{"product_id":"protein-misfolding-diseases-isbn-9780471799283","title":"Protein Misfolding Diseases","description":"An increasingly aging population will add to the number of individuals suffering from amyloid. \u003ci\u003eProtein Misfolding Diseases\u003c\/i\u003e provides a systematic overview of the current and emerging therapies for these types of protein misfolding diseases, including Alzheimer's, Parkinson's, and Mad Cow. The book emphasizes therapeutics in an amyloid disease context to help students, faculty, scientific researchers, and doctors working with protein misfolding diseases bridge the gap between basic science and pharmaceutical applications to protein misfolding disease.  CONTRIBUTORS.  \u003cp\u003eFOREWORD (\u003ci\u003eR. John Ellis\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003ePREFACE.\u003c\/p\u003e \u003cp\u003eACKNOWLEDGMENTS.\u003c\/p\u003e \u003cp\u003eINTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE (Vladimir N. Uversky).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART I PRINCIPLES OF PROTEIN MISFOLDING.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1 Why Proteins Misfold (\u003ci\u003eSilvia Campioni, Elodie Monsellier, and Fabrizio Chiti\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e2 Endoplasmic Reticulum Stress and Oxidative Stress: Mechanisms and Link to Disease (\u003ci\u003eJyoti D. Malhotra and Randal J. Kaufman\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e3 Role of Molecular Chaperones in Protein Folding (\u003ci\u003eKausik Chakraborty, Florian Georgescauld, Manajit Hayer-Hartl, and F. Ulrich Hartl\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e4 Kinetic Models for Protein Misfolding and Association (\u003ci\u003eEvan T. Powers and Frank A. Ferrone\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e5 Toxicity in Amyloid Diseases (\u003ci\u003eMassimo Stefani\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e6 Autophagy: An Alternative Degradation Mechanism for Misfolded Proteins (\u003ci\u003eMaria Kon and Ana Maria Cuervo\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e7 Role of Posttranslational Modifications in Amyloid Formation (\u003ci\u003eAndisheh Abedini, Ruchi Gupta, Peter Marek, Fanling Meng, Daniel P. Raleigh, Humeyra Taskent, and Sylvia Tracz\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e8 Unraveling Molecular Mechanisms and Structures of Self-Perpetuating Prions (\u003ci\u003ePeter M. Tessier and Susan Lindquist\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e9 Caenorhabditis elegans as a Model System to Study the Biology of Protein Aggregation and Toxicity (\u003ci\u003eElise A. Kikis, Anat Ben-Zvi, and Richard I. Morimoto\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e10 Using Drosophila to Reveal Insight Into Protein Misfolding Diseases (\u003ci\u003eJulide Bilen and Nancy M. Bonini\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e11 Animal Models to Study the Biology of Amyloid-β Protein Misfolding in Alzheimer Disease (\u003ci\u003eKaren H. Ashe\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART II PROTEIN MISFOLDING DISEASE: GAIN-OF-FUNCTION AND LOSS-OF-FUNCTION DISEASES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e12 Alzheimer Disease: Protein Misfolding, Model Systems, and Experimental Therapeutics (\u003ci\u003eDonald L. Price, Alena V. Savonenko, Tong Li, Michael K. Lee, and Philip C. Wong\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e13 Prion Disease Therapy: Trials and Tribulations (\u003ci\u003eValerie L. Sim and Byron Caughey\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e14 Misfolding and Aggregation in Huntington Disease and Other Expanded Polyglutamine Repeat Diseases (\u003ci\u003eRonald Wetzel\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e15 Systemic Amyloidoses (\u003ci\u003eMarina Ramirez-Alvarado and Joel N. Buxbaum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e16 Hemodialysis-Related Amyloidosis (\u003ci\u003eDavid P. Smith, Alison E. Ashcroft, and Sheena E. Radford\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e17 Copper?Zinc Superoxide Dismutase, Its Copper Chaperone, and Familial Amyotrophic Lateral Sclerosis (\u003ci\u003eDuane D. Winkler, Mercedes Prudencio, Celeste Karch, David R. Borchelt, and P. John Hart\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e18 Alpha-1-Antitrypsin Deficiency (\u003ci\u003eDavid A. Lomas and David H. Perlmutter\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e19 Folding Biology of Cystic Fibrosis: A Consortium-Based Approach to Disease (\u003ci\u003eWilliam E. Balch, Ineke