Linked Life Data

21474563

Source:http://linkedlifedata.com/resource/pubmed/id/21474563

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-5-2
pubmed:abstractText
Proteins in all cells turnover continuously such that rigorous control of proteolysis is required to govern levels of proteins with vastly different half-lives and actions including those regulating transcription, metabolic pathways, or the breakdown of muscle proteins to amino acids used in gluconeogenesis or the synthesis of new proteins. Critical cellular functions would be disrupted without precise regulation of protein degradation. Thus, it is surprising that the bulk of protein in all cells is degraded by the ATP-dependent, ubiquitin-proteasome system. The system achieves remarkable specificity by selective conjugation of ubiquitin (Ub) to a doomed protein in a process catalyzed by >1000 ubiquitin ligases that recognize individual substrate proteins. Because the pathogenesis of certain kidney diseases and their complications are linked to the function of the ubiquitin-proteasome system, understanding its mechanisms could lead to novel therapies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1533-3450
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 by the American Society of Nephrology
pubmed:issnType
Electronic
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
821-4
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Proteolysis by the ubiquitin-proteasome system and kidney disease.
pubmed:affiliation
Nephrology Division, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural