CLPB gene

Known as: ClpB, E. COLI, HOMOLOG OF, ankyrin-repeat containing bacterial clp fusion, HSP78 
 
National Institutes of Health

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Highly Cited
2013
Highly Cited
2013
HSP-100 protein machines, such as ClpB, play an essential role in reactivating protein aggregates that can otherwise be lethal to… (More)
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Review
2009
Review
2009
Heat-shock protein 104 (Hsp104) and caseinolytic peptidase B (ClpB), members of the AAA+ superfamily, are molecular machines… (More)
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Highly Cited
2007
Highly Cited
2007
Two members of the AAA+ superfamily, ClpB and Hsp104, collaborate with Hsp70 and Hsp40 to rescue aggregated proteins. However… (More)
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Highly Cited
2004
Highly Cited
2004
Cell survival under severe thermal stress requires the activity of the ClpB (Hsp104) AAA+ chaperone that solubilizes and… (More)
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Highly Cited
2004
Highly Cited
2004
The AAA+ protein ClpB cooperates with the DnaK chaperone system to solubilize and refold proteins from an aggregated state. The… (More)
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Highly Cited
2003
Highly Cited
2003
ClpB of Escherichia coli is an ATP-dependent ring-forming chaperone that mediates the resolubilization of aggregated proteins in… (More)
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Highly Cited
1999
Highly Cited
1999
UNLABELLED We systematically analyzed the capability of the major cytosolic chaperones of Escherichia coli to cope with protein… (More)
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Highly Cited
1999
Highly Cited
1999
Functional chaperone cooperation between Hsp70 (DnaK) and Hsp104 (ClpB) was demonstrated in vitro. In a eubacterium Thermus… (More)
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Highly Cited
1999
Highly Cited
1999
ClpB is a heat-shock protein from Escherichia coli with an unknown function. We studied a possible molecular chaperone activity… (More)
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Highly Cited
1998
Highly Cited
1998
We have constructed an Escherichia coli strain lacking the small heat shock proteins IbpA and IbpB and compared its growth and… (More)
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