Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-12-10
pubmed:abstractText
Using the yeast two-hybrid assay and in vivo binding assay, we investigated whether B-myb oncogene products (B-myb) can associate with each other. Specificity tests of the yeast two-hybrid system showed a self-association of B-myb proteins in yeast. Cotransfection experiments demonstrated that B-myb proteins form a complex in vivo. Deletion analysis revealed that this binding was sufficiently mediated by the carboxy-terminal conserved region of B-myb. In addition, the B-myb self-association is directly dependent on the amount of expressed B-myb in cells and slightly increased by the dephosphorylation state. These results suggested that B-myb could form a complex and influence its transcriptional activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
460
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
363-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
B-myb proto-oncogene products interact in vivo with each other via the carboxy-terminal conserved region.
pubmed:affiliation
Department of Biochemistry and Division of Life Sciences, Chungbuk National University, Cheongju, South Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't