Balance between folding and degradation for Hsp90-dependent client proteins: A key role for CHIP

Biochemistry

Volumn 49, Issue 35, 2010, Pages 7428-7438

  Kundrat, Lenka ^a   Regan, Lynne ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; MACHINERY; MAMMALS; PROTEIN FOLDING; STOICHIOMETRY;

DISSOCIATION CONSTANT; FOLDING PATHWAY; GROWTH CONDITIONS; IN-VITRO; IN-VIVO; IN-VIVO MEASUREMENT; MOLECULAR CHAPERONES; NORMAL CONDITION; PROTEIN DEGRADATION; QUANTITATIVE MODELS; UBIQUITIN LIGASES; UBIQUITINATION; VARIOUS SUBSTRATES;

DEGRADATION;

CHAPERONE; DNA; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HYBRID PROTEIN; UBIQUITIN PROTEIN LIGASE; HOMEODOMAIN PROTEIN; STUB1 PROTEIN, HUMAN;

ARTICLE; BACTERIAL CELL; COMPLEX FORMATION; ESCHERICHIA COLI; HUMAN; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; SURFACE PLASMON RESONANCE; UBIQUITINATION; CHEMISTRY; METABOLISM;

MAMMALIA;

HOMEODOMAIN PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; PROTEIN FOLDING; SURFACE PLASMON RESONANCE; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 77956144557     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100386w     Document Type: Article

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