Unwinding 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.
about
Replication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathwayThe bipolar filaments formed by herpes simplex virus type 1 SSB/recombination protein (ICP8) suggest a mechanism for DNA annealing.The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication.Modulation of the herpes simplex virus type-1 UL9 DNA helicase by its cognate single-strand DNA-binding protein, ICP8.Replication of herpes simplex virus DNA.The human DnaJ protein, hTid-1, enhances binding of a multimer of the herpes simplex virus type 1 UL9 protein to oris, an origin of viral DNA replication.The cellular localization pattern of Varicella-Zoster virus ORF29p is influenced by proteasome-mediated degradationOrigin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA.Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replicationAn initial ATP-independent step in the unwinding of a herpes simplex virus type I origin of replication by a complex of the viral origin-binding protein and single-strand DNA-binding protein.A multifunctional plasmid-encoded replication initiation protein both recruits and positions an active helicase at the replication origin.Double-stranded DNA and double-stranded RNA induce a common antiviral signaling pathway in human cells.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.Viral and Cellular Components of AAV2 Replication Compartments.The neural F-box protein NFB42 mediates the nuclear export of the herpes simplex virus type 1 replication initiator protein (UL9 protein) after viral infection.Targeting Holliday junctions by origin DNA-binding protein of herpes simplex virus type 1.The 60-residue C-terminal region of the single-stranded DNA binding protein of herpes simplex virus type 1 is required for cooperative DNA binding.Unwinding of a herpes simplex virus type 1 origin of replication (Ori(S)) by a complex of the viral origin binding protein and the single-stranded DNA binding protein.Complex of the herpes simplex virus type 1 origin binding protein UL9 with DNA as a platform for the design of a new type of antiviral drugs.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.Initiation of Epstein-Barr virus lytic replication requires transcription and the formation of a stable RNA-DNA hybrid molecule at OriLyt.Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.ssDNA-dependent colocalization of adeno-associated virus Rep and herpes simplex virus ICP8 in nuclear replication domains.The interaction of herpes simplex type 1 virus origin-binding protein (UL9 protein) with Box I, the high affinity element of the viral origin of DNA replication.Residues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity.The herpes simplex virus type 1 origin-binding protein. sequence-specific activation of adenosine triphosphatase activity by a double-stranded DNA containing box I.Isolation and characterization of a processive DNA helicase from the fission yeast Schizosaccharomyces pombe that translocates in a 5'-to-3' direction.Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.Activation of the herpes simplex virus type-1 origin-binding protein (UL9) by heat shock proteins.Cysteine 111 affects coupling of single-stranded DNA binding to ATP hydrolysis in the herpes simplex virus type-1 origin-binding protein.The herpes simplex virus type-1 single-strand DNA-binding protein, ICP8, increases the processivity of the UL9 protein DNA helicase.Dual functions of single-stranded DNA-binding protein in helicase loading at the bacteriophage T4 DNA replication fork.
P2860
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P2860
Unwinding 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.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Unwinding of the box I element ...... tein, and single-stranded DNA.
@ast
Unwinding of the box I element ...... tein, and single-stranded DNA.
@en
type
label
Unwinding of the box I element ...... tein, and single-stranded DNA.
@ast
Unwinding of the box I element ...... tein, and single-stranded DNA.
@en
prefLabel
Unwinding of the box I element ...... tein, and single-stranded DNA.
@ast
Unwinding of the box I element ...... tein, and single-stranded DNA.
@en
P2860
P356
P1476
Unwinding of the box I element ...... tein, and single-stranded DNA.
@en
P2093
P2860
P304
P356
10.1073/PNAS.94.7.2838
P407
P577
1997-04-01T00:00:00Z