The cellular DNA polymerase alpha-primase is required for papillomavirus DNA replication and associates with the viral E1 helicase
about
Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 subunit of DNA polymerase alphaBovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 proteinAssociation of the human papillomavirus type 11 E1 protein with histone H1Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteinsInteraction of herpes simplex virus 1 origin-binding protein with DNA polymerase alphaCrystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome.Nuclear accumulation of the papillomavirus E1 helicase blocks S-phase progression and triggers an ATM-dependent DNA damage responseInteractions of the papovavirus DNA replication initiator proteins, bovine papillomavirus type 1 E1 and simian virus 40 large T antigen, with human replication protein ARecruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNACompetition for DNA binding sites between the short and long forms of E2 dimers underlies repression in bovine papillomavirus type 1 DNA replication control.The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activitiesA C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit.Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin.An embryonic demethylation mechanism involving binding of transcription factors to replicating DNAEpisomal vectors for gene expression in mammalian cells.The human DnaJ protein, hTid-1, enhances binding of a multimer of the herpes simplex virus type 1 UL9 protein to oris, an origin of viral DNA replication.E1-mediated recruitment of a UAF1-USP deubiquitinase complex facilitates human papillomavirus DNA replicationRecent advances in diagnosis and therapy of human papillomaviruses.A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensableNuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance.Human TATA binding protein inhibits human papillomavirus type 11 DNA replication by antagonizing E1-E2 protein complex formation on the viral origin of replication.A systems biology analysis of the changes in gene expression via silencing of HPV-18 E1 expression in HeLa cells.Recruitment of Brd4 to the human papillomavirus type 16 DNA replication complex is essential for replication of viral DNA.Protein-protein interactions as targets for antiviral chemotherapy.Control of HPV 18 DNA replication by cellular and viral transcription factors.Interaction between cyclin-dependent kinases and human papillomavirus replication-initiation protein E1 is required for efficient viral replicationSmall molecule inhibitors of human papillomavirus protein - protein interactions.Initiation of DNA replication: lessons from viral initiator proteins.The Cell Cycle Timing of Human Papillomavirus DNA Replication.Inhibition of human papillomavirus DNA replication by an E1-derived p80/UAF1-binding peptide.Mutational analysis of the 18-base-pair inverted repeat element at the bovine papillomavirus origin of replication: identification of critical sequences for E1 binding and in vivo replicationCellular factors required for papillomavirus DNA replication.Genetic analysis of the activation domain of bovine papillomavirus protein E2: its role in transcription and replication.Isolation of an amino-terminal region of bovine papillomavirus type 1 E1 protein that retains origin binding and E2 interaction capacity.Evidence for a switch in the mode of human papillomavirus type 16 DNA replication during the viral life cycleCancer, Warts, or Asymptomatic Infections: Clinical Presentation Matches Codon Usage Preferences in Human PapillomavirusesRecent advances in the search for antiviral agents against human papillomaviruses.Targeting human papillomavirus genome replication for antiviral drug discoveryAn interaction between human papillomavirus 16 E2 and TopBP1 is required for optimum viral DNA replication and episomal genome establishment
P2860
Q22010642-4BACE001-5F8F-4FE0-A94D-6F1A63A62CD9Q22254410-5F94BF03-E117-46CE-A533-33A84473C467Q24316941-593AC34F-D7DA-477D-9B05-D70A3FC6372CQ24317609-5881C40A-2FE3-4604-BCA3-817EE111919AQ24324000-411C1366-8457-47B0-8224-C4485285E46FQ27638318-0542FCC8-D596-463C-B4E9-C417F1C2597DQ27935272-7052A568-345F-4ABC-BDDF-BB582BB7DE88Q28740849-3D75B5AB-2031-4E63-9606-0B162D012A24Q30629592-7FC40092-D551-48A3-AC8C-FE74A2B26998Q31038703-B8D39CF5-63C9-45CB-AECC-FB8135C4D88AQ33782324-C8F5AD44-2641-482B-BA5D-5BCEC36D5A11Q33783679-6295CC8F-6C50-46AE-81A4-0C0C51B8219EQ33783875-98669674-DEAE-4881-8661-1B79E7F1E272Q33809498-FA5D2651-07EB-48B2-9F1E-F205D06A1F0DQ33888429-19122F38-F085-4B8F-BA43-0F1DE3116006Q33916410-175959B3-739F-4E8E-8D55-C93A4E32E74AQ34011483-581A4330-1A40-4CB2-A1AA-8AB5A994F265Q34057851-4B782F50-9632-41F8-A6E8-001B0CBD37EBQ34074998-000B802E-DA2E-41B5-92C7-7F47246626DDQ34236588-D57428F0-15E7-44F2-AE7C-C885EA0FDD5CQ34295899-1254E4CC-9B44-4C57-9DD3-8AD9F3BA7A11Q34338679-EEE7429C-E114-4757-8751-EE35FF2476E3Q34461031-CD94A400-9205-4663-B2E5-96473F51AAEEQ34568110-03193538-EFA9-4529-BDC6-D73716D9707EQ34747522-3AB3541C-9E4F-4054-BB5B-B805C579F07BQ34782217-C35ECED6-36F9-4D8E-9FAD-60CA69658542Q34809313-1F7B6715-5C03-4DC0-A806-ECCD82458072Q35107717-32DDCE89-1C90-4C74-9709-6FE9C40B5230Q35541015-C4EBA39F-1F10-483D-8470-BD41B73B9E53Q35680285-3082892F-DDC6-4EBE-931E-8CCB16043144Q35826814-CD6D9D91-86AC-4D3A-BACF-00C46B6CB368Q35849102-693B4B6D-47A3-49C7-8B47-4484A3252F1DQ35852375-0CE21687-5547-400E-8588-44FFE5066473Q35863067-8E368522-CDF5-4E6A-836F-D69D82D4C092Q35876159-2DF75ABE-C4DB-4A17-A0ED-DD6576DBD9FCQ35894649-6A80507E-9043-4B99-BE7A-7321635F5CF9Q36023244-E3D53334-4A98-4E4A-9B1B-4D9C7BB27E2EQ36284493-58CD6926-F880-4762-9580-979369BEAD62Q36315302-AAFB5DC1-CF3E-4869-9345-AC1682F63E8CQ36397627-F86AD53C-7D59-44CF-BADB-F5844081753A
P2860
The cellular DNA polymerase alpha-primase is required for papillomavirus DNA replication and associates with the viral E1 helicase
description
1994 nî lūn-bûn
@nan
1994 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@ast
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@en
type
label
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@ast
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@en
prefLabel
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@ast
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@en
P2093
P2860
P356
P1476
The cellular DNA polymerase al ...... tes with the viral E1 helicase
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.18.8700
P407
P577
1994-08-01T00:00:00Z