Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro

Journal of Biological Chemistry

Volumn 281, Issue 44, 2006, Pages 33182-33191

  Evans, Christopher G ^a   Wisén, Susanne ^a   Gestwicki, Jason E ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID; FIBRILS; MOLECULAR CHAPERONES; PHARMACOLOGICAL STIMULATION; PHENOTYPES;

CONFORMATIONS; DISEASES; METABOLISM; OLIGOMERS; PHARMACOKINETICS; PHYSIOLOGICAL MODELS; POLYPEPTIDES; STARCH;

PROTEINS;

ADENOSINE TRIPHOSPHATASE; AMYLOID BETA PROTEIN[1-42]; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; NUCLEOTIDE DERIVATIVE; OLIGOMER; PYRIMIDINE DERIVATIVE; SW 02; THIOFLAVINE; UNCLASSIFIED DRUG;

AMYLOID NEUROPATHY; ARTICLE; COMBINATION CHEMOTHERAPY; DRUG INHIBITION; DRUG POTENCY; DRUG POTENTIATION; ENZYME ACTIVITY; HUMAN; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; STOICHIOMETRY;

ADENOSINE TRIPHOSPHATASES; AMYLOID BETA-PROTEIN; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; PROTEIN BINDING; RECOMBINANT PROTEINS; TIME FACTORS;

EID: 33845918172     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M606192200     Document Type: Article

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