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Author:   Vladimir N Uversky (Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, United States) ,  Yuri Lyubchenko
Publisher:   Elsevier Science Publishing Co Inc
Imprint:   Academic Press Inc
Dimensions:   Width: 21.60cm , Height: 3.30cm , Length: 27.60cm
Weight:   1.710kg
ISBN:  

9780123944313

ISBN 10:   0123944317
Pages:   552
Publication Date:   07 January 2014
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Active
Availability:   Manufactured on demand  
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Table of Contents

Part 1. Nanotechnology and nanoimaging of aggregating proteins Nanoimaging of aggregated proteins; Cryoelectron microscopy of beta(2)-microglobulin; Amyloid fibril length quantification by AFM; Seeing fibril formation in real time; Studying amyloidogensis by FRET; Structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy; Analyzing amyloid fibril structure by scanning transmission electron microscopy; Magic angle spinning NMR of amyloid fibrils; Analyzing protein deposits in vivo by confocal laser multiphoton laser scanning microscopy; Amyloid imaging agents; Reporters of amyloid structure; Immunohistochemical detection of amyloid components; Scanning tunneling microscopy of protein deposits; Probing of protein misfolding with single molecule force spectroscopy; Single molecule characterization of a-synuclein in aggregation-prone states Part 2. Polymorphism of protein misfolded and aggregated species Fibrillar polymorphism; Ab fibril polymorphism; Prefibrillar Ab oligomers; Structural heterogeneity of in vitro and ex vivo amyloid assemblies; Polymorphism of tau fibrils; Amyloid-like protofibrils with different physical properties; Micelle-Like Architecture of the Amyloid-ß Peptide; Insulin oligomers; Worm-like amyloid fibrils of mouse prion protein; Apolipoprotein C-II Amyloid Fibrils; Amylin oligomers and fibrils; Amyloid fibrils of human stefins; Fibrillar structure of Sup35 in vivo; Dopamine-induced a-synuclein oligomers ; Amyloid spherulites; A stable lipid-induced aggregate of alpha-synuclein Part 3. Polymorphism of protein misfolding and aggregation processes Multiple pathways of lysozyme aggregation; Structure-function study of amyloid ion channels in neurodegenerative diseases; Amyloid ß-protein assembly; Molecular mechanisms underlying alpha synucelin misassembly; Multiple pathways of amyloid assembly /disassembly studied by AFM; Sequestering of metastable proteins with essential cellular functions by amyloid-like aggregates; Misfolded intermediate of a PDZ domain; Structural characterization of the amyloidogenic state of human lysozyme; Landscape Model of Filamentous Protein Aggregation; Micelle formation by human islet amyloid polypeptide; Effect of anionic polysaccharide on ß-lactoglobulin fibrillation

Reviews

Among the topics are conformation-dependent antibodies as tools for characterizing amyloid protein aggregates, studying the molecular determinants of protein oligomerization in neurodegenerative disorders by bimolecular fluorence complimentation, possible function and toxicity of multiple oligomeric/conformational states of the globular protein human stefin B. --ProtoView.com, February 2014

Among the topics are conformation-dependent antibodies as tools for characterizing amyloid protein aggregates, studying the molecular determinants of protein oligomerization in neurodegenerative disorders by bimolecular fluorence complimentation, possible function and toxicity of multiple oligomeric/conformational states of the globular protein human stefin B. --ProtoView.com, February 2014

Author Information

Prof. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC, F.A.I.M.B.E., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF), is a pioneer in the field of protein intrinsic disorder. He has made a number of groundbreaking contributions in the field of protein folding, misfolding, and intrinsic disorder. He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, moved to the University of California Santa Cruz. In 2004, joined the Indiana University-Purdue University Indianapolis as a Senior Research Professor. Since 2010, Professor Uversky is with USF, where he works on various aspects of protein intrinsic disorder phenomenon and on analysis of protein folding and misfolding processes. Prof. Uversky has authored over 1250 scientific publications and edited several books and book series on protein structure, function, folding, misfolding, and intrinsic disorder. He is also serving as an editor in a number of scientific journals. He was a co-founder of the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference. Prof. Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.

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