Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

Molecular Microbiology

Volumn 50, Issue 2, 2003, Pages 585-595

  Mogk, Axel ^a,b   Deuerling, Elke ^a   Vorderwülbecke, Sonja ^a   Vierling, Elizabeth ^c   Bukau, Bernd ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b UNIVERSITY OF FREIBURG   (Germany)

^c UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN CLPB; HEAT SHOCK PROTEIN IBPA; HEAT SHOCK PROTEIN IBPB; PROTEIN DNAK; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; HIGH TEMPERATURE; INHIBITION KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION;

ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0142125283     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03710.x     Document Type: Article

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