Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-3-2
pubmed:abstractText
Antibodies were prepared against bacterially expressed polypeptides corresponding to various portions of the v-ets-encoded domain of P135gag-myb-ets, the transforming protein of avian leukemia virus E26. Immunoprecipitation analyses show that ca. 80 v-ets-encoded amino-acids located immediately after the v-myb/v-ets junction are not found in P54/56c-ets, the translation product of the c-ets proto-oncogene, nor in a set of cellular proteins of 64, 62, and 60 kDa related to but distinct from P54/56c-ets. In addition, Northern blot analyses show that these 5' v-ets sequences neither derive from the nontranslated region of the known cellular transcripts hybridizing to a v-ets probe nor from the c-myb transcript or the helper virus genetic information. Tryptic peptide analyses furthermore indicate that, except for these sequences and the last 16 carboxy terminal amino acids of P135gag-myb-ets, the amino acids encoded by v-ets are essentially colinear with those of P54c-ets.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
156
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-80
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The 5' extremity of the v-ets oncogene of avian leukemia virus E26 encodes amino acid sequences not derived from the major c-ets-encoded cellular proteins.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't