The chaperone αb-crystallin uses different interfaces to capture an amorphous and an amyloid client

Nature Structural and Molecular Biology

Volumn 22, Issue 11, 2015, Pages 898-905

  Mainz, Andi ^a,b,e   Peschek, Jirka ^a,f   Stavropoulou, Maria ^a   Back, Katrin C ^a   Bardiaux, Benjamin ^c   Asami, Sam ^a   Prade, Elke ^a   Peters, Carsten ^a   Weinkauf, Sevil ^a   Buchner, Johannes ^a   Reif, Bernd ^a,d  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^c INSTITUT PASTEUR   (France)

^d INSTITUTE OF EPIDEMIOLOGY   (Germany)

^e TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^f UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; AMYLOID; AMYLOID BETA PROTEIN[1-40]; CHAPERONE; LYSOZYME; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN HOMEOSTASIS; PROTEIN PROTEIN INTERACTION; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PROTEIN CONFORMATION;

ALPHA-CRYSTALLIN B CHAIN; AMYLOID; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 84948073235     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3108     Document Type: Article

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