{"product_id":"recent-advances-in-polyphenol-research-04-9781118329672","title":"Recent Advances in Polyphenol Research 04","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003ePlant polyphenols are secondary metabolites that constitute one of the most common and widespread groups of natural products. They express a large and diverse panel of biological activities including beneficial effects on both plants and humans.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003eAcknowledgments vii\u003c\/p\u003e \u003cp\u003eContributors xvii\u003c\/p\u003e \u003cp\u003ePreface xix\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Monolignol Biosynthesis and its Genetic Manipulation: The Good, the Bad, and the Ugly 1\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRichard A. Dixon, M.S. Srinivasa Reddy, and Lina Gallego-Giraldo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 2\u003c\/p\u003e \u003cp\u003e1.2 Function and distribution of lignin in plants 2\u003c\/p\u003e \u003cp\u003e1.3 Targets for modification of lignin biosynthesis 5\u003c\/p\u003e \u003cp\u003e1.3.1 Gene targets 1. Biosynthetic enzymes 5\u003c\/p\u003e \u003cp\u003e1.3.1.1 L-phenylalanine ammonia-lyase (PAL) 6\u003c\/p\u003e \u003cp\u003e1.3.1.2 Cinnamate 4-hydroxylase (C4H) 6\u003c\/p\u003e \u003cp\u003e1.3.1.3 4-coumarate: coenzyme-A ligase (4CL) 6\u003c\/p\u003e \u003cp\u003e1.3.1.4 Enzymes of the coumaroyl shikimate shunt 7\u003c\/p\u003e \u003cp\u003e1.3.1.5 Caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) 7\u003c\/p\u003e \u003cp\u003e1.3.1.6 Ferulate 5-hydroxylase (F5H) 8\u003c\/p\u003e \u003cp\u003e1.3.1.7 Caffeic acid 3-O-methyltransferase (COMT) 8\u003c\/p\u003e \u003cp\u003e1.3.1.8 Cinnamoyl-CoA reductase 8\u003c\/p\u003e \u003cp\u003e1.3.1.9 Cinnamyl alcohol dehydrogenase (CAD) 9\u003c\/p\u003e \u003cp\u003e1.3.2 Gene targets 2. Transcription factors 9\u003c\/p\u003e \u003cp\u003e1.4 Impacts of lignin modification through targeting of the monolignol biosynthetic pathway 9\u003c\/p\u003e \u003cp\u003e1.4.1 L-phenylalanine ammonia-lyase (PAL) 10\u003c\/p\u003e \u003cp\u003e1.4.2 Cinnamate 4-hydroxylase (C4H) 10\u003c\/p\u003e \u003cp\u003e1.4.3 4-coumarate: coenzyme-A ligase (4CL) 11\u003c\/p\u003e \u003cp\u003e1.4.4 Hydroxycinnamoyl-CoA: shikimate hydroxycinnamoyl transferase (HCT) 13\u003c\/p\u003e \u003cp\u003e1.4.5 4-coumaroyl shikimate 3′-hydroxylase (C3′H) 14\u003c\/p\u003e \u003cp\u003e1.4.6 Caffeoyl CoA 3-O-methyltransferase (CCoAOMT) 15\u003c\/p\u003e \u003cp\u003e1.4.7 Ferulate 5-hydroxylase (F5H) 17\u003c\/p\u003e \u003cp\u003e1.4.8 Caffeic acid O-methyltransferase (COMT) 18\u003c\/p\u003e \u003cp\u003e1.4.9 Cinnamoyl-CoA reductase (CCR) 20\u003c\/p\u003e \u003cp\u003e1.4.10 Cinnamyl alcohol dehydrogenase (CAD) 22\u003c\/p\u003e \u003cp\u003e1.5 Impacts of lignin modification through targeting of TFs 23\u003c\/p\u003e \u003cp\u003e1.5.1 NAC master switches 24\u003c\/p\u003e \u003cp\u003e1.5.2 MYB repressors of monolignol biosynthesis 24\u003c\/p\u003e \u003cp\u003e1.5.3 WRKY repressors