Linked Life Data

7649287

Source:http://linkedlifedata.com/resource/pubmed/id/7649287

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1995-9-25
pubmed:abstractText
Mitotic cyclins are key cell-cycle regulators that are relatively stable through most of the cell-cycle then rapidly degraded at mitosis. We have detected ubiquitin conjugates of full-length Xenopus cyclin B2 strongly suggesting that ubiquitination rather than a proteolytic cleavage is the initiating event in cyclin destruction. The highest levels of ubiquitin conjugates correlate with the phase of rapid proteolysis. This result supports previous findings that implicate the ubiquitin system in cyclin proteolysis. However, we also observe cyclin-ubiquitin conjugates in both cytostatic factor arrested and interphase extracts where cyclin is more stable. The physiologic role of ubiquitinated cyclin under these conditions is unclear.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
370
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Ubiquitination of full-length cyclin.
pubmed:affiliation
Department of Biochemistry, University of Utah, Salt Lake City 84132, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't