Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
about
ZAPS is a potent stimulator of signaling mediated by the RNA helicase RIG-I during antiviral responsesRapid evolution of PARP genes suggests a broad role for ADP-ribosylation in host-virus conflicts.Bookmarking promoters in mitotic chromatin: poly(ADP-ribose)polymerase-1 as an epigenetic markQuinolinate Phosphoribosyltransferase is an Antiviral Host Factor Against Hepatitis C Virus Infection.Helicobacter pylori activation of PARP-1: usurping a versatile regulator of host cellular healthSIRT1 deacetylates TopBP1 and modulates intra-S-phase checkpoint and DNA replication origin firingIdentification of a novel Gig2 gene family specific to non-amniote vertebrates.PARP-1 modulates amyloid beta peptide-induced neuronal damage.The Broad-Spectrum Antiviral Protein ZAP Restricts Human RetrotranspositionPost-Translational Modifications of Kaposi's Sarcoma-Associated Herpesvirus Regulatory Proteins - SUMO and KSHVVirus-Host Interactions and the ARTD/PARP Family of EnzymesPARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infectionEpstein-Barr Virus Oncoprotein LMP1 Mediates Epigenetic Changes in Host Gene Expression through PARP1.The Sound of Silence: RNAi in Poly (ADP-Ribose) ResearchRNAi reveals proteins for metabolism and protein processing associated with Langat virus infection in Ixodes scapularis (black-legged tick) ISE6 cells.Small molecule inhibition of Epstein-Barr virus nuclear antigen-1 DNA binding activity interferes with replication and persistence of the viral genome.Epigenetic regulation of EBV and KSHV latencyThe origin recognition complex in human diseases.At a crossroads: human DNA tumor viruses and the host DNA damage response.Base excision repair of oxidative DNA damage: from mechanism to disease.DNA ligand designed to antagonize EBNA1 represses Epstein-Barr virus-induced immortalization.Resolution of the cellular proteome of the nucleocapsid protein from a highly pathogenic isolate of porcine reproductive and respiratory syndrome virus identifies PARP-1 as a cellular target whose interaction is critical for virus biology.Synergistic inhibition of PARP-1 and NF-κB signaling downregulates immune response against recombinant AAV2 vectors during hepatic gene therapy.Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis.The coronavirus nucleocapsid protein is ADP-ribosylated.Structure-based mechanism of action of a viral poly(ADP-ribose) polymerase 1-interacting protein facilitating virus replication
P2860
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P2860
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@ast
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@en
type
label
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@ast
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@en
prefLabel
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@ast
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@en
P2093
P2860
P356
P1433
P1476
Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.
@en
P2093
Chi-Ju Chen
Constandache Atanasiu
Italo Tempera
Maria D'Erme
Paul M Lieberman
Zhong Deng
P2860
P304
P356
10.1128/JVI.02333-09
P577
2010-03-10T00:00:00Z