Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
about
The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperoneBiochemical activities of minute virus of mice nonstructural protein NS1 are modulated In vitro by the phosphorylation state of the polypeptideThe replication protein A binding site in simian virus 40 (SV40) T antigen and its role in the initial steps of SV40 DNA replication.Interaction of the transcription factor TFIID with simian virus 40 (SV40) large T antigen interferes with replication of SV40 DNA in vitro.Replicative functions of minute virus of mice NS1 protein are regulated in vitro by phosphorylation through protein kinase C.Pharmacological cyclin-dependent kinase inhibitors inhibit replication of wild-type and drug-resistant strains of herpes simplex virus and human immunodeficiency virus type 1 by targeting cellular, not viral, proteinsPeptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylatedStability and function of JC virus large T antigen and T' proteins are altered by mutation of their phosphorylated threonine 125 residues.Phosphorylation of Merkel cell polyomavirus large tumor antigen at serine 816 by ATM kinase induces apoptosis in host cells.Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replicationPurification of the simian virus 40 (SV40) T antigen DNA-binding domain and characterization of its interactions with the SV40 origin.Phosphorylation sites in polyomavirus large T antigen that regulate its function in viral, but not cellular, DNA synthesis.The N-terminal side of the origin-binding domain of simian virus 40 large T antigen is involved in A/T untwisting.Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.Phosphorylation site mutations affect herpes simplex virus type 1 ICP0 function.The retinoblastoma protein alters the phosphorylation state of polyomavirus large T antigen in murine cell extracts and inhibits polyomavirus origin DNA replication.Sequence requirements for the assembly of simian virus 40 T antigen and the T-antigen origin binding domain on the viral core origin of replication.Two regions of simian virus 40 T antigen determine cooperativity of double-hexamer assembly on the viral origin of DNA replication and promote hexamer interactions during bidirectional origin DNA unwinding.Polyomavirus large T antigen binds cooperatively to its multiple binding sites in the viral origin of DNA replication.Assembly of T-antigen double hexamers on the simian virus 40 core origin requires only a subset of the available binding sites.Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.Characterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropyCyclin-dependent kinase regulation of the replication functions of polyomavirus large T antigen.
P2860
Q24669835-8167B211-E98E-47E2-AE08-8EA4CD25A0B9Q28368835-CEE41C68-D4A9-401A-A700-2A39B2D90CEAQ31976778-0626C31B-0F0A-473F-8CFC-A9913E70896AQ33292492-0F22610C-06D9-492A-94B1-F02F00FA587EQ33786100-3B1762BF-D37C-46E0-B204-A2446F01D5B2Q34343774-B8A4DBF1-F39A-4DD3-9C54-EFB52683FF47Q34360447-6A88D549-D40D-4781-A4C4-1E4295294577Q34434734-4598E4D4-2736-4A84-BBAF-8F4414C64B9BQ35121370-FC3AEEF2-11DA-478D-92CC-50FE86A3BDBAQ35158114-1B6231BE-49A6-47BB-AE6A-35B2EDB7B340Q35883893-0EE439B7-29E1-469C-85FB-0F7E7592F9D0Q35891127-99BB02A5-E81E-4562-B4C3-15F374FAE1A8Q35898933-1177CC67-2373-478C-B343-775ED234A861Q35947912-1FFF5AE3-B653-47A1-8135-65761D6C2B30Q37743081-71D608BD-B2A9-4AF4-AFEE-C083805EAF53Q39549906-EFB5ECEF-4CA0-4737-9082-77E6CEFA227EQ39550997-0219C89C-145F-4E27-BD62-123EB5A44D31Q39551869-AF68F669-09BA-4308-B6A7-EA35F19F9AD5Q39580215-0A8F54B2-A74C-4BC3-98F8-C44ED9CA69B2Q39583872-7C20AF93-C50E-4B1F-8024-2EC3FB094897Q39612347-035EFA73-F4F9-4841-BA74-F96CD72A8FBDQ39748616-7CD33FAF-E20E-4B2F-9D87-86BBDBAAF09EQ39880787-7930C60A-CB71-4903-A71F-D6A72E7FB9EF
P2860
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@ast
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@en
type
label
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@ast
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@en
prefLabel
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@ast
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@en
P2093
P2860
P1433
P1476
Mechanisms of simian virus 40 T-antigen activation by phosphorylation of threonine 124
@en
P2093
P2860
P304
P407
P577
1996-06-01T00:00:00Z