Identification of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1.
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Human herpesvirus 6The Crystal Structure of PF-8, the DNA Polymerase Accessory Subunit from Kaposi's Sarcoma-Associated HerpesvirusInhibition of herpes simplex virus replication by a 2-amino thiazole via interactions with the helicase component of the UL5-UL8-UL52 complexThe positively charged surface of herpes simplex virus UL42 mediates DNA binding.Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisThe complete genome sequence of herpesvirus papio 2 (Cercopithecine herpesvirus 16) shows evidence of recombination events among various progenitor herpesvirusesEvidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction.Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateHelicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.Inhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecificTwo regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.The UL5 gene of herpes simplex virus type 1: isolation of a lacZ insertion mutant and association of the UL5 gene product with other members of the helicase-primase complex.Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype.The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for functionPurification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.Kinetics of expression of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1.Herpes simplex virus type 1 gene products required for DNA replication: identification and overexpression.Herpes simplex virus type 1 DNA synthesis requires the product of the UL8 gene: isolation and characterization of an ICP6::lacZ insertion mutation.Localization of the herpes simplex virus type 1 65-kilodalton DNA-binding protein and DNA polymerase in the presence and absence of viral DNA synthesis.The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity.Site-specific mutagenesis of a highly conserved region of the herpes simplex virus type 1 DNA polymerase gene.A major transcriptional regulatory protein (ICP4) of herpes simplex virus type 1 is associated with purified virions.The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymeraseExpression of herpes simplex virus type 1 DNA polymerase in Saccharomyces cerevisiae and detection of virus-specific enzyme activity in cell-free lysatesPurification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein: properties of the protein and evidence of its association with the virus-encoded DNA polymerase.Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated.Herpes simplex virus DNA synthesis at a preformed replication fork in vitro.Binding of the herpes simplex virus type 1 UL9 gene product to an origin of viral DNA replication.Characterization of human herpesvirus 8 ORF59 protein (PF-8) and mapping of the processivity and viral DNA polymerase-interacting domains.Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches.Association of a major transcriptional regulatory protein, ICP4, of herpes simplex virus type 1 with the plasma membrane of virus-infected cells.A subset of herpes simplex virus replication genes provides helper functions for productive adeno-associated virus replication.Localization on the herpes simplex virus type 1 genome of a region encoding proteins involved in adsorption to the cellular receptor.A subset of herpes simplex virus replication genes induces DNA amplification within the host cell genome.Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication.Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities.Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis.
P2860
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P2860
Identification of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Identification of the gene enc ...... f herpes simplex virus type 1.
@en
type
label
Identification of the gene enc ...... f herpes simplex virus type 1.
@en
prefLabel
Identification of the gene enc ...... f herpes simplex virus type 1.
@en
P2093
P2860
P1433
P1476
Identification of the gene enc ...... f herpes simplex virus type 1.
@en
P2093
D J McGeoch
D S Parris
H S Marsden
P2860
P304
P407
P577
1988-03-01T00:00:00Z