Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme.
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Crystallization ofChlorelladeoxyuridine triphosphataseCrystallization 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 replicationSalmon Gill Poxvirus, the Deepest Representative of the Chordopoxvirinae.A novel target and approach for identifying antivirals against molluscum contagiosum virus.Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.Mutations conferring resistance to viral DNA polymerase inhibitors in camelpox virus give different drug-susceptibility profiles in vaccinia virus.Low-resolution structure of vaccinia virus DNA replication machineryUsing structural-based protein engineering to modulate the differential inhibition effects of SAUGI on human and HSV uracil DNA glycosylase.Regulation of DNA glycosylases and their role in limiting disease.Orthopoxvirus targets for the development of new antiviral agents.Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.Proteomic Screen for Cellular Targets of the Vaccinia Virus F10 Protein Kinase Reveals that Phosphorylation of mDia Regulates Stress Fiber Formation.Genetic Confirmation that the H5 Protein Is Required for Vaccinia Virus DNA Replication.Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.The vaccinia virus DNA polymerase and its processivity factor.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.Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA.The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.Isolation and Characterization of vΔI3 Confirms that the Vaccinia Virus SSB Plays an Essential Role in Viral Replication.The French Armed Forces Virology Unit: A Chronological Record of Ongoing Research on Orthopoxvirus.
P2860
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P2860
Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@ast
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@en
type
label
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@ast
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@en
prefLabel
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@ast
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@en
P2093
P2860
P356
P1476
Evaluation of the role of the ...... the DNA polymerase holoenzyme.
@en
P2093
Eleni S Stanitsa
Jill K Lindgren
Kathleen A Boyle
Matthew D Greseth
Paula Traktman
P2860
P304
24702-24713
P356
10.1074/JBC.M111.222216
P407
P577
2011-05-13T00:00:00Z