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rdf:type |
|
|
lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1990-7-18
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pubmed:abstractText |
The temperature-sensitive bacteriophage lambda cI857 repressor protein rapidly renatures after thermal inactivation. E. coli mutants in the heat shock protein genes dnaK, dnaJ, and grpE do not efficiently reactivate heat-denatured repressor. Our results suggest that protein refolding is promoted by heat shock proteins and that such a process is the basis of the homeostatic role played by these proteins in the heat shock response.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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|
pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
61
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1013-20
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pubmed:dateRevised |
2008-8-14
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pubmed:meshHeading |
pubmed-meshheading:2140957-Bacteriophage lambda,
pubmed-meshheading:2140957-DNA Probes,
pubmed-meshheading:2140957-DNA-Binding Proteins,
pubmed-meshheading:2140957-Escherichia coli,
pubmed-meshheading:2140957-Galactokinase,
pubmed-meshheading:2140957-Genotype,
pubmed-meshheading:2140957-Heat-Shock Proteins,
pubmed-meshheading:2140957-Kinetics,
pubmed-meshheading:2140957-Mutation,
pubmed-meshheading:2140957-Protein Binding,
pubmed-meshheading:2140957-Protein Conformation,
pubmed-meshheading:2140957-Protein Denaturation,
pubmed-meshheading:2140957-Repressor Proteins,
pubmed-meshheading:2140957-Transcription Factors,
pubmed-meshheading:2140957-Viral Proteins,
pubmed-meshheading:2140957-Viral Regulatory and Accessory Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Renaturation of denatured lambda repressor requires heat shock proteins.
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pubmed:affiliation |
Institute of Cancer Research, College of Physicians & Surgeons, Columbia University, New York, New York 10032.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Retracted Publication
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