The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase
about
Functional human mitochondrial DNA polymerase gamma forms a heterotrimerBinding of herpes simplex virus-1 US11 to specific RNA sequencesThe Crystal Structure of PF-8, the DNA Polymerase Accessory Subunit from Kaposi's Sarcoma-Associated HerpesvirusCrystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1Hopping of a processivity factor on DNA revealed by single-molecule assays of diffusionContributions of nucleotide excision repair, DNA polymerase eta, and homologous recombination to replication of UV-irradiated herpes simplex virus type 1Each monomer of the dimeric accessory protein for human mitochondrial DNA polymerase has a distinct role in conferring processivity.Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes.Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesiscdc2 cyclin-dependent kinase binds and phosphorylates herpes simplex virus 1 U(L)42 DNA synthesis processivity factorThe A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymeraseThe human cytomegalovirus UL44 C clamp wraps around DNA.The positively charged surface of herpes simplex virus UL42 mediates DNA binding.A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complexEffects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisRole of the specific interaction of UL112-113 p84 with UL44 DNA polymerase processivity factor in promoting DNA replication of human cytomegalovirus.A model for the mediation of processivity of DNA-targeting proteins by nonspecific binding: dependence on DNA length and presence of obstacles.The carboxy-terminal segment of the human cytomegalovirus DNA polymerase accessory subunit UL44 is crucial for viral replication.A structural basis for processivity.Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.Kinetic approaches to understanding the mechanisms of fidelity of the herpes simplex virus type 1 DNA polymeraseRNA polymerase II-dependent transcription in trypanosomes is associated with a SNAP complex-like transcription factor.The logic of DNA replication in double-stranded DNA viruses: insights from global analysis of viral genomesCloning, expression, and functional characterization of the equine herpesvirus 1 DNA polymerase and its accessory subunit.Protein-protein interactions as targets for antiviral chemotherapy.Herpes simplex virus 1 activates cdc2 to recruit topoisomerase II alpha for post-DNA synthesis expression of late genes.Biochemical analysis of human POLG2 variants associated with mitochondrial disease.Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.The late promoter of the human cytomegalovirus viral DNA polymerase processivity factor has an impact on delayed early and late viral gene products but not on viral DNA synthesisBinding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism.Noncanonical TATA sequence in the UL44 late promoter of human cytomegalovirus is required for the accumulation of late viral transcripts.Low-resolution structure of vaccinia virus DNA replication machineryMolecular modeling and expression of the Litopenaeus vannamei proliferating cell nuclear antigen (PCNA) after white spot syndrome virus shrimp infection.Regulated transport into the nucleus of herpesviridae DNA replication core proteins.Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.Proliferating cell nuclear antigen uses two distinct modes to move along DNA.The flexible loop of the human cytomegalovirus DNA polymerase processivity factor ppUL44 is required for efficient DNA binding and replication in cells.DNA from Dust: Comparative Genomics of Large DNA Viruses in Field Surveillance SamplesEpstein-Barr virus polymerase processivity factor enhances BALF2 promoter transcription as a coactivator for the BZLF1 immediate-early protein.
P2860
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P2860
The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
@wuu
name
The crystal structure of an un ...... inus of its cognate polymerase
@ast
The crystal structure of an un ...... inus of its cognate polymerase
@en
The crystal structure of an un ...... inus of its cognate polymerase
@nl
type
label
The crystal structure of an un ...... inus of its cognate polymerase
@ast
The crystal structure of an un ...... inus of its cognate polymerase
@en
The crystal structure of an un ...... inus of its cognate polymerase
@nl
prefLabel
The crystal structure of an un ...... inus of its cognate polymerase
@ast
The crystal structure of an un ...... inus of its cognate polymerase
@en
The crystal structure of an un ...... inus of its cognate polymerase
@nl
P50
P3181
P1433
P1476
The crystal structure of an un ...... inus of its cognate polymerase
@en
P2093
P304
P3181
P356
10.1016/S1097-2765(00)80422-0
P577
2000-02-01T00:00:00Z