Braakman, Jeff Brodsky, Raymond Frizzell, William Guggino, Gergely L. Lukacs, Christopher Penland, Harvey Pollard, William Skach, Eric Sorscher, and Philip Thomas\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e20 Thiopurine S-Methyltransferase Pharmacogenomics: Protein Misfolding, Aggregation, and Degradation (\u003ci\u003eFang Li and Richard M. Weinshilboum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e21 Gaucher Disease (\u003ci\u003eTim Edmunds\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e22 Cataract as a Protein-Aggregation Disease (\u003ci\u003eYongting Wang and Jonathan A. King\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e23 Islet Amyloid Polypeptide (\u003ci\u003eAndisheh Abedini and Daniel P. Raleigh\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART III ROLE OF ACCESSORY MOLECULES AND RISK FACTORS.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e24 Role of Metals in Alzheimer Disease (\u003ci\u003eBlaine R. Roberts and Ashley I. Bush\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e25 Why Study the Role of Heparan Sulfate in In Vivo Amyloidogenesis? (\u003ci\u003eRobert Kisilevsky and John Ancsin\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e26 Serum Amyloid P Component (\u003ci\u003eSimon Kolstoe and Steve Wood\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e27 Role of Oxidatively Stressed Lipids in Amyloid Formation and Toxicity (\u003ci\u003ePaul H. Axelsen and Hiroaki Komatsu\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e28 Role of Oxidative Stress in Protein Misfolding and\/or Amyloid Formation (\u003ci\u003eJohanna C. Scheinost, Daniel P. Witter, Grant E. Boldt, and Paul Wentworth, Jr.\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e29 Aging and Aggregation-Mediated Proteotoxicity (\u003ci\u003eEhud Cohen and Andrew Dillin\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART IV MEDICAL ASPECTS OF DISEASE: DIAGNOSIS AND CURRENT THERAPIES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e30 Imaging of Misfolded Proteins (\u003ci\u003eHarry LeVine, III\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e31 Diagnosis of Systemic Amyloid Diseases (\u003ci\u003eMorie A. Gertz\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e32 Identification of Biomarkers for Diagnosis of Amyloid Diseases: Quantitative Free Light-Chain Assays (\u003ci\u003eJerry A. Katzmann\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e33 Real-Time Observation of Amyloid-b Fibril Growth by Total Internal Reflection Fluorescence Microscopy (\u003ci\u003eTadato Ban and Yuji Goto\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e34 Current and Future Therapies for Alzheimer Disease (\u003ci\u003eParamita Chakrabarty, Pritam Das, and Todd E. Golde\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e35 Current Therapies for Light-Chain Amyloidosis (\u003ci\u003eAngela Dispenzieri and Shaji Kumar\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e36 Familial and Senile Amyloidosis Caused by Transthyretin (\u003ci\u003eSteven R. Zeldenrust and Merrill D. Benson\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e37 Identifying Targets in a-Synuclein Metabolism to Treat Parkinson Disease and Related Disorders (\u003ci\u003eJulianna Tomlinson, Valerie Cullen, and Michael G. Schlossmacher\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e38 Emerging Molecular Targets in the Therapy of Dialysis-Related Amyloidosis (\u003ci\u003eGennaro Esposito and Vittorio Bellotti\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e39 Familial Amyloidosis Caused by Lysozyme (\u003ci\u003eMireille Dumoulin\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e40 Therapeutic Prospects for Polyglutamine Disease (\u003ci\u003eMaria Pennuto and Kenneth H. Fischbeck\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART V APPROACHES FOR NEW AND EMERGING THERAPIES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e41 Chemistry and Biology of Amyloid Inhibition (\u003ci\u003eMark A. Findeis\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e42 Immunotherapy in Secondary and Light-Chain Amyloidosis (\u003ci\u003eJonathan Wall\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e43 Anti-Misfolding and Anti-Fibrillization Therapies for Protein Misfolding Disorders (\u003ci\u003eZane Martin and Claudio Soto\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e44 Therapies Aimed at Controlling Gene Expression, Including Up-Regulating a Chaperone or Down-Regulating an Amyloidogenic Protein (\u003ci\u003eGregor P. Lotz and Paul J. Muchowski\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e45 Understanding and Ameliorating the TTR Amyloidoses (\u003ci\u003eSteven M. Johnson, R. Luke Wiseman, Natalia Reixach, Johan F. Paulsson, Sungwook Choi, Evan T. Powers, Joel N. Buxbaum, and Jeffery W. Kelly\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003eINDEX.