Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.
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Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alphaDetermination and analysis of the complete nucleotide sequence of human herpesvirusThe 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 DNAA yeast gene required for DNA replication encodes a protein with homology to DNA helicases.Inhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the UL5-UL8-UL52 complexPhosphorylation of the herpes simplex virus type 1 origin binding protein.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.Association between the herpes simplex virus-1 DNA polymerase and uracil DNA glycosylaseOrigin-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.Herpes simplex virus DNA replication: a spacer sequence directs the ATP-dependent formation of a nucleoprotein complex at oriS.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.Human herpesvirus 6B origin-binding protein: DNA-binding domain and consensus binding sequence.The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structuresProperties 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.Replication of simian virus 40 origin-containing DNA during infection with a recombinant Autographa californica multiple nuclear polyhedrosis virus expressing large T antigen.Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of oriLyt.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.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.The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA helicaseUnderstanding helicases as a means of virus control.Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.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.Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.cis-acting elements in the lytic origin of DNA replication of Epstein-Barr virusTwo regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for functionHerpes simplex virus: selection of origins of DNA replicationFunctional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activityCellular proteins bind to the downstream component of the lytic origin of DNA replication of Epstein-Barr virus.Cloning and expression of an equine herpesvirus 1 origin-binding proteinUnwinding 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.Vaccinia virion protein I8R has both DNA and RNA helicase activities: implications for vaccinia virus transcription.Inhibition of topoisomerase II by ICRF-193 prevents efficient replication of herpes simplex virus type 1.Initiation of lytic DNA replication in Epstein-Barr virus: search for a common family mechanism.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.
P2860
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P2860
Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Purification and characterizat ...... type 1 origin-binding protein.
@ast
Purification and characterizat ...... type 1 origin-binding protein.
@en
type
label
Purification and characterizat ...... type 1 origin-binding protein.
@ast
Purification and characterizat ...... type 1 origin-binding protein.
@en
prefLabel
Purification and characterizat ...... type 1 origin-binding protein.
@ast
Purification and characterizat ...... type 1 origin-binding protein.
@en
P2860
P1433
P1476
Purification and characterizat ...... type 1 origin-binding protein.
@en
P2093
Challberg MD
P2860
P304
P407
P577
1992-07-01T00:00:00Z