DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase beta. Implication for the identity of the rate-limiting conformational change.
about
DNA polymerase family X: function, structure, and cellular rolesCoordination of steps in single-nucleotide base excision repair mediated by apurinic/apyrimidinic endonuclease 1 and DNA polymerase betaStable complexes formed by HIV-1 reverse transcriptase at distinct positions on the primer-template controlled by binding deoxynucleoside triphosphates or foscarnetProcessive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations.Sequential structures provide insights into the fidelity of RNA replicationStructures of DNA Polymerase β with Active-Site Mismatches Suggest a Transient Abasic Site Intermediate during Misincorporationα,β-Difluoromethylene Deoxynucleoside 5′-Triphosphates: A Convenient Synthesis of Useful Probes for DNA Polymerase β Structure and FunctionDNA Polymerase Substrate Specificity: SIDE CHAIN MODULATION OF THE"A-RULE"Amino Acid Substitution in the Active Site of DNA Polymerase β Explains the Energy Barrier of the Nucleotidyl Transfer ReactionUnfavorable Electrostatic and Steric Interactions in DNA Polymerase β E295K Mutant Interfere with the Enzyme’s PathwayStructures of the Leishmania infantum polymerase betaAn AP endonuclease 1-DNA polymerase beta complex: theoretical prediction of interacting surfacesPhylogenetic analysis and evolutionary origins of DNA polymerase X-family membersComputer simulations of protein functions: searching for the molecular origin of the replication fidelity of DNA polymerasesRegulation of DNA repair fidelity by molecular checkpoints: "gates" in DNA polymerase beta's substrate selectionDistinct energetics and closing pathways for DNA polymerase beta with 8-oxoG template and different incoming nucleotides.Revealing the role of the product metal in DNA polymerase β catalysis.DNA polymerase β uses its lyase domain in a processive search for DNA damage.Fluorescence resonance energy transfer studies of DNA polymerase β: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.Fidelity of Nucleotide Incorporation by the RNA-Dependent RNA Polymerase from Poliovirus.DNA polymerase beta ribonucleotide discrimination: insertion, misinsertion, extension, and coding.Highly organized but pliant active site of DNA polymerase beta: compensatory mechanisms in mutant enzymes revealed by dynamics simulations and energy analyses.Dependence of DNA polymerase replication rate on external forces: a model based on molecular dynamics simulationsIn silico evidence for DNA polymerase-beta's substrate-induced conformational changeIdentification of critical residues for the tight binding of both correct and incorrect nucleotides to human DNA polymerase λModeling DNA polymerase μ motions: subtle transitions before chemistry.In silico studies of the African swine fever virus DNA polymerase X support an induced-fit mechanismSubstrate-induced DNA polymerase β activation.Efficiency and fidelity of human DNA polymerases λ and β during gap-filling DNA synthesis.Remote site control of an active site fidelity checkpoint in a viral RNA-dependent RNA polymerase.Energy analysis of chemistry for correct insertion by DNA polymerase beta.Sequential side-chain residue motions transform the binary into the ternary state of DNA polymerase lambda.Prechemistry versus preorganization in DNA replication fidelity.DNA replication fidelity.Loop II of DNA polymerase beta is important for polymerization activity and fidelity.DNA base excision repair: a mechanism of trinucleotide repeat expansion.Metal-induced DNA translocation leads to DNA polymerase conformational activation.Base excision repair: contribution to tumorigenesis and target in anticancer treatment paradigmsRequirement for transient metal ions revealed through computational analysis for DNA polymerase going in reverse.Nucleotide binding interactions modulate dNTP selectivity and facilitate 8-oxo-dGTP incorporation by DNA polymerase lambda.
P2860
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P2860
DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase beta. Implication for the identity of the rate-limiting conformational change.
description
2000 nî lūn-bûn
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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
DNA structure and aspartate 27 ...... imiting conformational change.
@ast
DNA structure and aspartate 27 ...... imiting conformational change.
@en
type
label
DNA structure and aspartate 27 ...... imiting conformational change.
@ast
DNA structure and aspartate 27 ...... imiting conformational change.
@en
prefLabel
DNA structure and aspartate 27 ...... imiting conformational change.
@ast
DNA structure and aspartate 27 ...... imiting conformational change.
@en
P2093
P2860
P356
P1476
DNA structure and aspartate 27 ...... imiting conformational change.
@en
P2093
Vande Berg BJ
P2860
P304
P356
10.1074/JBC.M002884200
P407
P577
2000-10-09T00:00:00Z