Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.
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Analysis of the Costructure of the Simian Virus 40 T-Antigen Origin Binding Domain with Site I Reveals a Correlation between GAGGC Spacing and Spiral AssemblyWerner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylationTwo heads are better than one: regulation of DNA replication by hexameric helicasesMutational analysis of simian virus 40 T-antigen primosome activities in viral DNA replication.In the simian virus 40 in vitro replication system, start site selection by the polymerase alpha-primase complex is not significantly altered by changes in the concentration of ribonucleotides.Phosphorylation of large T antigen regulates merkel cell polyomavirus replicationPeptides 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.Initiation of DNA replication: lessons from viral initiator proteins.Model for T-antigen-dependent melting of the simian virus 40 core origin based on studies of the interaction of the beta-hairpin with DNA.Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.Interactions required for binding of simian virus 40 T antigen to the viral origin and molecular modeling of initial assembly events.Cell cycle regulation of DNA replication.The simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding.Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant proteinCharacterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropyPartial proteolysis of simian virus 40 T antigen reveals intramolecular contacts between domains and conformation changes upon hexamer assembly.Bypass of a protein barrier by a replicative DNA helicase.
P2860
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P2860
Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.
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2000 nî lūn-bûn
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Phosphorylation of simian viru ...... ents of the viral core origin.
@en
Phosphorylation of simian viru ...... ents of the viral core origin.
@nl
type
label
Phosphorylation of simian viru ...... ents of the viral core origin.
@en
Phosphorylation of simian viru ...... ents of the viral core origin.
@nl
prefLabel
Phosphorylation of simian viru ...... ents of the viral core origin.
@en
Phosphorylation of simian viru ...... ents of the viral core origin.
@nl
P2093
P2860
P1433
P1476
Phosphorylation of simian viru ...... ents of the viral core origin.
@en
P2093
B A Barbaro
D R Winters
K R Sreekumar
P A Bullock
P2860
P304
P356
10.1128/JVI.74.18.8601-8613.2000
P407
P577
2000-09-01T00:00:00Z