10 Chapter Summary 159\u003c\/p\u003e \u003cp\u003e8.11 Problems 159\u003c\/p\u003e \u003cp\u003eReferences 160\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Emergency Planning and Response 163\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e9.1 The Importance of Emergency Planning and Response 164\u003c\/p\u003e \u003cp\u003e9.2 Planning for Emergencies 166\u003c\/p\u003e \u003cp\u003e9.2.1 Preparedness Training 166\u003c\/p\u003e \u003cp\u003e9.3 Plan Implementation 167\u003c\/p\u003e \u003cp\u003e9.3.1 Notification of Public and Regulatory Officials 168\u003c\/p\u003e \u003cp\u003e9.4 EP\u0026amp;R for Epidemics and Pandemics 169\u003c\/p\u003e \u003cp\u003e9.4.1 Federal Public Health and Medical Emergency Preparedness 170\u003c\/p\u003e \u003cp\u003e9.4.2 Emergency Operations Center 170\u003c\/p\u003e \u003cp\u003e9.4.3 Disease Containment 172\u003c\/p\u003e \u003cp\u003e9.4.4 Public Notification of Pandemic Quarantines and Lockdowns 173\u003c\/p\u003e \u003cp\u003e9.4.5 The National Strategy for Pandemic Influenza (NSPI) 173\u003c\/p\u003e \u003cp\u003e9.5 EP\u0026amp;R for Industrial Accidents 174\u003c\/p\u003e \u003cp\u003e9.5.1 Emergency Planning and Community Right-to-Know Act (epcra) 175\u003c\/p\u003e \u003cp\u003e9.5.2 The Planning Committee 177\u003c\/p\u003e \u003cp\u003e9.6 EP\u0026amp;R for Natural Disasters 179\u003c\/p\u003e \u003cp\u003e9.7 Current and Future Trends 181\u003c\/p\u003e \u003cp\u003e9.8 Applications 181\u003c\/p\u003e \u003cp\u003e9.9 Chapter Summary 184\u003c\/p\u003e \u003cp\u003e9.10 Problems 184\u003c\/p\u003e \u003cp\u003eReferences 185\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Ethical Considerations within Virology 189\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eContributing Author: Paul DiGaetano, Jr.\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Core Ethics Principles 190\u003c\/p\u003e \u003cp\u003e10.2 Important Tenets of Ethical Research 191\u003c\/p\u003e \u003cp\u003e10.2.1 Conducting Research During a Health Crisis 192\u003c\/p\u003e \u003cp\u003e10.2.2 Scientific Cooperation During a Health Crisis 192\u003c\/p\u003e \u003cp\u003e10.2.3 Fair and Ethical Study Design and Implementation 193\u003c\/p\u003e \u003cp\u003e10.3 Ethical Dilemmas in Public Health 193\u003c\/p\u003e \u003cp\u003e10.3.1 Public Health Surveillance 193\u003c\/p\u003e \u003cp\u003e10.3.2 Ethical Evaluation of Nonpharmaceutical Interventions 195\u003c\/p\u003e \u003cp\u003e10.3.3 Ethical Consideration Involving Restrictions of Movement 197\u003c\/p\u003e \u003cp\u003e10.4 Ethical Considerations Regarding Medical Interventions 199\u003c\/p\u003e \u003cp\u003e10.4.1 Emergency Use Of Medical Interventions 200\u003c\/p\u003e \u003cp\u003e10.5 Applications 201\u003c\/p\u003e \u003cp\u003e10.6 Chapter Summary 202\u003c\/p\u003e \u003cp\u003e10.7 Problems 203\u003c\/p\u003e \u003cp\u003eReferences 203\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Health and Hazard Risk Assessment 205\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction to Risk Assessment 207\u003c\/p\u003e \u003cp\u003e11.2 The Health Risk Assessment Process 209\u003c\/p\u003e \u003cp\u003e11.3 Dose–Response Assessment 211\u003c\/p\u003e \u003cp\u003e11.4 The Hazard Risk Assessment Process 213\u003c\/p\u003e \u003cp\u003e11.5 Hazard Risk Versus Health Risk 214\u003c\/p\u003e \u003cp\u003e11.5.1 Health Risk Assessment (HRA) Example 215\u003c\/p\u003e \u003cp\u003e11.5.2 Hazard Risk Assessment (HRZA) Example 215\u003c\/p\u003e \u003cp\u003e11.6 COVID-19 Pandemic Hazard Risk 216\u003c\/p\u003e \u003cp\u003e11.7 The Uncertainty Factor 217\u003c\/p\u003e \u003cp\u003e11.8 Applications 218\u003c\/p\u003e \u003cp\u003e11.9 Chapter Summary 220\u003c\/p\u003e \u003cp\u003e11.10 Problems 220\u003c\/p\u003e \u003cp\u003eReferences 221\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III Engineering Considerations 223\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Introduction to Mathematical Methods 225\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eContributing Author: Julian Theodore\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Differentiation 226\u003c\/p\u003e \u003cp\u003e12.2 Integration 228\u003c\/p\u003e \u003cp\u003e12.2.1 The Trapezoidal Rule 228\u003c\/p\u003e \u003cp\u003e12.2.2 Simpson’s Rule 229\u003c\/p\u003e \u003cp\u003e12.3 Simultaneous Linear Algebraic Equations 230\u003c\/p\u003e \u003cp\u003e12.3.1 Gauss–Jordan Reduction 231\u003c\/p\u003e \u003cp\u003e12.3.2 Gauss Elimination 232\u003c\/p\u003e \u003cp\u003e12.3.3 Gauss–Seidel Approach 232\u003c\/p\u003e \u003cp\u003e12.4 Nonlinear Algebraic Equations 233\u003c\/p\u003e \u003cp\u003e12.5 Ordinary Differential Equations 234\u003c\/p\u003e \u003cp\u003e12.6 Partial Differential Equations 237\u003c\/p\u003e \u003cp\u003e12.7 Applications 237\u003c\/p\u003e \u003cp\u003e12.8 Chapter Summary 240\u003c\/p\u003e \u003cp\u003e12.9 Problems 240\u003c\/p\u003e \u003cp\u003eReferences 241\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Probability and Statistical Principles 243\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e13.1 Probability Definitions and Interpretations 244\u003c\/p\u003e \u003cp\u003e13.2 Introduction to Probability Distributions 246\u003c\/p\u003e \u003cp\u003e13.3 Discrete Probability Distributions 247\u003c\/p\u003e \u003cp\u003e13.3.1 The Binomial Distribution 248\u003c\/p\u003e \u003cp\u003e13.3.2 Multinomial Distribution 248\u003c\/p\u003e \u003cp\u003e13.3.3 Hypergeometric Distribution 249\u003c\/p\u003e \u003cp\u003e13.3.4 Poisson Distribution 250\u003c\/p\u003e \u003cp\u003e13.4 Continuous Probability Distributions 250\u003c\/p\u003e \u003cp\u003e13.4.1 Measures of Central Tendency and Scatter 251\u003c\/p\u003e \u003cp\u003e13.4.2 The Normal Distribution 252\u003c\/p\u003e \u003cp\u003e13.4.3 The Lognormal Distribution 256\u003c\/p\u003e \u003cp\u003e13.4.4 The Exponential Distribution 257\u003c\/p\u003e \u003cp\u003e13.4.5 The Weibull Distribution 258\u003c\/p\u003e \u003cp\u003e13.5 Contemporary Statistics 259\u003c\/p\u003e \u003cp\u003e13.5.1 Confidence Intervals for Means 260\u003c\/p\u003e \u003cp\u003e13.5.2 Confidence Intervals for Proportions 260\u003c\/p\u003e \u003cp\u003e13.5.3 Hypothesis Testing 261\u003c\/p\u003e \u003cp\u003e13.5.4 Hypothesis Test for Means and Proportions 261\u003c\/p\u003e \u003cp\u003e13.5.5 The F Distribution 262\u003c\/p\u003e \u003cp\u003e13.5.6 Analysis of Variance (ANOVA) 262\u003c\/p\u003e \u003cp\u003e13.5.7 Nonparametric Tests 264\u003c\/p\u003e \u003cp\u003e13.6 Applications 264\u003c\/p\u003e \u003cp\u003e13.7 Chapter Summary 268\u003c\/p\u003e \u003cp\u003e13.8 Problems 268\u003c\/p\u003e \u003cp\u003eReferences 