Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK

Journal of Biological Chemistry

Volumn 278, Issue 33, 2003, Pages 31033-31042

  Mogk, Axel ^a,b   Schlieker, Christian ^a   Friedrich, Kenneth L ^c   Schönfeld, Hans Joachim ^d   Vierling, Elizabeth ^c   Bukau, Bernd ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b UNIVERSITY OF FREIBURG   (Germany)

^c UNIVERSITY OF ARIZONA   (United States)

^d F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; BIOCHEMISTRY; CHEMICAL BONDS; CONFORMATIONS; DISSOCIATION; SOLUBILITY;

MOLECULAR CHAPERONES;

PROTEINS;

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; PROTEIN DNAK;

ARTICLE; CHEMICAL REACTION; COMPLEX FORMATION; DISSOCIATION; HEAT STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION; QUALITY CONTROL; SOLUBILITY;

ANIMALS; ESCHERICHIA COLI PROTEINS; HEAT; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MALATE DEHYDROGENASE; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; SOLUBILITY;

EID: 0042733148     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M303587200     Document Type: Article

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