Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1998-8-11
|
| pubmed:abstractText |
The defining feature of the Hsp40 chaperone family is a approximately 70-amino-acid-residue signature, termed the J domain, that is necessary for orchestrating interactions with its Hsp70 chaperone partner(s). J-domain proteins play important regulatory roles as co-chaperones, recruiting Hsp70 partners and accelerating the ATP-hydrolysis step of the chaperone cycle. Certain proteins could have acquired a J domain in order to present a specific substrate(s) to an Hsp70 partner and thus capitalize upon chaperone activities when carrying out cellular functions. J-domain proteins participate in complex biological processes, such as cell-cycle control by DNA tumor viruses, regulation of protein kinases and exocytosis.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0968-0004
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
23
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
222-7
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9644977-Amino Acid Sequence,
pubmed-meshheading:9644977-Animals,
pubmed-meshheading:9644977-HSP70 Heat-Shock Proteins,
pubmed-meshheading:9644977-Humans,
pubmed-meshheading:9644977-Models, Molecular,
pubmed-meshheading:9644977-Molecular Sequence Data,
pubmed-meshheading:9644977-Protein Conformation,
pubmed-meshheading:9644977-Structure-Activity Relationship
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
The J-domain family and the recruitment of chaperone power.
|
| pubmed:affiliation |
Dépt de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, Switzerland. william.kelley@medecine.unige.ch
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|