of lignification in pith 24\u003c\/p\u003e \u003cp\u003e1.6 Monolignol pathway modification and plant growth 25\u003c\/p\u003e \u003cp\u003e1.7 Conclusions: it isn’t all that bad! 26\u003c\/p\u003e \u003cp\u003eReferences 27\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Perturbing Lignin Biosynthesis: Metabolic Changes in Response to Manipulation of the Phenylpropanoid Pathway 39\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eNickolas A. Anderson and Clint Chapple\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 40\u003c\/p\u003e \u003cp\u003e2.1.1 Cell wall-bound phenylpropanoids 40\u003c\/p\u003e \u003cp\u003e2.1.2 Soluble phenylpropanoids 43\u003c\/p\u003e \u003cp\u003e2.2 Changes in metabolism associated with phenylpropanoid-pathway disruptions 44\u003c\/p\u003e \u003cp\u003e2.2.1 Phenylalanine ammonia-lyase (PAL) 44\u003c\/p\u003e \u003cp\u003e2.2.2 Cinnamate 4-hydroxylase (C4H) 45\u003c\/p\u003e \u003cp\u003e2.2.3 4-coumarate: CoA ligase (4CL) 46\u003c\/p\u003e \u003cp\u003e2.2.4 Hydroxycinnamoyl-coenzyme A: shikimate\/quinate hydroxycinnamoyltransferase (HCT)\/p-coumaroyl shikimate 3′-hydroxylase (C3′H) 46\u003c\/p\u003e \u003cp\u003e2.2.5 Cinnamoyl CoA reductase (CCR) 47\u003c\/p\u003e \u003cp\u003e2.2.6 Ferulate 5-hydroxylase (F5H) 48\u003c\/p\u003e \u003cp\u003e2.2.7 Caffeic acid\/5-hydroxyferulic acid O-methyltransferase (COMT)\/caffeoyl CoA 3-O-methyltransferase (CCoAOMT) 49\u003c\/p\u003e \u003cp\u003e2.2.8 Cinnamyl alcohol dehydrogenases (CAD) 50\u003c\/p\u003e \u003cp\u003e2.3 Atypical lignins 50\u003c\/p\u003e \u003cp\u003e2.4 Dwarfism 51\u003c\/p\u003e \u003cp\u003e2.5 Conclusions 52\u003c\/p\u003e \u003cp\u003eReferences 52\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Function, Structure, and Evolution of Flavonoid Glycosyltransferases in Plants 61\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eKeiko Yonekura-Sakakibara and Kazuki Saito\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 61\u003c\/p\u003e \u003cp\u003e3.2 UDP-dependent glycosyltransferases 63\u003c\/p\u003e \u003cp\u003e3.2.1 Functional identification of flavonoid UGTs 63\u003c\/p\u003e \u003cp\u003e3.2.1.1 Flavonoid 3-O-glycosyltransferases 63\u003c\/p\u003e \u003cp\u003e3.2.1.2 Flavonoid 7-O-glycosyltransferases 63\u003c\/p\u003e \u003cp\u003e3.2.1.3 Flavonoid glycosyltransferases that glycosylate the sugar moiety attached to a flavonoid aglycone 67\u003c\/p\u003e \u003cp\u003e3.2.1.4 Flavonoid 3′-O-glycosyltransferase 69\u003c\/p\u003e \u003cp\u003e3.2.1.5 Flavonoid C-glycosyltransferase 69\u003c\/p\u003e \u003cp\u003e3.2.2 3D structures of flavonoid UGTs 70\u003c\/p\u003e \u003cp\u003e3.2.3 Functional evolution in UGTs 72\u003c\/p\u003e \u003cp\u003e3.2.3.1 Functional evolution in flavonoid UGTs 74\u003c\/p\u003e \u003cp\u003e3.3 Glycoside hydrolase-type glycosyltransferases 75\u003c\/p\u003e \u003cp\u003e3.3.1 Functional identification of flavonoid GH1-type glycosyltransferases 75\u003c\/p\u003e \u003cp\u003e3.3.1.1 Anthocyanin 5\/7-O-glycosyltransferases 75\u003c\/p\u003e \u003cp\u003e3.3.1.2 Anthocyanin 3-O-6′′-O-coumaroylglucoside: glucosyltransferase 76\u003c\/p\u003e \u003cp\u003e3.3.2 The reaction mechanism of GH1-type glycosyltransferases 78\u003c\/p\u003e \u003cp\u003e3.4 Conclusions 78\u003c\/p\u003e \u003cp\u003eReferences 78\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 The Chemistry and Chemical Ecology of Ellagitannins in Plant–Insect Interactions: From Underestimated Molecules to Bioactive Plant Constituents 83\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJuha-Pekka Salminen\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 84\u003c\/p\u003e \u003cp\u003e4.2 Definitions and chemical structures of hydrolyzable tannins 85\u003c\/p\u003e \u003cp\u003e4.3 Biosynthetic pathways of hydrolyzable tannins in plants 87\u003c\/p\u003e \u003cp\u003e4.3.1 Tannin biosynthetic pathways have many branching points that affect the flux of biosynthetic energy towards different tannins 90\u003c\/p\u003e \u003cp\u003e4.3.2 Biosynthesis of gallic acid, galloylglucoses, and gallotannins 91\u003c\/p\u003e \u003cp\u003e4.3.3 Biosynthesis of ellagitannins 92\u003c\/p\u003e \u003cp\u003e4.4 Distributions of different types of tannin in plants 94\u003c\/p\u003e \u003cp\u003e4.5 Tannins in plant–herbivore interactions 98\u003c\/p\u003e \u003cp\u003e4.5.1 General aspects of tannins and plant–herbivore interactions 98\u003c\/p\u003e \u003cp\u003e4.5.2 The tannin oxidation hypothesis and its verification in plant–herbivore interactions 102\u003c\/p\u003e \u003cp\u003e4.5.3 The ease of oxidation of individual ellagitannins can be predicted by their chemical structures and chromatographic properties 104\u003c\/p\u003e \u003cp\u003e4.5.4 Other factors that may affect ellagitannin activities against insect herbivores 107\u003c\/p\u003e \u003cp\u003e4.6 Conclusions 108\u003c\/p\u003e \u003cp\u003eAcknowledgments 109\u003c\/p\u003e \u003cp\u003eReferences 109\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Diverse Ecological Roles of Plant Tannins: Plant Defense and Beyond 115\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eC. Peter Constabel, Kazuko Yoshida, and Vincent Walker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 115\u003c\/p\u003e \u003cp\u003e5.2 Overview of tannin structure and function in defense 116\u003c\/p\u003e \u003cp\u003e5.2.1 Structural diversity and distribution 116\u003c\/p\u003e \u003cp\u003e5.2.2 In vitro biochemical activities 119\u003c\/p\u003e \u003cp\u003e5.2.3 Old and new views on tannins in defense 120\u003c\/p\u003e \u003cp\u003e5.2.4 The antimicrobial nature of tannins 122\u003c\/p\u003e \u003cp\u003e5.3 Tissue localization and ecological function 124\u003c\/p\u003e \u003cp\u003e5.3.1 Distribution of tannins in vegetative tissues 125\u003c\/p\u003e \u003cp\u003e5.3.2 Tannins in seeds and fruit 126\u003c\/p\u003e \u003cp\u003e5.3.3 Ecology of fruit tannins 127\u003c\/p\u003e \u003cp\u003e5.4 Tannins in plant–soil–environment interactions 129\u003c\/p\u003e \u003cp\u003e5.4.1 Tannin distribution and stability