Functional analysis of the herpes simplex virus UL42 protein.
about
Inhibition of Epstein-Barr virus replication by a benzimidazole L-riboside: novel antiviral mechanism of 5, 6-dichloro-2-(isopropylamino)-1-beta-L-ribofuranosyl-1H-benzimidazole.Hopping of a processivity factor on DNA revealed by single-molecule assays of diffusionHerpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.The 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 synthesisEvidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interfaceCloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory functionCytomegalovirus-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 UL42Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateTwo regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.The carboxyl terminus of the bacteriophage T4 DNA polymerase is required for holoenzyme complex formation.Regulated transport into the nucleus of herpesviridae DNA replication core proteins.DNA from Dust: Comparative Genomics of Large DNA Viruses in Field Surveillance SamplesCloning and functional analysis of Kaposi's sarcoma-associated herpesvirus DNA polymerase and its processivity factorCharacterization 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.Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein UL44 are crucial for interaction with the UL54 catalytic subunit.Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit.The pre-NH(2)-terminal domain of the herpes simplex virus 1 DNA polymerase catalytic subunit is required for efficient viral replication.
P2860
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P2860
Functional analysis of the herpes simplex virus UL42 protein.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Functional analysis of the herpes simplex virus UL42 protein.
@en
type
label
Functional analysis of the herpes simplex virus UL42 protein.
@en
prefLabel
Functional analysis of the herpes simplex virus UL42 protein.
@en
P2093
P2860
P1433
P1476
Functional analysis of the herpes simplex virus UL42 protein
@en
P2093
P2860
P304
P407
P50
P577
1993-03-01T00:00:00Z