The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.
about
The Epstein-Barr virus replication protein BBLF2/3 provides an origin-tethering function through interaction with the zinc finger DNA binding protein ZBRK1 and the KAP-1 corepressorMechanism and evolution of DNA primasesInitiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alphaThe DNA helicase-primase complex as a target for herpes viral infectionInhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the UL5-UL8-UL52 complexInhibition of human cytomegalovirus DNA maturation by a benzimidazole ribonucleoside is mediated through the UL89 gene productThe Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins.Autographa californica multiple nucleopolyhedrovirus LEF-2 is a capsid protein required for amplification but not initiation of viral DNA replication.Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex.An intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity.Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes.Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.Proteomic characterization of pseudorabies virus extracellular virionsLeading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome.Human cytomegalovirus UL102 geneThe catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.Poxvirus DNA primaseHelicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.Interaction of herpes primase with the sugar of a NTP.Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays.Coordinated leading and lagging strand DNA synthesis by using the herpes simplex virus 1 replication complex and minicircle DNA templatesAnalysis of the complete DNA sequence of murine cytomegalovirus.Herpes simplex virus-1 DNA primase: a remarkably inaccurate yet selective polymerase.Eleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA replication.The UL8 subunit of the helicase/primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.Identification of conserved amino acids in the herpes simplex virus type 1 UL8 protein required for DNA synthesis and UL52 primase interaction in the virus replisome.Temporal profiling of the coding and noncoding murine cytomegalovirus transcriptomes.
P2860
Q24558692-3132110E-0065-49D3-A5DA-D0E90EF24B28Q24612068-C13CE90E-C64B-47A4-8125-56C664920739Q24652672-2F51FE74-CF41-4FBC-9343-1298D76FCB92Q26849412-A19D13D4-85C4-4915-9042-2536249AE7E1Q28368363-17B2DDAE-8EA2-48EA-96AD-71F725C4C6DBQ28379289-0753233F-45F6-4296-A7ED-74B3FB39C67DQ33785198-D61D7922-0833-4A58-A09B-E644DC68780FQ33826825-2E3CC87E-5FE6-4A4B-8532-75F16B1EA544Q33883880-3602D0E0-C712-48B4-9A53-21971853F03AQ34069495-CD40C9CE-9FBA-4643-92AB-48B596DFFC42Q34348919-795968E1-96FB-4497-9188-53648234C288Q34482269-1C413061-8E04-4D87-B01A-A21D7CF62940Q34781727-9C691CBF-1A38-47E1-A5A8-EAB30B07E374Q35008795-C2A55DC6-1ABB-4D43-B6A1-8317CF96224DQ35077562-AF00FE24-0C59-4C55-945A-D4D434A0AF42Q35665398-A0BEE5D6-233F-416B-9F9E-2BEDDC787C4CQ35834751-28E6505A-B2F8-49CA-A814-F36CE05586E3Q35891002-5EBED3B8-1961-4B63-A549-5B79F583AD66Q35947833-F389735B-B1F0-4507-87CE-064A00BF6D3DQ36276981-0A3C9F2B-304A-40E9-8B2D-A74C648CB09CQ36634160-AD57A118-9D92-43EC-A1DE-EA533BBC78F2Q36653318-AE44802B-9138-4553-AB0E-9343B1679E60Q36981224-416C2EB6-2D5D-4A54-BE90-BAD98DE4C1FEQ38296033-BE4E83FB-5DFF-4A50-8A2F-5AC5BB07103DQ38339479-106159C9-6870-442B-9ABA-C55B6E88BA2FQ39877356-1200FEC1-32B7-4375-8B08-9D8E2B0C7AB8Q39904188-F37324D4-8AC3-437A-B1C7-AEED56EEC743Q40048289-BB84DF58-3D2A-4415-B524-86C7921AC502Q40108625-20161BF9-0392-43EB-8C3E-5466ED7EE2F7Q42565934-1001586A-3A76-4EEA-8AF2-D06C97A636BEQ42779866-591C8FDA-27D9-4D99-BA62-C802D11C980F
P2860
The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The UL8 subunit of the herpes ...... efficient primer utilization.
@ast
The UL8 subunit of the herpes ...... efficient primer utilization.
@en
type
label
The UL8 subunit of the herpes ...... efficient primer utilization.
@ast
The UL8 subunit of the herpes ...... efficient primer utilization.
@en
prefLabel
The UL8 subunit of the herpes ...... efficient primer utilization.
@ast
The UL8 subunit of the herpes ...... efficient primer utilization.
@en
P2093
P2860
P1433
P1476
The UL8 subunit of the herpes ...... r efficient primer utilization
@en
P2093
Challberg MD
Gottlieb J
P2860
P304
P407
P577
1992-08-01T00:00:00Z