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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6583
|
pubmed:dateCreated |
1996-7-9
|
pubmed:abstractText |
The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0028-0836
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
381
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
571-9
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading | |
pubmed:year |
1996
|
pubmed:articleTitle |
Molecular chaperones in cellular protein folding.
|
pubmed:affiliation |
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.
|
pubmed:publicationType |
Journal Article,
Review
|