269\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Linear Regression 271\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e14.1 Rectangular Coordinates 272\u003c\/p\u003e \u003cp\u003e14.2 Logarithmic Coordinates 273\u003c\/p\u003e \u003cp\u003e14.3 Methods of Plotting Data 275\u003c\/p\u003e \u003cp\u003e14.4 Scatter Diagrams 275\u003c\/p\u003e \u003cp\u003e14.5 Curve Fitting 278\u003c\/p\u003e \u003cp\u003e14.6 Method of Least Squares 280\u003c\/p\u003e \u003cp\u003e14.7 Applications 284\u003c\/p\u003e \u003cp\u003e14.8 Chapter Summary 287\u003c\/p\u003e \u003cp\u003e14.9 Problems 288\u003c\/p\u003e \u003cp\u003eReferences 288\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Ventilation 289\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction to Industrial Ventilation Systems 290\u003c\/p\u003e \u003cp\u003e15.2 Components of Ventilation Systems 291\u003c\/p\u003e \u003cp\u003e15.3 Fans, Valves and Fittings, and Ductwork 293\u003c\/p\u003e \u003cp\u003e15.3.1 Fans 293\u003c\/p\u003e \u003cp\u003e15.3.2 Valves and Fittings 295\u003c\/p\u003e \u003cp\u003e15.4 Selecting Ventilation Systems 296\u003c\/p\u003e \u003cp\u003e15.5 Key Process Equations 298\u003c\/p\u003e \u003cp\u003e15.5.1 Regarding Friction Losses 299\u003c\/p\u003e \u003cp\u003e15.6 Ventilation Models 300\u003c\/p\u003e \u003cp\u003e15.7 Model Limitations 302\u003c\/p\u003e \u003cp\u003e15.8 Infection Control Implications 303\u003c\/p\u003e \u003cp\u003e15.9 Applications 305\u003c\/p\u003e \u003cp\u003e15.10 Chapter Summary 309\u003c\/p\u003e \u003cp\u003e15.11 Problems 310\u003c\/p\u003e \u003cp\u003eReferences 310\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Pandemic Health Data Modeling 313\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e16.1 COVID-19: A Rude Awakening 315\u003c\/p\u003e \u003cp\u003e16.2 Earlier Work 316\u003c\/p\u003e \u003cp\u003e16.3 Planning for Pandemics 318\u003c\/p\u003e \u003cp\u003e16.4 Generating Mathematical Models 319\u003c\/p\u003e \u003cp\u003e16.5 Pandemic Health Data Models 324\u003c\/p\u003e \u003cp\u003e16.6 In Review 329\u003c\/p\u003e \u003cp\u003e16.7 Applications 331\u003c\/p\u003e \u003cp\u003e16.8 Chapter Summary 338\u003c\/p\u003e \u003cp\u003e16.9 Problems 338\u003c\/p\u003e \u003cp\u003eReferences 339\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Optimization Procedures 341\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e17.1 The History of Optimization 342\u003c\/p\u003e \u003cp\u003e17.2 The Scope of Optimization 344\u003c\/p\u003e \u003cp\u003e17.3 Conventional Optimization Procedures 346\u003c\/p\u003e \u003cp\u003e17.4 Analytical Fomulation of the Optimum 347\u003c\/p\u003e \u003cp\u003e17.5 Contemporary Optimization: Concepts in Linear Programming 350\u003c\/p\u003e \u003cp\u003e17.6 Applied Concepts in Linear Programming 351\u003c\/p\u003e \u003cp\u003e17.7 Applications 355\u003c\/p\u003e \u003cp\u003e17.8 Chapter Summary 357\u003c\/p\u003e \u003cp\u003e17.9 Problems 358\u003c\/p\u003e \u003cp\u003eReferences 359\u003c\/p\u003e \u003cp\u003eIndex 361\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49407172804951,"sku":"9781119853138","price":97.85,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781119853138.jpg?v=1730498430"}],"url":"https:\/\/bookcurl.com\/collections\/chemical-biology.oembed?page=3","provider":"Book Curl","version":"1.0","type":"link"}