Linked Life Data

1740189

Source:http://linkedlifedata.com/resource/pubmed/id/1740189

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-3-26
pubmed:abstractText
Selective degradation of cellular proteins serves to eliminate abnormal proteins and to mediate the turnover of certain short-lived proteins, many of which have regulatory functions. In eukaryotes a major pathway for selective protein degradation is ATP-dependent and is mediated by the ubiquitin system. This pathway involves substrate recognition by components of a ubiquitin-protein ligase system, covalent attachment of ubiquitin moieties to proteolytic substrates, and subsequent degradation of these conjugates by a multicatalytic protease complex. Recent genetic evidence suggests that the remarkable selectivity of this process is largely controlled at the level of substrate recognition by the ubiquitin ligase system. In Saccharomyces cerevisiae, ubiquitin-conjugating enzymes UBC1, UBC4 and UBC5 have been identified as key components of this highly conserved degradation pathway. Genetic analysis indicates that ubiquitin-dependent proteolysis is essential for cell viability and that UBC4 and UBC5 enzymes are essential components of the eukaryotic stress response.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-4754
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
48
pubmed:geneSymbol
UBC, UBC1, UBC4, UBC5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
172-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Genetic analysis of ubiquitin-dependent protein degradation.
pubmed:affiliation
Friedrich-Miescher-Laboratorium, Max-Planck-Gesellschaft, Tübingen, Germany.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't