Dissecting the fidelity of bacteriophage RB69 DNA polymerase: site-specific modulation of fidelity by polymerase accessory proteins
about
The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerasesCharacterization of a replicative DNA polymerase mutant with reduced fidelity and increased translesion synthesis capacityVariation in Mutation Rates Caused by RB69pol Fidelity Mutants Can Be Rationalized on the Basis of Their Kinetic Behavior and Crystal StructuresA Remote Palm Domain Residue of RB69 DNA Polymerase Is Critical for Enzyme Activity and Influences the Conformation of the Active SiteDpb2p, a noncatalytic subunit of DNA polymerase epsilon, contributes to the fidelity of DNA replication in Saccharomyces cerevisiae.The high fidelity and unique error signature of human DNA polymerase epsilonBiochemical analysis of DNA polymerase η fidelity in the presence of replication protein ARPA and PCNA suppress formation of large deletion errors by yeast DNA polymerase delta.The fidelity of DNA synthesis by yeast DNA polymerase zeta alone and with accessory proteins.Effects of accessory proteins on the bypass of a cis-syn thymine-thymine dimer by Saccharomyces cerevisiae DNA polymerase eta.RB69 DNA polymerase structure, kinetics, and fidelity.Clusters of mutations from transient hypermutabilityMutational clusters generated by non-processive polymerases: A case study using DNA polymerase betain vitroThe C-terminal domain of the DNA polymerase catalytic subunit regulates the primase and polymerase activities of the human DNA polymerase α-primase complexReversal of a mutator activity by a nearby fidelity-neutral substitution in the RB69 DNA polymerase binding pocket.Kinetic 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 accuracyChaos and order in spontaneous mutation.The bacteriophage T4 rapid-lysis genes and their mutational proclivities.The roles of Tyr391 and Tyr619 in RB69 DNA polymerase replication fidelity.The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.Nucleic acid polymerases use a general acid for nucleotidyl transfer.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.
P2860
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P2860
Dissecting the fidelity of bacteriophage RB69 DNA polymerase: site-specific modulation of fidelity by polymerase accessory proteins
description
2002 nî lūn-bûn
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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2002年の論文
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2002年論文
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2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Dissecting the fidelity of bac ...... polymerase accessory proteins
@ast
Dissecting the fidelity of bac ...... polymerase accessory proteins
@en
Dissecting the fidelity of bac ...... polymerase accessory proteins
@nl
type
label
Dissecting the fidelity of bac ...... polymerase accessory proteins
@ast
Dissecting the fidelity of bac ...... polymerase accessory proteins
@en
Dissecting the fidelity of bac ...... polymerase accessory proteins
@nl
prefLabel
Dissecting the fidelity of bac ...... polymerase accessory proteins
@ast
Dissecting the fidelity of bac ...... polymerase accessory proteins
@en
Dissecting the fidelity of bac ...... polymerase accessory proteins
@nl
P2093
P2860
P1433
P1476
Dissecting the fidelity of bac ...... polymerase accessory proteins
@en
P2093
Anna Bebenek
Farid A Kadyrov
Geraldine T Carver
Holly Kloos Dressman
Jim D Karam
John W Drake
Joseph K Haseman
Vasiliy Petrov
William H Konigsberg
P2860
P304
P407
P50
P577
2002-11-01T00:00:00Z