Degradation of wild-type alpha-synuclein by a molecular chaperone leads to reduced aggregate formation

Cell Biochemistry and Function

Volumn 23, Issue 2, 2005, Pages 125-132

  Kong, Byungmoon ^a   Chae, Youngkee ^a   Lee, Kyunghee ^a  

^a Sejong University   (South Korea)

Author keywords

Aggregate formation; Aging; Alpha synuclein; Hsp104p; Molecular chaperone; Parkinson's disease

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; AMYLOID; CHAPERONE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 104P; HISTIDINE; MUTANT PROTEIN; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM; CELL PROTECTION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DEGENERATIVE DISEASE; DISSOCIATION; FLUORESCENCE; GENE EXPRESSION SYSTEM; IN VITRO STUDY; IN VIVO STUDY; LEWY BODY; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; SOLUBILIZATION; STRESS;

ALPHA-SYNUCLEIN; ESCHERICHIA COLI; GLUTATHIONE TRANSFERASE; HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES; NERVE TISSUE PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SYNUCLEINS;

BACTERIA (MICROORGANISMS);

EID: 14944377082     PISSN: 02636484     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbf.1219     Document Type: Article

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