Heat-induced oligomerization of gp96 occurs via a site distinct from substrate binding and is regulated by ATP

Biochemical and Biophysical Research Communications

Volumn 323, Issue 4, 2004, Pages 1163-1171

  Thorne, Meghan E ^a   McQuade, Kristi L ^a  

^a BRADLEY UNIVERSITY   (United States)

Author keywords

Chaperone; Gp96; GRP94; Oligomerization

Indexed keywords

ADENOSINE 5' (N ETHYLCARBOXAMIDE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONE; DIMER; GLYCOPROTEIN GP 96; MONOMER;

ARTICLE; BINDING AFFINITY; HEAT SHOCK; HEATING; HYDROLYSIS; OLIGOMERIZATION; PRIORITY JOURNAL; REGULATORY MECHANISM; STATISTICAL SIGNIFICANCE; TEMPERATURE DEPENDENCE;

ADENOSINE TRIPHOSPHATE; BINDING SITES; DIMERIZATION; ENZYME ACTIVATION; ENZYME STABILITY; HEAT; HSP70 HEAT-SHOCK PROTEINS; KINETICS; MEMBRANE PROTEINS; MOLECULAR WEIGHT; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 4644338644     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.215     Document Type: Article

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