Linked Life Data

17218518

Source:http://linkedlifedata.com/resource/pubmed/id/17218518

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5809
pubmed:dateCreated
2007-1-12
pubmed:abstractText
Ubiquitination is a reversible posttranslational modification of cellular proteins, in which a 76-amino acid polypeptide, ubiquitin, is primarily attached to the epsilon-amino group of lysines in target proteins. Ubiquitination is a major player in regulating a broad host of cellular processes, including cell division, differentiation, signal transduction, protein trafficking, and quality control. Aberrations in the ubiquitination system are implicated in pathogenesis of some diseases, certain malignancies, neurodegenerative disorders, and pathologies of the inflammatory immune response. Here, we discuss the proteasome-independent roles of ubiquitination in signaling and endocytosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
315
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-5
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Proteasome-independent functions of ubiquitin in endocytosis and signaling.
pubmed:affiliation
Department of Biochemistry, University of Geneva, 30 Quai Ernest Ansermet, CH-1211 Geneva, Switzerland.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't