{"product_id":"the-nuclear-pore-complex-9781071623367","title":"The Nuclear Pore Complex","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eThis volume covers all methods used to discover the composition, structure, and dynamics of the nuclear pore complex (NPC), as well as the soluble transport factors involved in the transport process.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003ePart I: The Nuclear Pore Complex and Nucleoporins            \u003c\/p\u003e  \u003cp\u003e1.     Affinity Isolation of Endogenous Saccharomyces cerevisiae Nuclear Pore Complexes\u003c\/p\u003e  \u003cp\u003eIlona Nudelman, Javier Fernandez-Martinez, and Michael P. Rout\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  2.     Transformation of Chaetomium thermophilum and affinity-purification of native thermostable protein complexes\u003cp\u003e\u003c\/p\u003e  \u003cp\u003eNikola Kellner and Ed Hurt\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e3.     Nuclear Pore Complex Assembly using Xenopus Egg Extract\u003c\/p\u003e  \u003cp\u003eGuillaume Holzer and Wolfram Antonin\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e Part II:  Nucleo-cytoplasmic Passage            \u003c\/p\u003e  \u003cp\u003e4.     Analysis of Nuclear Pore Complex Permeability in Mammalian Cells and Isolated Nuclei Using Fluorescent Dextrans\u003c\/p\u003e  Marcela Raices and Maximiliano A. D’Angelo\u003cp\u003e\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e5.     Hormone-inducible Transport Reporter Assay to Study Nuclear Import Defects in Neurodegenerative Diseases\u003c\/p\u003e  \u003cp\u003eSaskia Hutten and Dorothee Dormann\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e6.     Subcellular Fractionation Suitable for Studies of RNA and Protein Trafficking\u003c\/p\u003e  \u003cp\u003eBiljana Culjkovic-Kraljacic and Katherine L.B. Borden\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e7.     Localising Total mRNA in Plant Cells\u003c\/p\u003e  \u003cp\u003eGeraint Parry\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e8.     Using Single Molecule RNA FISH to Determine Nuclear Export and Transcription Phenotypes in Drosophila Tissues\u003c\/p\u003e  \u003cp\u003e Jennifer R. Aleman, Shawn C. Little, and Maya Capelson\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003ePart III: Functional Analysis of Nucleoporins\u003c\/p\u003e  \u003cp\u003e9.     Analysis of Nucleoporin Function using Inducible Degron Techniques\u003c\/p\u003e  \u003cp\u003eVasilisa Aksenova, Alexei Arnaoutov, and Mary Dasso\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e10.  Monitoring of Chromatin Organization at the Nuclear Pore Complex, Inner Nuclear Membrane and Nuclear Interior in Live Cells by Fluorescence Ratiometric Imaging of Chromatin (FRIC)\u003c\/p\u003e  \u003cp\u003eFrida Niss, Cecilia Bergqvist, Anna-Lena Ström, and Einar Hallberg\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e11.  Analysis of Nuclear Pore Complexes in Caenorhabditis elegans by Live Imaging and Functional Genomic\u003c\/p\u003e  \u003cp\u003e Patricia de la Cruz Ruiz, Raquel Romero-Bueno, and Peter Askjaer\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e12.  Protein Retargeting in Aspergillus nidulans to Study the Function of Nuclear Pore Complex Proteins\u003c\/p\u003e  \u003cp\u003eSubbulakshmi Suresh and Stephen A. Osmani\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003ePart IV: Protein-Protein Interactions  \u003c\/p\u003e  \u003cp\u003e13.  Split-GFP Complementation to Study the Nuclear Membrane Proteome using Microscopy. Shary N. Shelton, Sarah E. Smith, and Sue L. Jaspersen\u003c\/p\u003e  \u003cp\u003e14.  Bimolecular Fluorescence Complementation: Quantitative Analysis of In Cell Interaction of Nuclear Transporter Importin a with Cargo Proteins\u003c\/p\u003e  \u003cp\u003eAlexander Lee, Marie A. Bogoyevitch and David A. Jans\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e15.  Validation of Nuclear Pore Complex Protein-Protein Interactions by Transient Expression in Plants\u003c\/p\u003e  \u003cp\u003e Fumika Ikeda and Kentaro Tamura\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e16.  Binding affinity measurement of Nuclear Export Signal peptides to their exporter CRM1. Ho Yee Joyce Fung, and Yuh Min Chook\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003ePart V: Post Translational Modifications       \u003c\/p\u003e  \u003cp\u003e17.  Analysis of Ubiquitylation and SUMOylation of Yeast Nuclear Pore Complex Proteins\u003c\/p\u003e  \u003cp\u003eCatherine Dargemont\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e18.  Purification of Cdk-CyclinB-Kinase-Targeted Phosphopeptides from Nuclear Envelope\u003c\/p\u003e  \u003cp\u003e Justin D. Blethrow, Amanda L. DiGuilio, and Joseph S. Glavy\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  Part VI: Biophysical Methods \u003cp\u003e\u003c\/p\u003e  \u003cp\u003e19.  Crystallization of Nuclear Export Signals or Small Molecule Inhibitors Bound to Nuclear Exporter CRM1\u003c\/p\u003e  Yee Joyce Fung and Yuh Min Chook\u003cp\u003e\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e20.  Atomic Force Microscopy for Structural and Biophysical Investigations on Nuclear Pore Complexes\u003c\/p\u003e  \u003cp\u003e Ivan Liashkovich, Gonzalo Rosso, and Victor Shahin\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  21.  Multivalent Interactions with Intrinsically Disordered Proteins Measured by Surface Plasmon Resonance\u003cp\u003e\u003c\/p\u003e  \u003cp\u003eLarisa E. Kapinos and Roderick Y. H. Lim\u003c\/p\u003e   \u003cp\u003e\u003c\/p\u003e  \u003cp\u003e22.  Assembly and Use of a Microfluidic Device to Study Nuclear Mechanobiology during Confined Migration\u003c\/p\u003e  Richa Agrawal, Aaron Windsor, and Jan Lammerding\u003cp\u003e\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003ePart VII:  Imaging NPCs and Transport\u003c\/p\u003e  23.  SPEED Microscopy: High-Speed Single-Molecule Tracking and Mapping of Nucleocytoplasmic Transport\u003cp\u003e\u003c\/p\u003e  \u003cp\u003eSteven J. Schnell, Mark Tingey, and Weidong Yang \u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e24.  Imaging Fluorescent Nuclear Pore Complex Proteins in C. elegans\u003c\/p\u003e  \u003cp\u003eCourtney Lancaster, Giulia Zavagno, James Groombridge, Adelaide Raimundo, David Weinkove, Tim Hawkins, Joanne Robson and Martin W. Goldberg\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e25.  Visualizing Nuclear Pore Complexes in Xenopus Egg Extracts\u003c\/p\u003e  \u003cp\u003eSampada Mishra and Daniel L. Levy\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e26.  TEM Imaging of Membrane Choreography During Mitosis of Drosophila Tissue Culture Cells\u003c\/p\u003e  \u003cp\u003eAnton Strunov, Lidiya V. Boldyreva, Alexey V. Pindyurin, Maurizio Gatti, and Elena Kiseleva\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e27.  Scanning Electron Microscopy (SEM) and Immuno-SEM of Nuclear Pore Complexes from Amphibian Oocytes, Mammalian Cell Cultures, Yeast and Plants\u003c\/p\u003e  \u003cp\u003eMartin W. Goldberg and Jindřiška Fišerová\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e28.  NPC Structure in Model Organisms: Transmission Electron Microscopy and Immuno-gold Labelling using High Pressure Freezing\/Freeze Substitution of Yeast, Worms and Plants\u003c\/p\u003e  \u003cp\u003e A. Christine Richardson, Jindřiška Fišerová, and Martin W. Goldberg\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e29.  High Resolution Imaging and Analysis of Individual Nuclear Pore Complexes\u003c\/p\u003e  \u003cp\u003e Boris Fichtman, Saroj G. Regmi, Mary Dasso, and Amnon Harel\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e30.  Live CLEM imaging of Tetrahymena to Analyze the Dynamic Behavior of the Nuclear Pore Complex\u003c\/p\u003e  \u003cp\u003eTokuko Haraguchi, Hiroko Osakada, and Masaaki Iwamoto\u003c\/p\u003e  \u003cp\u003e \u003c\/p\u003e  \u003cp\u003e31.  Visualizing Nuclear Pore Complex Assembly In Situ in Human Cells at Nanometer Resolution by Correlating Live Imaging with Electron Microscopy\u003c\/p\u003e  \u003cp\u003eHelena Bragulat-Teixidor, M. Julius Hossain, and Shotaro Otsuka\u003c\/p\u003e","brand":"Springer-Verlag New York Inc.","offers":[{"title":"Default Title","offer_id":53186413822295,"sku":"9781071623367","price":208.99,"currency_code":"GBP","in_stock":true}],"url":"https:\/\/bookcurl.com\/products\/the-nuclear-pore-complex-9781071623367","provider":"Book Curl","version":"1.0","type":"link"}