in soil 129\u003c\/p\u003e \u003cp\u003e5.4.2 Impact of tannins on soil nitrogen cycling and microbial activity 130\u003c\/p\u003e \u003cp\u003e5.4.3 Interaction with community and ecosystem processes 131\u003c\/p\u003e \u003cp\u003e5.4.4 Tannins and other plant stress adaptations 133\u003c\/p\u003e \u003cp\u003e5.5 Conclusions 134\u003c\/p\u003e \u003cp\u003eAcknowledgments 134\u003c\/p\u003e \u003cp\u003eReferences 134\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Epigenetics, Plant (Poly)phenolics, and Cancer Prevention 143\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eClarissa Gerhauser\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 143\u003c\/p\u003e \u003cp\u003e6.2 Influence of polyphenols on DNA methylation 145\u003c\/p\u003e \u003cp\u003e6.2.1 DNA methylation in normal and tumor cells 145\u003c\/p\u003e \u003cp\u003e6.2.2 Inhibition of DNMTs in vitro 145\u003c\/p\u003e \u003cp\u003e6.2.3 Inhibition of DNA methylation in cellular systems and in vivo 147\u003c\/p\u003e \u003cp\u003e6.2.3.1 Quercetin 147\u003c\/p\u003e \u003cp\u003e6.2.3.2 Nordihydroguaiaretic acid (NDGA) 147\u003c\/p\u003e \u003cp\u003e6.2.3.3 Resveratrol 158\u003c\/p\u003e \u003cp\u003e6.2.3.4 Apple polyphenols 159\u003c\/p\u003e \u003cp\u003e6.2.3.5 Black raspberry polyphenols 159\u003c\/p\u003e \u003cp\u003e6.3 Influence of polyphenols on histone-modifying enzymes 160\u003c\/p\u003e \u003cp\u003e6.3.1 Acetylation of histones and non-histone proteins 161\u003c\/p\u003e \u003cp\u003e6.3.1.1 Anacardic acid 161\u003c\/p\u003e \u003cp\u003e6.3.1.2 Curcumin 165\u003c\/p\u003e \u003cp\u003e6.3.1.3 Garcinol 166\u003c\/p\u003e \u003cp\u003e6.3.1.4 Gallic acid 167\u003c\/p\u003e \u003cp\u003e6.3.1.5 Delphinidin 167\u003c\/p\u003e \u003cp\u003e6.3.2 Deacetylation by HDACs and sirtuins 168\u003c\/p\u003e \u003cp\u003e6.3.2.1 Inhibition of HDAC activity 168\u003c\/p\u003e \u003cp\u003e6.3.2.2 Modulation of sirtuin activity 168\u003c\/p\u003e \u003cp\u003e6.3.3 Histone methylation marks 171\u003c\/p\u003e \u003cp\u003e6.3.3.1 Histone lysine methylation 171\u003c\/p\u003e \u003cp\u003e6.3.3.2 Histone lysine demethylation 171\u003c\/p\u003e \u003cp\u003e6.4 Influence of noncoding miRNAs on gene expression 172\u003c\/p\u003e \u003cp\u003e6.5 Chemopreventive polyphenols affecting the epigenome via multiple mechanisms 173\u003c\/p\u003e \u003cp\u003e6.5.1 (−)-epigallocatechin 3-gallate (EGCG) and green-tea polyphenols (GTPs) 173\u003c\/p\u003e \u003cp\u003e6.5.1.1 DNA methylation 174\u003c\/p\u003e \u003cp\u003e6.5.1.2 Histone-modifying enzymes (HATs, HDACs, HMTs) 178\u003c\/p\u003e \u003cp\u003e6.5.1.3 miRNAs 181\u003c\/p\u003e \u003cp\u003e6.5.2 Genistein and soy isoflavones 183\u003c\/p\u003e \u003cp\u003e6.5.2.1 DNA methylation 183\u003c\/p\u003e \u003cp\u003e6.5.2.2 Influence on histone acetylation and methylation 189\u003c\/p\u003e \u003cp\u003e6.5.2.3 miRNAs affected by isoflavones 192\u003c\/p\u003e \u003cp\u003e6.6 Conclusions 195\u003c\/p\u003e \u003cp\u003e6.6.1 DNA methylation 195\u003c\/p\u003e \u003cp\u003e6.6.2 Histone-modifying enzymes 195\u003c\/p\u003e \u003cp\u003e6.6.3 miRNAs 196\u003c\/p\u003e \u003cp\u003e6.6.4 Summary 196\u003c\/p\u003e \u003cp\u003eReferences 196\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Discovery of Polyphenol-Based Drugs for Cancer Prevention and Treatment: The Tumor Proteasome as a Novel Target 209\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eFathima R. Kona, Min Shen, Di Chen, Tak Hang Chan, and Q. Ping Dou\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 209\u003c\/p\u003e \u003cp\u003e7.2 Secondary metabolites of plants 210\u003c\/p\u003e \u003cp\u003e7.3 Plant polyphenols and their analogs 211\u003c\/p\u003e \u003cp\u003e7.3.1 Classification and bioavailability of plant polyphenols 211\u003c\/p\u003e \u003cp\u003e7.3.2 Tea and tea polyphenols 212\u003c\/p\u003e \u003cp\u003e7.3.3 Targeting of the tumor proteasome by tea polyphenols 216\u003c\/p\u003e \u003cp\u003e7.3.4 EGCG analogs as proteasome inhibitors 217\u003c\/p\u003e \u003cp\u003e7.3.4.1 Peracetate and other prodrugs of EGCG 219\u003c\/p\u003e \u003cp\u003e7.3.4.2 Fluoro-substituted EGCG analogs 222\u003c\/p\u003e \u003cp\u003e7.3.4.3 Para-amino substituent on the D ring 222\u003c\/p\u003e \u003cp\u003e7.3.4.4 Bis-galloyl derivatives of EGCG 223\u003c\/p\u003e \u003cp\u003e7.3.4.5 Methylation-resistant (−)-EGCG analogs 223\u003c\/p\u003e \u003cp\u003e7.3.5 Other molecular targets of tea polyphenols 224\u003c\/p\u003e \u003cp\u003e7.3.5.1 AMPK activation 224\u003c\/p\u003e \u003cp\u003e7.3.6 Proteasome inhibitory action of other plant polyphenols 225\u003c\/p\u003e \u003cp\u003e7.4 Natural polyphenols in reversal of drug resistance 226\u003c\/p\u003e \u003cp\u003e7.4.1 Mechanisms of tumor drug resistance 226\u003c\/p\u003e \u003cp\u003e7.4.2 The ubiquitin–proteasome pathway in drug resistance 226\u003c\/p\u003e \u003cp\u003e7.4.3 EGCG and overcoming drug resistance 227\u003c\/p\u003e \u003cp\u003e7.4.4 Genistein and overcoming drug resistance 228\u003c\/p\u003e \u003cp\u003e7.4.5 Curcumin and overcoming drug resistance 228\u003c\/p\u003e \u003cp\u003e7.4.6 Clinical trials using polyphenols and chemotherapy 229\u003c\/p\u003e \u003cp\u003e7.5 Conclusions 231\u003c\/p\u003e \u003cp\u003eAcknowledgments 231\u003c\/p\u003e \u003cp\u003eReferences 231\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Flavonoid Occurrence, Bioavailability, Metabolism, and Protective Effects in Humans: Focus on Flavan-3-ols and Flavonols 239\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eLuca Calani, Margherita Dall’Asta, Renato Bruni, and Daniele Del Rio\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 240\u003c\/p\u003e \u003cp\u003e8.2 Focus on flavan-3-ols and flavonols: chemical structures and dietary sources 240\u003c\/p\u003e \u003cp\u003e8.2.1 Flavan-3-ols 240\u003c\/p\u003e \u003cp\u003e8.2.2 Flavonols 243\u003c\/p\u003e \u003cp\u003e8.3 Metabolism and bioavailability of flavonoids in humans 244\u003c\/p\u003e \u003cp\u003e8.3.1 Flavan-3-ols 245\u003c\/p\u003e \u003cp\u003e8.3.2 Flavonols 251\u003c\/p\u003e \u003cp\u003e8.4 In vitro studies 255\u003c\/p\u003e \u003cp\u003e8.4.1 Flavan-3-ols 256\u003c\/p\u003e \u003cp\u003e8.4.1.1 Phase II metabolites 256\u003c\/p\u003e \u003cp\u003e8.4.1.2 Microbe-derived metabolites 259\u003c\/p\u003e \u003cp\u003e8.4.2 Flavonols 260\u003c\/p\u003e \u003cp\u003e8.4.2.1 Phase II metabolites 260\u003c\/p\u003e \u003cp\u003e8.4.2.2 Microbe-derived metabolites 265\u003c\/p\u003e \u003cp\u003e8.5 In vivo studies 266\u003c\/p\u003e \u003cp\u003e8.5.1 Cardiovascular and endothelial protection 267\u003c\/p\u003e \u003cp\u003e8.5.1.1 Flavan-3-ols 267\u003c\/p\u003e \u003cp\u003e8.5.1.2 Flavonols 268\u003c\/p\u003e \u003cp\u003e8.5.2 Neuroprotection 269\u003c\/p\u003e \u003cp\u003e8.5.2.1 Flavan-3-ols 269\u003c\/p\u003e \u003cp\u003e8.5.3 Cancer prevention 269\u003c\/p\u003e \u003cp\u003e8.5.3.1 Flavan-3-ols 269\u003c\/p\u003e \u003cp\u003e8.5.3.2 Flavonols 270\u003c\/p\u003e \u003cp\u003e8.6 Conclusions 271\u003c\/p\u003e \u003cp\u003eReferences 272\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Inhibition of VEGF Signaling by Polyphenols in Relation to Atherosclerosis and Cardiovascular Disease 281\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRebecca L. Edwards and Paul A. Kroon\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 282\u003c\/p\u003e \u003cp\u003e9.2 VEGF and VEGF signaling 282\u003c\/p\u003e \u003cp\u003e9.3 VEGF signaling and angiogenesis 286\u003c\/p\u003e \u003cp\u003e9.4 Angiogenesis and atherosclerosis 286\u003c\/p\u003e \u003cp\u003e9.5 Polyphenols in foods and diets, and their absorption and metabolism 289\u003c\/p\u003e \u003cp\u003e9.6 Effects of polyphenols on VEGF signaling, angiogenesis, and atherosclerosis 290\u003c\/p\u003e \u003cp\u003e9.6.1 VEGF signaling 314\u003c\/p\u003e \u003cp\u003e9.6.2 Angiogenesis 315\u003c\/p\u003e \u003cp\u003e9.6.3 Atherosclerosis 315\u003c\/p\u003e \u003cp\u003e9.7 Relationships between polyphenol consumption and CVD risk 316\u003c\/p\u003e \u003cp\u003e9.7.1 Epidemiological studies 316\u003c\/p\u003e \u003cp\u003e9.7.2 Intervention studies 318\u003c\/p\u003e \u003cp\u003e9.8 Conclusions 319\u003c\/p\u003e \u003cp\u003eAcknowledgments 320\u003c\/p\u003e \u003cp\u003eReferences 320\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Phenolic Compounds from a Sex-Gender Perspective 327\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eIlaria Campesi, Annalisa Romani, Maria Marino, and Flavia Franconi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction 328\u003c\/p\u003e \u003cp\u003e10.2 Phenolic compound classification and molecular mechanisms 329\u003c\/p\u003e \u003cp\u003e10.3 Sex-gender and the xenokinetics of phenolic compounds 330\u003c\/p\u003e \u003cp\u003e10.4 Sex-gender differences in xenodynamics 333\u003c\/p\u003e \u003cp\u003e10.5 Conclusions 334\u003c\/p\u003e \u003cp\u003eReferences 334\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Thermodynamic and Kinetic Processes of Anthocyanins and Related Compounds and their Bio-Inspired Applications 341\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eFernando Pina\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 342\u003c\/p\u003e \u003cp\u003e11.2 Anthocyanins in aqueous solution 342\u003c\/p\u003e \u003cp\u003e11.2.1 Step-by-step procedure for calculating rate and equilibrium constants 349\u003c\/p\u003e \u003cp\u003e11.2.1.1 Step 1: determination of the equilibrium constant K′a 349\u003c\/p\u003e \u003cp\u003e11.2.1.2 Step 2: determination of the equilibrium constant Ka 349\u003c\/p\u003e \u003cp\u003e11.2.1.3 Step 3: determination of the equilibrium constant Kt and the respective rate constants 350\u003c\/p\u003e \u003cp\u003e11.2.1.4 Step 4: determination of the hydration rate and equilibrium constants 350\u003c\/p\u003e \u003cp\u003e11.2.1.5 Step 5: determination of the isomerization rate and equilibrium constants 350\u003c\/p\u003e \u003cp\u003e11.2.1.6 Step 6: verification of the self-consistency of all the data 351\u003c\/p\u003e \u003cp\u003e11.3 Influence of anthocyanin self-aggregation on the determination of rate and equilibrium constants 351\u003c\/p\u003e \u003cp\u003e11.4 Photochromism: applications bio-inspired in anthocyanins 357\u003c\/p\u003e \u003cp\u003e11.4.1 Systems lacking the cis–trans isomerization barrier 357\u003c\/p\u003e \u003cp\u003e11.4.2 Systems exhibiting high cis–trans isomerization barriers 361\u003c\/p\u003e \u003cp\u003e11.4.2.1 The concept of right–lock–read–unlock–erase optical memories 361\u003c\/p\u003e \u003cp\u003e11.4.3 Styryl-1-benzopyrylium (styryl flavylium) and naphthoflavylium 362\u003c\/p\u003e \u003cp\u003e11.4.4 Dye-sensitized solar cells based on anthocyanins 362\u003c\/p\u003e \u003cp\u003e11.5 How to construct an energy-level diagram 364\u003c\/p\u003e \u003cp\u003e11.6 How to calculate the mole-fraction distribution of a network species 367\u003c\/p\u003e \u003cp\u003eReferences 368\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Synthetic Strategies and Tactics for Catechin and Related Polyphenols 371\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eKen Ohmori and Keisuke Suzuki\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 371\u003c\/p\u003e \u003cp\u003e12.2 Early synthetic work 375\u003c\/p\u003e \u003cp\u003e12.3 Stereoselective approaches to flavan-3-ols 380\u003c\/p\u003e \u003cp\u003e12.3.1 Synthesis of catechin-series (= 2,3-trans) derivatives 380\u003c\/p\u003e \u003cp\u003e12.3.2 Synthesis of epi-series (= 2,3-cis) catechins 393\u003c\/p\u003e \u003cp\u003e12.4 Conclusions 407\u003c\/p\u003e \u003cp\u003eAbbreviations 407\u003c\/p\u003e \u003cp\u003eAcknowledgments 408\u003c\/p\u003e \u003cp\u003eReferences 408\u003c\/p\u003e \u003cp\u003eIndex 411\u003c\/p\u003e","brand":"John Wiley and Sons Ltd","offers":[{"title":"Default Title","offer_id":49406851580247,"sku":"9781118329672","price":159.26,"currency_code":"GBP","in_stock":false}],"url":"https:\/\/bookcurl.com\/products\/recent-advances-in-polyphenol-research-04-9781118329672","provider":"Book Curl","version":"1.0","type":"link"}