ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

Journal of Biological Chemistry

Volumn 274, Issue 40, 1999, Pages 28083-28086

  Zolkiewski, Michal ^a  

^a KANSAS STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; LUCIFERASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME REACTIVATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATASES; ANIMALS; BACTERIAL PROTEINS; CATTLE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES; MOLECULAR CHAPERONES; PROTEIN RENATURATION;

BACTERIA (MICROORGANISMS); BOVINAE; ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033214052     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.40.28083     Document Type: Article

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