Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
|
pubmed:dateCreated |
1997-12-9
|
pubmed:abstractText |
Eukaryotes contain a highly conserved multi-enzyme system that covalently links ubiquitin to a variety of intracellular proteins that bear degradation signals recognized by this system. The resulting ubiquitin-protein conjugates are degraded by the 26S proteasome, a large ATP-dependent protease. Pathways that involve ubiquitin underlie a multitude of processes, including cell differentiation, the cell cycle and responses to stress.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0968-0004
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
22
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
383-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading | |
pubmed:year |
1997
|
pubmed:articleTitle |
The ubiquitin system.
|
pubmed:affiliation |
Division of Biology, California Institute of Technology, Pasadena 91125, USA. avarsh@cco.caltech.edu
|
pubmed:publicationType |
Journal Article
|