Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-12-30
pubmed:abstractText
Polyomavirus middle-T antigen induces the transformation of established cell lines in culture and is known to interact with and/or modulate the activity of several enzymes (pp60c.src, protein kinase C and phosphatidylinositol kinase) in vitro. This review is a compilation of the reported mutants of middle-T antigen and their biochemical and biological properties as they relate to the transformation event. The mutants of polyomavirus middle-T antigen have been previously classified phenotypically. Given the now large number of mutants, the classification presented here is based upon the position within the molecule. A model of middle-T is presented in which the protein is considered as consisting of three domains: a hydrophobic domain (the putative membrane-binding domain), the amino-terminal half of the molecule (the putative pp60c.src-binding domain) and the intervening amino acids (the putative modulatory domain). A current model for the induction of transformation by polyomavirus middle-T is presented.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
907
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-321
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Mutants of polyomavirus middle-T antigen.
pubmed:affiliation
Integrated Genetics, Framingham, MA 01701.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't