The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision.
about
Initiation of new DNA strands by the herpes simplex virus-1 primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alphaProcessing of lagging-strand intermediates in vitro by herpes simplex virus type 1 DNA polymeraseEffects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisKinetic approaches to understanding the mechanisms of fidelity of the herpes simplex virus type 1 DNA polymeraseProcessivity clamp gp45 and ssDNA-binding-protein gp32 modulate the fidelity of bacteriophage RB69 DNA polymerase in a sequence-specific manner, sometimes enhancing and sometimes compromising accuracyDNA mismatch repair proteins are required for efficient herpes simplex virus 1 replicationReplication-Coupled Recruitment of Viral and Cellular Factors to Herpes Simplex Virus Type 1 Replication Forks for the Maintenance and Expression of Viral Genomes.3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity.Identifying the features of purine dNTPs that allow accurate and efficient DNA replication by herpes simplex virus I DNA polymerase.Mechanisms by which herpes simplex virus DNA polymerase limits translesion synthesis through abasic sites.Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.Engineering of a chimeric RB69 DNA polymerase sensitive to drugs targeting the cytomegalovirus enzyme.Replication and recombination of herpes simplex virus DNAPolymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated.Coordinated leading and lagging strand DNA synthesis by using the herpes simplex virus 1 replication complex and minicircle DNA templatesProtein Displacement by Herpes Helicase-Primase and the Key Role of UL42 during Helicase-Coupled DNA Synthesis by the Herpes Polymerase.Altered order of substrate binding by DNA polymerase X from African Swine Fever virus.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.Contribution of the 3'- to 5'-exonuclease activity of herpes simplex virus type 1 DNA polymerase to the fidelity of DNA synthesis.Proofreading-Deficient Coronaviruses Adapt for Increased Fitness over Long-Term Passage without Reversion of Exoribonuclease-Inactivating Mutations.Enzymatic therapeutic index of acyclovir. Viral versus human polymerase gamma specificity.
P2860
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P2860
The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision.
description
2003 nî lūn-bûn
@nan
2003年の論文
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2003年論文
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2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
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2003年论文
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2003年论文
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2003年论文
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name
The herpes simplex virus type ...... or polymerization or excision.
@en
type
label
The herpes simplex virus type ...... or polymerization or excision.
@en
prefLabel
The herpes simplex virus type ...... or polymerization or excision.
@en
P2093
P2860
P356
P1476
The herpes simplex virus type ...... or polymerization or excision.
@en
P2093
Deborah S Parris
Liping Song
Murari Chaudhuri
P2860
P304
P356
10.1074/JBC.M210023200
P407
P577
2003-01-08T00:00:00Z