Sequence and mapping analyses of the herpes simplex virus DNA polymerase gene predict a C-terminal substrate binding domain.
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Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerasesA human cytomegalovirus mutant resistant to the nucleoside analog 9-([2-hydroxy-1-(hydroxymethyl)ethoxy]methyl)guanine (BW B759U) induces reduced levels of BW B759U triphosphateAnti-human immunodeficiency virus agent 3'-azido-3'-deoxythymidine inhibits replication of Epstein-Barr virusSequence analyses of herpesviral enzymes suggest an ancient origin for human sexual behavior.DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence, mapping of a temperature-sensitive mutation, and protein homology with other DNA polymerasesThe highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-Ser in alpha-like DNA polymerases is required by phage phi 29 DNA polymerase for protein-primed initiation and polymerizationIdentification of amino acids in herpes simplex virus DNA polymerase involved in substrate and drug recognition.Replication of herpes simplex virus DNA.A monoclonal antibody that neutralizes Epstein-Barr virus, human cytomegalovirus, human herpesvirus 6, and bacteriophage T4 DNA polymerases.T5 DNA polymerase: structural--functional relationships to other DNA polymerases.Structural and functional relationships between prokaryotic and eukaryotic DNA polymerases.Genetic evidence for two protein domains and a potential new activity in bacteriophage T4 DNA polymeraseBacteriophage PRD1 DNA polymerase: evolution of DNA polymerasesSpecific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interfaceHomology between DNA polymerases of poxviruses, herpesviruses, and adenoviruses: nucleotide sequence of the vaccinia virus DNA polymerase geneMutation within the herpes simplex virus DNA polymerase gene conferring resistance to (R)-9-(3,4-dihydroxybutyl)guanine.Compilation and alignment of DNA polymerase sequences.A point mutation in the human cytomegalovirus DNA polymerase gene confers resistance to ganciclovir and phosphonylmethoxyalkyl derivatives.Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells.Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction.Structural and functional analysis of temperature-sensitive mutants of the phage phi 29 DNA polymerase.Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity.Aphidicolin resistance in herpes simplex virus type I reveals features of the DNA polymerase dNTP binding site.Conformational changes induced in herpes simplex virus DNA polymerase upon DNA binding.Anionic regions in nuclear proteinsGenomic localization, sequence analysis, and transcription of the putative human cytomegalovirus DNA polymerase gene.The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.In vitro expression of the human cytomegalovirus DNA polymerase gene: effects of sequence alterations on enzyme activity.Molecular genetic analysis of vaccinia virus DNA polymerase mutants.Structure-function studies of the herpes simplex virus type 1 DNA polymerase.Restricted expression of herpes simplex virus lytic genes during establishment of latent infection by thymidine kinase-negative mutant viruses.Engineered herpes simplex virus DNA polymerase point mutants: the most highly conserved region shared among alpha-like DNA polymerases is involved in substrate recognition.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.Isolation and characterization of herpes simplex virus mutants containing engineered mutations at the DNA polymerase locus.Translational regulation of herpes simplex virus DNA polymerase.Identification of herpes simplex virus type 1 genes required for origin-dependent DNA synthesis.Structures of herpes simplex virus type 1 genes required for replication of virus DNALocations of amino acid substitutions in bacteriophage T4 tsL56 DNA polymerase predict an N-terminal exonuclease domain.Analysis of the transcript of the herpes simplex virus DNA polymerase gene provides evidence that polymerase expression is inefficient at the level of translation.
P2860
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P2860
Sequence and mapping analyses of the herpes simplex virus DNA polymerase gene predict a C-terminal substrate binding domain.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1985
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Sequence and mapping analyses ...... inal substrate binding domain.
@en
Sequence and mapping analyses ...... inal substrate binding domain.
@nl
type
label
Sequence and mapping analyses ...... inal substrate binding domain.
@en
Sequence and mapping analyses ...... inal substrate binding domain.
@nl
prefLabel
Sequence and mapping analyses ...... inal substrate binding domain.
@en
Sequence and mapping analyses ...... inal substrate binding domain.
@nl
P2093
P2860
P356
P1476
Sequence and mapping analyses ...... minal substrate binding domain
@en
P2093
P2860
P304
P356
10.1073/PNAS.82.23.7969
P407
P577
1985-12-01T00:00:00Z