Biochemical analysis of mutants with changes in the origin-binding domain of simian virus 40 tumor antigen
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The Crystal Structure of the SV40 T-Antigen Origin Binding Domain in Complex with DNAIn vivo expression of a single viral DNA-binding protein generates systemic lupus erythematosus-related autoimmunity to double-stranded DNA and histones.The origin DNA-binding and single-stranded DNA-binding domains of simian virus 40 large T antigen are distinctRole of single-stranded DNA binding activity of T antigen in simian virus 40 DNA replicationOrigin remodeling and opening in bacteria rely on distinct assembly states of the DnaA initiatorCrystal structure of the simian virus 40 large T-antigen origin-binding domainDevelopment 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 replicationZinc-binding and protein-protein interactions mediated by the polyomavirus large T antigen zinc finger.A TEF-1-independent mechanism for activation of the simian virus 40 (SV40) late promoter by mutant SV40 large T antigensPurification of the simian virus 40 (SV40) T antigen DNA-binding domain and characterization of its interactions with the SV40 origin.trans-Dominant and non-trans-dominant mutant simian virus 40 large T antigens show distinct responses to ATP.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.The cap region of topoisomerase I binds to sites near both ends of simian virus 40 T antigen.Nonspecific double-stranded DNA binding activity of simian virus 40 large T antigen is involved in melting and unwinding of the origin.The simian virus 40 core origin contains two separate sequence modules that support T-antigen double-hexamer assembly.Assembly of T-antigen double hexamers on the simian virus 40 core origin requires only a subset of the available binding sites.An N-terminal deletion mutant of simian virus 40 (SV40) large T antigen oligomerizes incorrectly on SV40 DNA but retains the ability to bind to DNA polymerase alpha and replicate SV40 DNA in vitro.The DNA-binding domain of simian virus 40 tumor antigen has multiple functions.Modeling of the SV40 DNA Replication Machine.Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication.
P2860
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P2860
Biochemical analysis of mutants with changes in the origin-binding domain of simian virus 40 tumor antigen
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1993 nî lūn-bûn
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1993年の論文
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1993年論文
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1993年論文
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1993年論文
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1993年論文
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1993年论文
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name
Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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type
label
Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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P2093
P2860
P1433
P1476
Biochemical analysis of mutant ...... simian virus 40 tumor antigen
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P2093
P2860
P304
P407
P577
1993-07-01T00:00:00Z