Cellular proteins that associate with the middle and small T antigens of polyomavirus.
about
A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2AIdentification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirusAssociation of protein phosphatase 2A with polyoma virus medium tumor antigenMolecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa proteinAn Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinasesMolecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigensThe third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36- and 63-kilodalton PP2A subunits, bears little resemblance to T antigens.Identification of TAZ as a binding partner of the polyomavirus T antigens.Generation of a large library of point mutations in polyoma middle T antigen.Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src).Serine 257 phosphorylation regulates association of polyomavirus middle T antigen with 14-3-3 proteinsIdentification and characterization of the hamster polyomavirus middle T antigen.Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen.Enhancer-mediated role for polyomavirus middle T/small T in DNA replication.Identification of regions in polyomavirus middle T and small t antigens important for association with protein phosphatase 2A.Amino-terminal regions of polyomavirus middle T antigen are required for interactions with protein phosphatase 2A.Regulation of cell cycle progression and nuclear affinity of the retinoblastoma protein by protein phosphatases.Protein phosphatases and DNA tumor viruses: transformation through the back door?A tightly associated serine/threonine protein kinase regulates phosphoinositide 3-kinase activity.Mutation of a cysteine residue in polyomavirus middle T antigen abolishes interactions with protein phosphatase 2A, pp60c-src, and phosphatidylinositol-3 kinase, activation of c-fos expression, and cellular transformation.Transformation-defective mutants of polyomavirus middle T antigen associate with phosphatidylinositol 3-kinase (PI 3-kinase) but are unable to maintain wild-type levels of PI 3-kinase products in intact cellsEvidence that the middle T antigen of polyomavirus interacts with the membrane skeletonAn Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinaseCharacterization of pp85, a target of oncogenes and growth factor receptorsStoichiometry of cellular and viral components in the polyomavirus middle-T antigen-tyrosine kinase complex.A completely transformation-defective point mutant of polyomavirus middle T antigen which retains full associated phosphatidylinositol kinase activityAssociation of simian virus 40 small-t antigen with the 61-kilodalton component of a cellular protein complexPP2A Counterbalances Phosphorylation of pRB and Mitotic Proteins by Multiple CDKs: Potential Implications for PP2A Disruption in CancerRegulation of pp60c-src and its interaction with polyomavirus middle T antigen in insect cellsAssociation of p62c-yes with polyomavirus middle T-antigen mutants correlates with transforming ability.The cellular proteins which can associate specifically with polyomavirus middle T antigen in human 293 cells include the major human 70-kilodalton heat shock proteins.Induction of c-jun protooncogene expression and transcription factor AP-1 activity by the polyoma virus middle-sized tumor antigen.Merkel cell carcinoma: a virus-induced human cancerThe critical protein interactions and structures that elicit growth deregulation in cancer and viral replication.Novel monoclonal antibodies that differentiate between the binding of pp60c-src or protein phosphatase 2A by polyomavirus middle T antigen.Identification of the adenovirus E4orf4 protein binding site on the B55α and Cdc55 regulatory subunits of PP2A: Implications for PP2A function, tumor cell killing and viral replication.Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A.Negative regulation of CHK2 activity by protein phosphatase 2A is modulated by DNA damage.Characterization of the interaction of polyomavirus middle T antigen with type 2A protein phosphatase.Phosphatidylinositol metabolism in cells transformed by polyomavirus middle T antigen.
P2860
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P2860
Cellular proteins that associate with the middle and small T antigens of polyomavirus.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Cellular proteins that associate with the middle and small T antigens of polyomavirus.
@en
type
label
Cellular proteins that associate with the middle and small T antigens of polyomavirus.
@en
prefLabel
Cellular proteins that associate with the middle and small T antigens of polyomavirus.
@en
P2093
P2860
P1433
P1476
Cellular proteins that associate with the middle and small T antigens of polyomavirus.
@en
P2093
B Schaffhausen
D C Pallas
T M Roberts
V Cherington
P2860
P304
P407
P577
1988-11-01T00:00:00Z