Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.
about
The HSV-1 exonuclease, UL12, stimulates recombination by a single strand annealing mechanismStructural modelling and mutagenesis of human cytomegalovirus alkaline nuclease UL98Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.Productive replication of human papillomavirus 31 requires DNA repair factor Nbs1.Efficient herpes simplex virus 1 replication requires cellular ATR pathway proteinsRecombination promoted by DNA viruses: phage λ to herpes simplex virus.DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replicationSelective recruitment of nuclear factors to productively replicating herpes simplex virus genomes.Herpes simplex viruses: mechanisms of DNA replication.Activation of H2AX and ATM in varicella-zoster virus (VZV)-infected cells is associated with expression of specific VZV genesReplication and recombination of herpes simplex virus DNABridging the past and the future of virology: surface plasmon resonance as a powerful tool to investigate virus/host interactions.Elimination of mitochondrial DNA is not required for herpes simplex virus 1 replication.HSV-I and the cellular DNA damage response.Localization of Double-Strand Break Repair Proteins to Viral Replication Compartments following Lytic Reactivation of Kaposi's Sarcoma-Associated Herpesvirus.An Intrinsically Disordered Region of the DNA Repair Protein Nbs1 Is a Species-Specific Barrier to Herpes Simplex Virus 1 in Primates.Design, fabrication and in vitro evaluation of a novel polymer-hydrogel hybrid scaffold for bone tissue engineering.Core histones H2B and H4 are mobilized during infection with herpes simplex virus 1.Stimulation of homology-directed repair at I-SceI-induced DNA breaks during the permissive life cycle of human cytomegalovirus.Spatiotemporally different DNA repair systems participate in Epstein-Barr virus genome maturation.Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins.The Telomeric Response to Viral Infection.The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.The exonuclease activity of HSV-1 UL12 is required for the production of viral DNA that can be packaged to produce infectious virus.Co-opting the Fanconi anemia genomic stability pathway enables herpesvirus DNA synthesis and productive growthMitochondrial nucleases ENDOG and EXOG participate in mitochondrial DNA depletion initiated by herpes simplex virus 1 UL12.5.The Non-Homologous End Joining Protein PAXX Acts to Restrict HSV-1 Infection.
P2860
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P2860
Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.
description
2010 nî lūn-bûn
@nan
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
2010年论文
@zh
2010年论文
@zh-cn
name
Physical interaction between t ...... and break-sensing MRN complex.
@en
type
label
Physical interaction between t ...... and break-sensing MRN complex.
@en
prefLabel
Physical interaction between t ...... and break-sensing MRN complex.
@en
P2093
P2860
P356
P1433
P1476
Physical interaction between t ...... and break-sensing MRN complex.
@en
P2093
George Korza
Gregory Buchek
Nandakumar Balasubramanian
P2860
P304
12504-12514
P356
10.1128/JVI.01506-10
P407
P577
2010-10-13T00:00:00Z