Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells.
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Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assemblyThe infectious dose of variola (smallpox) virusOrigin-independent plasmid replication occurs in vaccinia virus cytoplasmic factories and requires all five known poxvirus replication factorsHuman cytomegalovirus uracil DNA glycosylase associates with ppUL44 and accelerates the accumulation of viral DNA.Vaccinia Virus D4 Mutants Defective in Processive DNA Synthesis Retain Binding to A20 and DNACrystallization and preliminary X-ray diffraction analysis of three recombinant mutants ofVaccinia virusuracil DNA glycosylaseCrystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminal domainPoxvirus DNA replicationIdentification of polymerase and processivity inhibitors of vaccinia DNA synthesis using a stepwise screening approachExpanding the repertoire of Modified Vaccinia Ankara-based vaccine vectors via genetic complementation strategiesRecruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1.Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseOpinion: uracil DNA glycosylase (UNG) plays distinct and non-canonical roles in somatic hypermutation and class switch recombination.Evidence for an essential catalytic role of the F10 protein kinase in vaccinia virus morphogenesis.A novel target and approach for identifying antivirals against molluscum contagiosum virus.Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme.Identification of inhibitors that block vaccinia virus infection by targeting the DNA synthesis processivity factor D4.Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication.Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.Selection of recombinant MVA by rescue of the essential D4R gene.Orthopoxvirus targets for the development of antiviral therapies.Poxvirus DNA primaseEffects of vaccinia virus uracil DNA glycosylase catalytic site and deoxyuridine triphosphatase deletion mutations individually and together on replication in active and quiescent cells and pathogenesis in mice.Orthopoxvirus targets for the development of new antiviral agents.Differential regulation of S-region hypermutation and class-switch recombination by noncanonical functions of uracil DNA glycosylaseUracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.Identification of protein-protein interaction inhibitors targeting vaccinia virus processivity factor for development of antiviral agents.A role for vaccinia virus protein C16 in reprogramming cellular energy metabolism.Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.The vaccinia virus DNA polymerase and its processivity factor.Characterisation of the substrate specificity of homogeneous vaccinia virus uracil-DNA glycosylase.Identification of Vaccinia Virus Replisome and Transcriptome Proteins by Isolation of Proteins on Nascent DNA Coupled with Mass Spectrometry.Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase.Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA.Targeting Nucleotide Biosynthesis: A Strategy for Improving the Oncolytic Potential of DNA Viruses.Uracil-directed ligand tethering: an efficient strategy for uracil DNA glycosylase (UNG) inhibitor developmentRequirement of non-canonical activity of uracil DNA glycosylase for class switch recombination.
P2860
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P2860
Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@ast
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@en
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@nl
type
label
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@ast
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@en
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@nl
prefLabel
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@ast
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@en
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@nl
P2860
P1433
P1476
Vaccinia virus uracil DNA glyc ...... replication in cultured cells.
@en
P2093
Frank S De Silva
P2860
P304
P356
10.1128/JVI.77.1.159-166.2003
P407
P50
P577
2003-01-01T00:00:00Z