Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.
about
Mechanism and evolution of DNA primasesDetermination and analysis of the complete nucleotide sequence of human herpesvirusOrigin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new membersThe 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 complexMolecular cloning of a Plasmodium falciparum gene interrupted by 15 introns encoding a functional primase 53 kDa subunit as demonstrated by expression in a baculovirus systemHerpes simplex virus type 1 UL51 protein is involved in maturation and egress of virus particles.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.Processing of lagging-strand intermediates in vitro by herpes simplex virus type 1 DNA polymeraseAn intertypic herpes simplex virus helicase-primase complex associated with a defect in neurovirulence has reduced primase activity.UL54-null pseudorabies virus is attenuated in mice but productively infects cells in cultureEvidence 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.Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationRecruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Oral bioavailability and in vivo efficacy of the helicase-primase inhibitor BILS 45 BS against acyclovir-resistant herpes simplex virus type 1.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.Coordinated leading and lagging strand DNA synthesis by using the herpes simplex virus 1 replication complex and minicircle DNA templatesBaculovirus replication factor LEF-1 is a DNA primase.Pseudorabies virus and equine herpesvirus 1 share a nonessential gene which is absent in other herpesviruses and located adjacent to a highly conserved gene cluster.Formation of herpes simplex virus type 1 replication compartments by transfection: requirements and localization to nuclear domain 10.Characterization of the interaction between the baculovirus replication factors LEF-1 and LEF-2.Herpes simplex virus-1 DNA primase: a remarkably inaccurate yet selective polymerase.The UL8 subunit of the helicase/primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.Epstein-barr virus encodes three bona fide ubiquitin-specific proteases.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.
P2860
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P2860
Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.
description
1994 nî lūn-bûn
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1994年の論文
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1994年論文
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1994年論文
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1994年論文
@zh-hk
1994年論文
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1994年論文
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1994年论文
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1994年论文
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1994年论文
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name
Helicase-primase complex of he ...... it abolishes primase activity.
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Helicase-primase complex of he ...... it abolishes primase activity.
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type
label
Helicase-primase complex of he ...... it abolishes primase activity.
@ast
Helicase-primase complex of he ...... it abolishes primase activity.
@en
prefLabel
Helicase-primase complex of he ...... it abolishes primase activity.
@ast
Helicase-primase complex of he ...... it abolishes primase activity.
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P2860
P1433
P1476
Helicase-primase complex of he ...... nit abolishes primase activity
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P2093
Challberg MD
Klinedinst DK
P2860
P304
P407
P577
1994-06-01T00:00:00Z