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.
about
Initiation 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 infectionFurther studies on the role of the residue 890 cysteine to tyrosine mutation in the M70 primase ORF of the temperature-sensitive mutant (tsm5) of murine cytomegalovirus.Helicase-primase inhibitors for herpes simplex virus: looking to the future of non-nucleoside inhibitors for treating herpes virus infections.The effects of viral load on pseudorabies virus gene expressionA cysteine-rich metal-binding domain from rubella virus non-structural protein is essential for viral protease activity and virus replication.Molecular dissection of the domain architecture and catalytic activities of human PrimPol.Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationA 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.Herpes simplex viruses: mechanisms of DNA replication.Replication and recombination of herpes simplex virus DNACoordinated leading and lagging strand DNA synthesis by using the herpes simplex virus 1 replication complex and minicircle DNA templatesPrimPol-Prime Time to Reprime.Production and characterisation of Epstein-Barr virus helicase-primase complex and its accessory protein BBLF2/3.UL52 primase interactions in the herpes simplex virus 1 helicase-primase are affected by antiviral compounds and mutations causing drug resistanceICP8 Filament Formation Is Essential for Replication Compartment Formation during Herpes Simplex Virus InfectionConserved structure/function of the orthoreovirus major core proteinsThe 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.The Zn-finger domain of human PrimPol is required to stabilize the initiating nucleotide during DNA priming.Helicase-Primase Inhibitors: A New Approach to Combat Herpes Simplex Virus and Varicella Zoster Virus
P2860
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P2860
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.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@ast
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@en
type
label
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@ast
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@en
prefLabel
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@ast
Mutations in the putative zinc ...... pe 1 helicase/primase complex.
@en
P2093
P2860
P1433
P1476
Mutations in the putative zinc ...... ype 1 helicase/primase complex
@en
P2093
Stacy D Carrington-Lawrence
P2860
P304
P356
10.1128/JVI.79.14.9088-9096.2005
P577
2005-07-01T00:00:00Z