Linked Life Data

20694452

Source:http://linkedlifedata.com/resource/pubmed/id/20694452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-8-9
pubmed:abstractText
Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this review, we will describe the different data that demonstrate a role for HSP90, HSP70, HSP27, and áB-crystallin in the partitioning of proteins to either one of these pathways, referred as protein triage.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1537-744X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1543-52
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Heat shock proteins: cell protection through protein triage.
pubmed:affiliation
INSERM U866, University of Burgundy, Dijon, France.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't