The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.
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Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alphaDetermination and analysis of the complete nucleotide sequence of human herpesvirusAssessing the contribution of the herpes simplex virus DNA polymerase to spontaneous mutationsThe Crystal Structure of PF-8, the DNA Polymerase Accessory Subunit from Kaposi's Sarcoma-Associated HerpesvirusMode of antiviral action of penciclovir in MRC-5 cells infected with herpes simplex virus type 1 (HSV-1), HSV-2, and varicella-zoster virusInhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the UL5-UL8-UL52 complexMultiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infectionHerpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.Identification of a region of the herpes simplex virus single-stranded DNA-binding protein involved in cooperative bindingThe A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymeraseThe positively charged surface of herpes simplex virus UL42 mediates DNA binding.Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisHSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseResistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and managementOne severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Kinetic approaches to understanding the mechanisms of fidelity of the herpes simplex virus type 1 DNA polymeraseRNA polymerase II-dependent transcription in trypanosomes is associated with a SNAP complex-like transcription factor.Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interfaceCloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: relationship to the structure of alpha-like DNA polymerasesProteomic characterization of pseudorabies virus extracellular virionsIdentification of inhibitors that block vaccinia virus infection by targeting the DNA synthesis processivity factor D4.Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory functionCloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction.Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42Herpes simplex ICP27 mutant viruses exhibit reduced expression of specific DNA replication genesEvidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3'-5' exonuclease.Functional and physical interactions between the Epstein-Barr virus (EBV) proteins BZLF1 and BMRF1: Effects on EBV transcription and lytic replicationThe 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.Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity.Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism.Cathepsin B mediates cleavage of herpes simplex virus type 1 origin binding protein (OBP) to yield OBPC-1, and cleavage is dependent upon viral DNA replication.Conformational changes induced in herpes simplex virus DNA polymerase upon DNA binding.Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin.The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: implications for a dual role as a primer recognition factor and processivity clamp.Role of cellular phosphatase cdc25C in herpes simplex virus 1 replication.The Pseudorabies Virus DNA Polymerase Accessory Subunit UL42 Directs Nuclear Transport of the Holoenzyme.A novel cis element essential for stimulated transcription of the p41 promoter of human herpesvirus 6.
P2860
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P2860
The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
The herpes simplex virus type ...... ions to increase processivity.
@en
type
label
The herpes simplex virus type ...... ions to increase processivity.
@en
prefLabel
The herpes simplex virus type ...... ions to increase processivity.
@en
P2093
P2860
P1433
P1476
The herpes simplex virus type ...... ions to increase processivity.
@en
P2093
J Gottlieb
M D Challberg
P2860
P304
P407
P577
1990-12-01T00:00:00Z