Linked Life Data

2543940

Source:http://linkedlifedata.com/resource/pubmed/id/2543940

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-7-21
pubmed:abstractText
The rel oncogene from the avian reticuloendotheliosis virus strain T is a 59 kd phosphoprotein localized primarily to the cytoplasm of transformed cells. Recently, the v-rel protein was shown to associate with several cellular proteins with molecular weights of 124 kd, 115 kd, and 36 kd. We have analysed the subcellular distribution of v-rel protein complexes after biochemical fractionation of [35S]methionine and [32P]orthophosphate labeled cells. Our results demonstrate that the v-rel protein coprecipitates with a characteristic set of proteins, some of which are distinct to nuclear or cytoplasmic fractions. We also demonstrate that the normal cellular homolog of the viral rel protein, c-rel, coprecipitates with several cellular proteins from normal chick hematopoietic tissue. These cellular proteins have apparent molecular weights similar to those which are coprecipitated with v-rel from cytoplasmic fractions. Our results demonstrate that both v-rel and c-rel interact with a variety of cellular proteins and suggest that this association is important for the function or regulation of the rel protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
677-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Viral rel and cellular rel associate with cellular proteins in transformed and normal cells.
pubmed:affiliation
Department of Microbiology, State University of New York, Stony Brook 11794.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.