Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype.
about
Antivirals reduce the formation of key Alzheimer's disease molecules in cell cultures acutely infected with herpes simplex virus type 1Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection.Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.HSV-1 Cgal+ infection promotes quaking RNA binding protein production and induces nuclear-cytoplasmic shuttling of quaking I-5 isoform in human hepatoma cells.Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.Cytomegalovirus-mediated induction of antisense mRNA expression to UL44 inhibits virus replication in an astrocytoma cell line: identification of an essential gene.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 UL42Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures.Herpes simplex ICP27 mutant viruses exhibit reduced expression of specific DNA replication genesInteraction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateInhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecificThe extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.Characterization of lymphocytic choriomeningitis virus-binding protein(s): a candidate cellular receptor for the virus.Activity of the simian virus 40 early promoter-enhancer in herpes simplex virus type 1 vectors is dependent on its position, the infected cell type, and the presence of Vmw175.Identification of replication-competent HSV-1 Cgal+ strain signaling targets in human hepatoma cells by functional organelle proteomics.Identifying the features of purine dNTPs that allow accurate and efficient DNA replication by herpes simplex virus I DNA polymerase.Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.Cloning and functional analysis of Kaposi's sarcoma-associated herpesvirus DNA polymerase and its processivity factorND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase.Characterization of human herpesvirus 8 ORF59 protein (PF-8) and mapping of the processivity and viral DNA polymerase-interacting domains.Improved cell survival by the reduction of immediate-early gene expression in replication-defective mutants of herpes simplex virus type 1 but not by mutation of the virion host shutoff function.Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.Functional analysis of the herpes simplex virus UL42 protein.Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain.Cytotoxicity of a replication-defective mutant of herpes simplex virus type 1.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 mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis.The Epstein-Barr virus BMRF1 gene is essential for lytic virus replication.Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replication.
P2860
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P2860
Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype.
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
Isolation of a herpes simplex ...... ization of its null phenotype.
@ast
Isolation of a herpes simplex ...... ization of its null phenotype.
@en
type
label
Isolation of a herpes simplex ...... ization of its null phenotype.
@ast
Isolation of a herpes simplex ...... ization of its null phenotype.
@en
prefLabel
Isolation of a herpes simplex ...... ization of its null phenotype.
@ast
Isolation of a herpes simplex ...... ization of its null phenotype.
@en
P2093
P2860
P1433
P1476
Isolation of a herpes simplex ...... ization of its null phenotype.
@en
P2093
D S Parris
P A Johnson
T Friedmann
P2860
P304
P407
P577
1991-02-01T00:00:00Z