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.
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A wolf in sheep's clothing: SV40 co-opts host genome maintenance proteins to replicate viral DNAThe Crystal Structure of the SV40 T-Antigen Origin Binding Domain in Complex with DNAStructure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domainAnalysis of the Costructure of the Simian Virus 40 T-Antigen Origin Binding Domain with Site I Reveals a Correlation between GAGGC Spacing and Spiral AssemblyPolyomavirus Large T Antigen Binds Symmetrical Repeats at the Viral Origin in an Asymmetrical MannerInsights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domainTwo heads are better than one: regulation of DNA replication by hexameric helicasesThermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.Mutational analysis of simian virus 40 T-antigen primosome activities in viral DNA replication.ATM and ATR activities maintain replication fork integrity during SV40 chromatin replication.The replication protein A binding site in simian virus 40 (SV40) T antigen and its role in the initial steps of SV40 DNA replication.Structural mechanism of RPA loading on DNA during activation of a simple pre-replication complex.Interaction of the transcription factor TFIID with simian virus 40 (SV40) large T antigen interferes with replication of SV40 DNA in vitro.Topoisomerase I associates specifically with simian virus 40 large-T-antigen double hexamer-origin complexesIn 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.Role of single-stranded DNA binding activity of T antigen in simian virus 40 DNA replicationPhosphorylation 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.Crystal structure of the simian virus 40 large T-antigen origin-binding domainSV40 DNA replication: from the A gene to a nanomachine.Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replicationAnalyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replicationStructure of the origin-binding domain of simian virus 40 large T antigen bound to DNA.Inhibition of human papillomavirus DNA replication by an E1-derived p80/UAF1-binding peptide.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.Nonspecific double-stranded DNA binding activity of simian virus 40 large T antigen is involved in melting and unwinding of the origin.Origin DNA melting and unwinding in DNA replication.Replication-fork dynamics.Role of the hydrophilic channels of simian virus 40 T-antigen helicase in DNA replicationThe simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.Large T-antigen double hexamers imaged at the simian virus 40 origin of 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.Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.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 protein
P2860
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P2860
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.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@en
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@nl
type
label
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@en
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@nl
prefLabel
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@en
Two regions of simian virus 40 ...... ectional origin DNA unwinding.
@nl
P2093
P2860
P1433
P1476
Two regions of simian virus 40 ...... rectional origin DNA unwinding
@en
P2093
P2860
P304
P407
P577
1999-03-01T00:00:00Z