Binding of the herpes simplex virus type 1 UL9 gene product to an origin of viral DNA replication.
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Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alphaAlphaherpesvirus origin-binding protein homolog encoded by human herpesvirus 6B, a betaherpesvirus, binds to nucleotide sequences that are similar to ori regions of alphaherpesvirusesCellular transcription factors enhance herpes simplex virus type 1 oriS-dependent DNA replication.Site-directed mutagenesis of large DNA palindromes: construction and in vitro characterization of herpes simplex virus type 1 mutants containing point mutations that eliminate the oriL or oriS initiation functionHerpes simplex virus DNA replication: a spacer sequence directs the ATP-dependent formation of a nucleoprotein complex at oriS.Cloning and characterization of herpes simplex virus type 1 oriL: comparison of replication and protein-DNA complex formation by oriL and oriSHuman 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 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, OBPCDifferential effects of nerve growth factor and dexamethasone on herpes simplex virus type 1 oriL- and oriS-dependent DNA replication in PC12 cells.Human cytomegalovirus UL84 interacts with an RNA stem-loop sequence found within the RNA/DNA hybrid region of oriLyt.Replication-Coupled Recruitment of Viral and Cellular Factors to Herpes Simplex Virus Type 1 Replication Forks for the Maintenance and Expression of Viral Genomes.Complementary intrastrand base pairing during initiation of Herpes simplex virus type 1 DNA replicationTranscriptional 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.Inhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecificCellular 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 functionConstruction and properties of a recombinant herpes simplex virus 1 lacking both S-component origins of DNA synthesis.Herpes simplex virus type 1 origin-specific binding protein: oriS-binding properties and effects of cellular proteinsHerpes simplex virus origin-binding protein (UL9) loops and distorts the viral replication originPurification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.Localization of a phytochrome-responsive element within the upstream region of pea rbcS-3AIdentification of the lytic origin of DNA replication in human cytomegalovirus by a novel approach utilizing ganciclovir-induced chain termination.Structural 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 interactionsCloning and expression of an equine herpesvirus 1 origin-binding proteinThe 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.Novel DNA binding specificities of a putative herpesvirus bZIP oncoprotein.A 269-amino-acid segment with a pseudo-leucine zipper and a helix-turn-helix motif codes for the sequence-specific DNA-binding domain of herpes simplex virus type 1 origin-binding protein.Boundaries and structure of human cytomegalovirus oriLyt, a complex origin for lytic-phase DNA replication.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 helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities.Common structural features of replication origins in all life forms.Spacing between GT-1 binding sites within a light-responsive element is critical for transcriptional activity.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.Stepwise evolution of the herpes simplex virus origin binding protein and origin of replicationActivation 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.
P2860
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P2860
Binding of the herpes simplex virus type 1 UL9 gene product to an origin of viral DNA replication.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Binding of the herpes simplex ...... igin of viral DNA replication.
@en
type
label
Binding of the herpes simplex ...... igin of viral DNA replication.
@en
prefLabel
Binding of the herpes simplex ...... igin of viral DNA replication.
@en
P2093
P2860
P356
P1476
Binding of the herpes simplex ...... igin of viral DNA replication.
@en
P2093
P2860
P304
P356
10.1093/NAR/17.4.1409
P407
P577
1989-02-01T00:00:00Z