Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils

Journal of Biological Chemistry

Volumn 282, Issue 16, 2007, Pages 11931-11940

  Lian, Hui Yong ^a,d   Zhang, Hong ^a,d   Zhang, Zai Rong ^a,d   Loovers, Harriët M ^b   Jones, Gary W ^b   Rowling, Pamela J E ^c   Itzhaki, Laura S ^c   Zhou, Jun Mei ^a   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b NATIONAL UNIVERSITY OF IRELAND   (Ireland)

^c HUTCHISON MRC RESEARCH CENTRE   (United Kingdom)

^d UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRILS; INHIBITORY EFFECTS; LAG PHASE; NATIVE STATE;

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; CURING; GENE EXPRESSION; NUCLEATION; YEAST;

PROTEINS;

AMYLOID; BOVINE SERUM ALBUMIN; CHAPERONE; GLUTATHIONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PRION PROTEIN; THIOFLAVINE; UNCLASSIFIED DRUG; URE2 PROTEIN; HEAT SHOCK PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SIS1 PROTEIN, S CEREVISIAE; THIAZOLE DERIVATIVE; URE2 PROTEIN, S CEREVISIAE; YDJ1 PROTEIN, S CEREVISIAE;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CARBOXY TERMINAL SEQUENCE; GEL PERMEATION CHROMATOGRAPHY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; SURFACE PLASMON RESONANCE; YEAST; CHEMISTRY; HUMAN; KINETICS; METABOLISM; PRION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

BOVINAE; SACCHAROMYCES CEREVISIAE;

AMYLOID; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; MICROSCOPY, ATOMIC FORCE; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SURFACE PLASMON RESONANCE; THIAZOLES;

EID: 34249689651     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M606856200     Document Type: Article

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