Linked Life Data

12463161

Source:http://linkedlifedata.com/resource/pubmed/id/12463161

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-12-4
pubmed:abstractText
Intracellular proteins are targeted for degradation by the covalent attachment of chains of the small protein ubiquitin; a process known as ubiquitylation. Many proteins are phosphorylated prior to ubiquitylation, and therefore ubiquitylation and degradation of these proteins is regulated by kinase activity and signalling cascades. Many ubiquitylated proteins are degraded by the 26 S proteasome complex, which is found in the cytosol and nucleus. The 26 S proteasome consists of a 20 S core with proteolytic activity and 18 S regulatory complexes containing ATPases and ubiquitin-chain-binding proteins. Proteins degraded by the ubiquitin-proteasome pathway include cyclins and other regulators of the cell cycle, and transcription factors. Abnormal polypeptides are also degraded by the ubiquitin pathway, including abnormal polypeptides in the endoplasmic reticulum, which are translocated back out of the endoplasmic reticulum prior to ubiquitylation and degradation by the proteasome. The ubiquitin-proteasome pathway is implicated in numerous diseases including cancer and neurodegenerative diseases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0071-1365
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
51-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
The ubiquitin-proteasome pathway of intracellular proteolysis.
pubmed:affiliation
Laboratory of Intracellular Proteolysis, School of Biomedical Sciences, University of Nottingham Medical School, Queen's Medical Centre, Nottingham NG7 2UH, U.K.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't