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Bio-nanoimaging : protein misfolding & aggregation

Author: Vladimir N Uversky; Yuri L Lyubchenko
Publisher: Amsterdam : Elsevier/AP, [2014]
Edition/Format:   Print book : EnglishView all editions and formats

Provides an introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. This book focuses on nanoimaging  Read more...


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Additional Physical Format: Online version:
London : Academic Press/Elsevier, [2014]
Document Type: Book
All Authors / Contributors: Vladimir N Uversky; Yuri L Lyubchenko
ISBN: 0123944317 9780123944313
OCLC Number: 844308245
Description: xix, 526 pages : illustrations (some color) ; 29 cm
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 -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 -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
Responsibility: edited by Vladimir N. Uversky, Yuri L. Lyubchenko.
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"Among the topics are conformation-dependent antibodies as tools for characterizing amyloid protein aggregates, studying the molecular determinants of protein oligomerization in neurodegenerative Read more...

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