Herpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication origin
about
Human herpesvirus 6B origin: sequence diversity, requirement for two binding sites for origin-binding protein, and enhanced replication from origin multimersPhosphorylation of the herpes simplex virus type 1 origin binding protein.Origin binding protein-containing protein-DNA complex formation at herpes simplex virus type 1 oriS: role in oriS-dependent DNA replication.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.Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: visualization of a specific preunwinding complex.Genetic requirements for homologous recombination in Autographa californica nucleopolyhedrovirusDNA binding activity of the herpes simplex virus type 1 origin binding protein, UL9, can be modulated by sequences in the N terminus: correlation between transdominance and DNA binding.An 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.Kaposi's sarcoma-associated herpesvirus ori-Lyt-dependent DNA replication: dual role of replication and transcription activator.Herpes simplex virus DNA replication: a spacer sequence directs the ATP-dependent formation of a nucleoprotein complex at oriS.The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structuresThe variable 3' ends of a human cytomegalovirus oriLyt transcript (SRT) overlap an essential, conserved replicator element.Properties of the novel herpes simplex virus type 1 origin binding protein, OBPCUnwinding 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.Easily unwound DNA sequences and hairpin structures in the Epstein-Barr virus origin of plasmid replication.Identification of EBNA1 amino acid sequences required for the interaction of the functional elements of the Epstein-Barr virus latent origin of DNA replicationCellular protein interactions with herpes simplex virus type 1 oriS.The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for functionInteraction of Epstein-Barr virus nuclear antigen 1 with the viral latent origin of replication.EBNA1 distorts oriP, the Epstein-Barr virus latent replication origin.Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.Herpes simplex virus: selection of origins of DNA replicationStructural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.Nucleoprotein complex formed between herpes simplex virus UL9 protein and the origin of DNA replication: inter- and intramolecular interactionsComplex 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 linking regions of EBNA1 are essential for its support of replication and transcription.Identification of persistent RNA-DNA hybrid structures within the origin of replication of human cytomegalovirus.Human cytomegalovirus UL84 localizes to the cell nucleus via a nuclear localization signal and is a component of viral replication compartments.Multiple regions within EBNA1 can link DNAs.Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.Sequence requirements of the Epstein-Barr virus latent origin of DNA replication.Boundaries and structure of human cytomegalovirus oriLyt, a complex origin for lytic-phase DNA replication.Human cytomegalovirus DNA replication requires transcriptional activation via an IE2- and UL84-responsive bidirectional promoter element within oriLyt.A truncated herpes simplex virus origin binding protein which contains the carboxyl terminal origin binding domain binds to the origin of replication but does not alter its conformation.Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.Evidence for DNA hairpin recognition by Zta at the Epstein-Barr virus origin of lytic replication.A DNA-binding activity in BPV initiator protein E1 required for melting duplex ori DNA but not processive helicase activity initiated on partially single-stranded DNA.
P2860
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P2860
Herpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication origin
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Herpes simplex virus origin-bi ...... s the viral replication origin
@ast
Herpes simplex virus origin-bi ...... s the viral replication origin
@en
type
label
Herpes simplex virus origin-bi ...... s the viral replication origin
@ast
Herpes simplex virus origin-bi ...... s the viral replication origin
@en
prefLabel
Herpes simplex virus origin-bi ...... s the viral replication origin
@ast
Herpes simplex virus origin-bi ...... s the viral replication origin
@en
P2093
P2860
P1433
P1476
Herpes simplex virus origin-bi ...... s the viral replication origin
@en
P2093
P2860
P304
P407
P577
1991-06-01T00:00:00Z