A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
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The genome of Melanoplus sanguinipes entomopoxvirusMembers of a novel family of mammalian protein kinases complement the DNA-negative phenotype of a vaccinia virus ts mutant defective in the B1 kinaseLatency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus recruits uracil DNA glycosylase 2 at the terminal repeats and is important for latent persistence of the 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 DNACrystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminal domainPoxvirus DNA replicationMutations in active-site residues of the uracil-DNA glycosylase encoded by vaccinia virus are incompatible with virus viabilityMolecular characterization of Plasmodium falciparum uracil-DNA glycosylase and its potential as a new anti-malarial drug targetExpanding the repertoire of Modified Vaccinia Ankara-based vaccine vectors via genetic complementation strategiesVaccinia virus G8R protein: a structural ortholog of proliferating cell nuclear antigen (PCNA)Role of vaccinia virus A20R protein in DNA replication: construction and characterization of temperature-sensitive mutants.Repression of vaccinia virus Holliday junction resolvase inhibits processing of viral DNA into unit-length genomes.The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymeraseVaccinia 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.Identification of genes encoding zinc finger proteins, non-histone chromosomal HMG protein homologue, and a putative GTP phosphohydrolase in the genome of Chilo iridescent virusEvaluation 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.Vaccinia virus gene A18R encodes an essential DNA helicaseHuman cytomegalovirus uracil DNA glycosylase is required for the normal temporal regulation of both DNA synthesis and viral replicationOrthopoxvirus targets for the development of antiviral therapies.Low-resolution structure of vaccinia virus DNA replication machineryEffects 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.Identification of non-nucleoside DNA synthesis inhibitors of vaccinia virus by high-throughput screening.Orthopoxvirus targets for the development of new antiviral agents.Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays.Characterization of the single-stranded DNA binding protein encoded by the vaccinia virus I3 gene.The vaccinia virus DNA polymerase and its processivity factor.Requirement for uracil-DNA glycosylase during the transition to late-phase cytomegalovirus DNA replication.Clustered charge-to-alanine mutagenesis of the vaccinia virus A20 gene: temperature-sensitive mutants have a DNA-minus phenotype and are defective in the production of processive DNA polymerase activity.Characterisation of the substrate specificity of homogeneous vaccinia virus uracil-DNA glycosylase.Construction of a vaccinia virus deficient in the essential DNA repair enzyme uracil DNA glycosylase by a complementing cell line.Identification and characterization of a novel structural glycoprotein in pseudorabies virus, gL.Identification of Vaccinia Virus Replisome and Transcriptome Proteins by Isolation of Proteins on Nascent DNA Coupled with Mass Spectrometry.A Conserved Tripeptide Sequence at the C Terminus of the Poxvirus DNA Processivity Factor D4 Is Essential for Protein Integrity and Function.Uracil-directed ligand tethering: an efficient strategy for uracil DNA glycosylase (UNG) inhibitor developmentCombined Proteomics/Genomics Approach Reveals Proteomic Changes of Mature Virions as a Novel Poxvirus Adaptation Mechanism.The French Armed Forces Virology Unit: A Chronological Record of Ongoing Research on Orthopoxvirus.A structurally conserved motif in γ-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping.
P2860
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P2860
A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
@en
type
label
A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
@en
prefLabel
A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
@en
P2093
P2860
P1433
P1476
A poxvirus-encoded uracil DNA glycosylase is essential for virus viability.
@en
P2093
P2860
P304
P407
P577
1993-05-01T00:00:00Z