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Bio-Nanoimaging: Protein Misfolding and Aggregation

Bio-Nanoimaging: Protein Misfolding and Aggregation (Hardcover)

Vladimir Uversky (지은이)
Academic Press Inc
354,910원

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Bio-Nanoimaging: Protein Misfolding and Aggregation
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책 정보

· 제목 : Bio-Nanoimaging: Protein Misfolding and Aggregation (Hardcover) 
· 분류 : 외국도서 > 과학/수학/생태 > 과학 > 생명과학 > 생물학
· ISBN : 9780123944313
· 쪽수 : 552쪽
· 출판일 : 2013-11-26

목차

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 α-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-β 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 α-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 β-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 β-lactoglobulin fibrillation

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