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.
about
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 synthesisSpecific 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.Protein-protein interactions as targets for antiviral chemotherapy.Leading and lagging strand DNA synthesis in vitro by a reconstituted herpes simplex virus type 1 replisome.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 UL42The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer templateThe carboxyl terminus of the bacteriophage T4 DNA polymerase is required for holoenzyme complex formation.The DNA ligands influence the interactions between the herpes simplex virus 1 origin binding protein and the single strand DNA-binding protein, ICP-8.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.Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44Characterization of monoclonal antibodies that recognize the amino- and carboxy-terminal epitopes of the pseudorabies virus UL42 protein.The C-terminal domain of Saccharomyces cerevisiae DNA topoisomerase II.Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase.
P2860
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P2860
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.
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
Sequences at the C-terminus of ...... gin-dependent DNA replication.
@en
type
label
Sequences at the C-terminus of ...... gin-dependent DNA replication.
@en
prefLabel
Sequences at the C-terminus of ...... gin-dependent DNA replication.
@en
P2860
P356
P1476
Sequences at the C-terminus of ...... gin-dependent DNA replication.
@en
P2093
P2860
P356
10.1093/NAR/21.1.87
P577
1993-01-01T00:00:00Z