Linked Life Data

21071203

Source:http://linkedlifedata.com/resource/pubmed/id/21071203

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-2-11
pubmed:abstractText
Conjugation of ubiquitin to cellular proteins has emerged as a post-translational modification, which affects major cellular processes, including cell cycle, proliferation and apoptosis. The ubiquitin-mediated signaling is frequently altered in cancer cells, with several tumor suppressors and oncogenes representing enzymes of the ubiquitin conjugation and deconjugation pathways. Recently, ubiquitination has been involved into selective degradation of both proteins and mitochondria by autophagy. Studying this novel role of ubiquitin can shed light on autophagy as a tumor suppressor mechanism as well as provide insights into the role of autophagy in survival of tumor cells, thus aiding the design of better cancer therapies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1879-0380
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-8
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Ubiquitin networks in cancer.
pubmed:affiliation
Merck KGaA, Frankfurter Str. 250, D-64293 Darmstadt, Germany. vladimir.kirkin@merck.de
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't