Linked Life Data

10370241

Source:http://linkedlifedata.com/resource/pubmed/id/10370241

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-8-4
pubmed:abstractText
Hsp90 is a molecular chaperone associated with the folding of signal-transducing proteins, such as steroid hormone receptors and protein kinases. Results from recent studies have shed light on the structure of Hsp90 and have demonstrated that it can bind to and hydrolyse ATP. Hsp90 forms several discrete subcomplexes, each containing distinct groups of co-chaperones that function in folding pathways. Although Hsp90 is not generally involved in the folding of nascent polypeptide chains, there is a growing list of proteins whose activity depends on its function, including heat-shock factor. This review addresses recent developments in our understanding of the structure and function of Hsp90.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0962-8924
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
262-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Hsp90's secrets unfold: new insights from structural and functional studies.
pubmed:affiliation
Dept of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, NY 10029, USA. acaplan@smtplink.mssm.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't