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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-10-15
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pubmed:abstractText |
Molecular chaperones are known to facilitate cellular protein folding. They bind non-native proteins and orchestrate the folding process in conjunction with regulatory cofactors that modulate the affinity of the chaperone for its substrate. However, not every attempt to fold a protein is successful and chaperones can direct misfolded proteins to the cellular degradation machinery for destruction. Protein quality control thus appears to involve close cooperation between molecular chaperones and energy-dependent proteases. Molecular mechanisms underlying this interplay have been largely enigmatic so far. Here we present a novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11600451-10075921,
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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 |
Oct
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
885-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11600451-Animals,
pubmed-meshheading:11600451-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11600451-HSP90 Heat-Shock Proteins,
pubmed-meshheading:11600451-Ligases,
pubmed-meshheading:11600451-Models, Biological,
pubmed-meshheading:11600451-Models, Genetic,
pubmed-meshheading:11600451-Molecular Chaperones,
pubmed-meshheading:11600451-Protein Binding,
pubmed-meshheading:11600451-Protein Folding,
pubmed-meshheading:11600451-Protein Structure, Tertiary,
pubmed-meshheading:11600451-Ubiquitin
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pubmed:year |
2001
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pubmed:articleTitle |
From the cradle to the grave: molecular chaperones that may choose between folding and degradation.
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pubmed:affiliation |
Institut für Zellbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Ulrich-Haberland-Strasse 61a, D-53121 Bonn, Germany. hoehfeld@uni-bonn.de
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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