The DNA-binding properties of polyomavirus large T antigen are altered by ATP and other nucleotides.
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Asymmetric Assembly of Merkel Cell Polyomavirus Large T-Antigen Origin Binding Domains at the Viral OriginStudy of SV40 large T antigen nucleotide specificity for DNA unwindingNegative regulation of the adeno-associated virus (AAV) P5 promoter involves both the P5 rep binding site and the consensus ATP-binding motif of the AAV Rep68 proteinPeptides containing cyclin/Cdk-nuclear localization signal motifs derived from viral initiator proteins bind to DNA when unphosphorylatedE1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding.Different phenotypes in vivo are associated with ATPase motif mutations in Schizosaccharomyces pombe minichromosome maintenance proteinsMinute virus of mice transcriptional activator protein NS1 binds directly to the transactivation region of the viral P38 promoter in a strictly ATP-dependent manner.Specific transcription factors stimulate simian virus 40 and polyomavirus origins of DNA replication.Determination of the origin-specific DNA-binding domain of polyomavirus large T antigen.The simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.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.Polyomavirus large T antigen binds cooperatively to its multiple binding sites in the viral origin of DNA replication.Phosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.Sequences flanking the pentanucleotide T-antigen binding sites in the polyomavirus core origin help determine selectivity of DNA replication.Murine polyomavirus and simian virus 40 large T antigens produce different structural alterations in viral origin DNA.Cyclin-dependent kinase regulation of the replication functions of polyomavirus large T antigen.The mouse DNA polymerase alpha-primase subunit p48 mediates species-specific replication of polyomavirus DNA in vitro.p53 inhibits DNA replication in vitro in a DNA-binding-dependent manner.The replication functions of polyomavirus large tumor antigen are regulated by phosphorylation.c-Jun stimulates origin-dependent DNA unwinding by polyomavirus large Tantigen.A unique subpopulation of murine DNA polymerase alpha/primase specifically interacts with polyomavirus T antigen and stimulates DNA replication.
P2860
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P2860
The DNA-binding properties of polyomavirus large T antigen are altered by ATP and other nucleotides.
description
1991 nî lūn-bûn
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1991年の論文
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1991年論文
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1991年論文
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1991年論文
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1991年論文
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1991年論文
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1991年论文
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1991年论文
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1991年论文
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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The DNA-binding properties of ...... by ATP and other nucleotides.
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1991-02-01T00:00:00Z