\u003c\/p\u003e  “The book is very well organized and clearly written, and contains a large number of nice figures and illustrations, some in color, which certainly help to simplify the complex thematic material. The contributions provide a sufficient body of background information, are concisely written, and contain many references, which make them valuable bibliographic sources.” (\u003ci\u003eAngewandte Chemie\u003c\/i\u003e, December 2010)  \u003cp\u003e\"In this valuable contribution to the understanding of protein- deposition diseases, Ramirez-Alvarado (biochemistry and molecular biology, Mayo Clinic College of Medicine) and international contributors to 45 chapters present an integrated approach to the process and consequences of protein aggregation.\" (\u003ci\u003eBook News\u003c\/i\u003e, September 2010)\u003c\/p\u003e  \u003cb\u003eMARINA RAMIREZ-ALVARADO\u003c\/b\u003e is an Assistant professor of Biochemistry and Molecular Biology at the Mayo Clinic. Despite being a young investigator, she is already a world leader in the study of molecular determinants of light chain amyloidosis, a reare misfolding disease.  \u003cp\u003e\u003cb\u003eJEFFERY W. KELLY\u003c\/b\u003e is a Professor of Chemistry and Molecular and Experimental Medicine at the Scripps Research Institute. He is one of the leading authorities in the field of protein misfolding, with over 250 publications to his credit.\u003c\/p\u003e \u003cp\u003e\u003cb\u003eCHRISTOPHER M. DOBSON\u003c\/b\u003e is a Professor in the Department of Chemistry at the University of Cambridge. Dr. Dobson is a leading researcher studying the structure and biochemical bases of protein misfolding diseases and has over 500 publications.\u003c\/p\u003e  \u003cb\u003eAn in-depth look at new discoveries in protein misfolding disease research\u003c\/b\u003e  \u003cp\u003eProtein misfolding\/aggregation diseases are a medical puzzle that has baffled researchers for many years. These diseases are characterized by the presence of protein deposits, or amyloid fibrils, which gather in the intracellular and\/or extracellular spaces in a variety of tissues. Unchecked, the process of amyloidogenesis leads to proteotoxicity, cell loss, and eventually organ dysfunction, and causes such well-known and devastating diseases as Alzheimer's, Parkinson's, and Mad Cow.\u003c\/p\u003e \u003cp\u003eEmploying a diversity of research approaches, including chemical and biophysical, cellular, and animal models, the authors investigate various amyloid diseases and outline progress made in understanding them in this important book. Included are novel strategies to combat a wide variety of degenerative diseases. With a systematic overview, Protein Misfolding Diseases:\u003c\/p\u003e \u003cul\u003e \u003cli\u003e \u003cp\u003eEmphasizes therapeutics in an amyloid disease context, which helps bridge the gap between basic science and pharmaceutical applications to protein misfolding diseases\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eProvides a comprehensive survey of many of the topics surrounding the universal biological aspects of protein misfolding\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eIncludes a Foreword by R. John Ellis, International Gairdner Award Winner 2004\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eIs coedited by Jeffery W. Kelly and Christopher M. Dobson, leaders in the field of protein biochemistry\u003c\/p\u003e \u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003e\u003ci\u003eProtein Misfolding Diseases\u003c\/i\u003e uses the latest medical data from expert scientists and protein misfolding clinicians to launch a multi-targeted assault on the process of amyloid fibril formation. Fresh insight into the etiology of these maladies helps researchers gain a thorough understanding of the bases of these diseases and offers guidance in designing therapeutic strategies to build on promising new findings—and bring hope one step closer to reality.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989880291557,"sku":"NP9780471799283","price":263.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9780471799283.jpg?v=1761785773","url":"https:\/\/k12savings.com\/es\/products\/protein-misfolding-diseases-isbn-9780471799283","provider":"K12savings","version":"1.0","type":"link"}