The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein α-synuclein

Journal of Biological Chemistry

Volumn 284, Issue 45, 2009, Pages 31190-31199

  Falsone, S Fabio ^a   Kungl, Andreas J ^b   Rek, Angelika ^b   Cappai, Roberto ^c   Zangger, Klaus ^a  

^a UNIVERSITY OF GRAZ   (Austria)

^b UNIVERSITY OF GRAZ   (Austria)

^c UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL FORMATION; AMYLOIDOGENESIS; CONFORMATIONAL FLUCTUATIONS; FIBRIL FORMATION; FIBRIL GROWTH; FOLDING PROCESS; IN-VITRO; INTRINSICALLY UNSTRUCTURED PROTEINS; MICROMOLAR RANGE; MOLECULAR CHAPERONES; SYNUCLEIN; TIGHTLY-COUPLED;

OLIGOMERS; PROTEINS;

GLYCOPROTEINS;

ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; AMYLOID; HEAT SHOCK PROTEIN 90; OLIGOMER;

ARTICLE; CELL VACUOLE; CONTROLLED STUDY; FIBER; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; STOICHIOMETRY;

ADENOSINE TRIPHOSPHATE; ALPHA-SYNUCLEIN; AMYLOID; HSP90 HEAT-SHOCK PROTEINS; HUMANS; KINETICS; MODELS, BIOLOGICAL; PARKINSON DISEASE; PROTEIN BINDING; PROTEIN FOLDING;

EID: 71449111785     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.057240     Document Type: Article

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