Linked Life Data

18414022

Source:http://linkedlifedata.com/resource/pubmed/id/18414022

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2008-5-29
pubmed:abstractText
The Hsp90 proteomic network is expansive and includes a variety of cell processes operating within the cytoplasm and nucleoplasm. Though the functional significance of the extensive interactions has not been defined, we suggest that the Hsp90 molecular chaperone machinery promotes dynamic behaviors for client proteins that is critical to achieve homeostasis. A general rapid action by cell factors would permit both proper assembly of biological complexes and efficient transitions between distinct structures. Here, we describe why the properties that are inherent to molecular chaperones place these proteins in a unique position to drive the dynamic cellular environment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1006-12
pubmed:dateRevised
2008-9-23
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
HSP90: the Rosetta stone for cellular protein dynamics?
pubmed:affiliation
Department of Cell and Developmental Biology, University of Illinois, Urbana, Illinois, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural