Activation of the redox-regulated molecular chaperone Hsp33 - A two-step mechanism

Structure

Volumn 9, Issue 5, 2001, Pages 377-387

  Graumann, Johannes ^a   Lilie, Hauke ^c   Tang, Xianli ^a   Tucker, Katherine A ^a   Hoffmann, J�rg H ^a   Vijayalakshmi, J ^a   Saper, Mark ^a,b   Bardwell, James C A ^a   Jakob, Ursula ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c University of Halle   (United Kingdom)

Author keywords

Dimerization; Disulfide bond formation; Heat shock protein; Oxidative stress; Redox regulation; Structure

Indexed keywords

CHAPERONE; DIMER; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; HYDROGEN PEROXIDE; MONOMER; UNCLASSIFIED DRUG; ZINC;

ACCELERATION; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPARATIVE STUDY; CONCENTRATION RESPONSE; DIMERIZATION; DISULFIDE BOND; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN STRUCTURE; REGULATORY MECHANISM; TEMPERATURE SENSITIVITY;

BACTERIAL PROTEINS; DIMERIZATION; DISULFIDES; ENZYME ACTIVATION; HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; MUTAGENESIS; OXIDATION-REDUCTION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; ZINC;

EID: 0034991998     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00599-8     Document Type: Article

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