Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.
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The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitroThe herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNAModulation of the herpes simplex virus type-1 UL9 DNA helicase by its cognate single-strand DNA-binding protein, ICP8.Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8.Replication of herpes simplex virus DNA.Identification of a region of the herpes simplex virus single-stranded DNA-binding protein involved in cooperative bindingThe Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins.Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.Characterization of varicella-zoster virus gene 21 and 29 proteins in infected cellsHelicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9.Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay.Catalysis of strand exchange by the HSV-1 UL12 and ICP8 proteins: potent ICP8 recombinase activity is revealed upon resection of dsDNA substrate by nuclease.HSV-1 protein expression using recombinant baculovirusesLeading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome.Existence of transdominant and potentiating mutants of UL9, the herpes simplex virus type 1 origin-binding protein, suggests that levels of UL9 protein may be regulated during infection.The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structuresThe lytic cycle of Epstein-Barr virus in the nonproducer Raji line can be rescued by the expression of a 135-kilodalton protein encoded by the BALF2 open reading frameFunctional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures.Herpes simplex ICP27 mutant viruses exhibit reduced expression of specific DNA replication genesProperties of the novel herpes simplex virus type 1 origin binding protein, OBPCUse of transdominant mutants of the origin-binding protein (UL9) of herpes simplex virus type 1 to define functional domains.Assembly of complete, functionally active herpes simplex virus DNA replication compartments and recruitment of associated viral and cellular proteins in transient cotransfection assays.The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of oriLyt.Reconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1Unwinding of the box I element of a herpes simplex virus type 1 origin by a complex of the viral origin binding protein, single-strand DNA binding protein, and single-stranded DNA.On the mechanism of strand assimilation by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8)Complementary intrastrand base pairing during initiation of Herpes simplex virus type 1 DNA replicationDirect interaction between the N- and C-terminal portions of the herpes simplex virus type 1 origin binding protein UL9 implies the formation of a head-to-tail dimer.3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity.Transcriptional analysis of the region of the herpes simplex virus type 1 genome containing the UL8, UL9, and UL10 genes and identification of a novel delayed-early gene product, OBPC.Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activityStructural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.RNA binding and R-loop formation by the herpes simplex virus type-1 single-stranded DNA-binding protein (ICP8).The DNA ligands influence the interactions between the herpes simplex virus 1 origin binding protein and the single strand DNA-binding protein, ICP-8.Equilibrium binding of single-stranded DNA with herpes simplex virus type I-coded single-stranded DNA-binding protein, ICP8.A novel conformation of the herpes simplex virus origin of DNA replication recognized by the origin binding protein.The herpes simplex virus type 1 origin binding protein. Specific recognition of phosphates and methyl groups defines the interacting surface for a monomeric DNA binding domain in the major groove of DNA.Role of protein-protein interactions during herpes simplex virus type 1 recombination-dependent replication.ATP-dependent unwinding of a minimal origin of DNA replication by the origin-binding protein and the single-strand DNA-binding protein ICP8 from herpes simplex virus type I.
P2860
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P2860
Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.
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
Physical interaction between t ...... nded DNA-binding protein ICP8.
@ast
Physical interaction between t ...... nded DNA-binding protein ICP8.
@en
type
label
Physical interaction between t ...... nded DNA-binding protein ICP8.
@ast
Physical interaction between t ...... nded DNA-binding protein ICP8.
@en
prefLabel
Physical interaction between t ...... nded DNA-binding protein ICP8.
@ast
Physical interaction between t ...... nded DNA-binding protein ICP8.
@en
P2860
P356
P1476
Physical interaction between t ...... nded DNA-binding protein ICP8.
@en
P2093
I R Lehman
P E Boehmer
P2860
P304
P356
10.1073/PNAS.90.18.8444
P407
P577
1993-09-01T00:00:00Z