Preferred WMSA catalytic mechanism of the nucleotidyl transfer reaction in human DNA polymerase κ elucidates error-free bypass of a bulky DNA lesion.
about
A new paradigm of DNA synthesis: three-metal-ion catalysis.Molecular modeling of nucleic acid structure: energy and samplingAn overview of Y-Family DNA polymerases and a case study of human DNA polymerase ηRevelation of a catalytic calcium-binding site elucidates unusual metal dependence of a human apyraseStructural and dynamic characterization of polymerase κ's minor groove lesion processing reveals how adduct topology impacts fidelity.DNA cytosine methylation: structural and thermodynamic characterization of the epigenetic marking mechanism.Born-Oppenheimer Ab Initio QM/MM Molecular Dynamics Simulations of Enzyme Reactions.Variants of mouse DNA polymerase κ reveal a mechanism of efficient and accurate translesion synthesis past a benzo[a]pyrene dG adduct.Molecular modeling of nucleic acid structure: energy and sampling.Quantum mechanical modeling: a tool for the understanding of enzyme reactions.Applications of quantum mechanical/molecular mechanical methods to the chemical insertion step of DNA and RNA polymerization.Sirtuin Deacetylation Mechanism and Catalytic Role of the Dynamic Cofactor Binding Loop.Structure and mechanism of error-free replication past the major benzo[a]pyrene adduct by human DNA polymerase κ.Cooperative motion of a key positively charged residue and metal ions for DNA replication catalyzed by human DNA Polymerase-η.Translesion synthesis by POLKComputational Simulations of DNA Polymerases: Detailed Insights on Structure/Function/Mechanism from Native Proteins to Cancer Variants.POLK incorporates dNMP opposite to damaged DNA baseAnalysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases.Multiple proton relay routes in the reaction mechanism of RNAP II: assessing the effect of structural model.Enhanced Sampling in Molecular Dynamics Using Metadynamics, Replica-Exchange, and Temperature-Acceleration
P2860
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P2860
Preferred WMSA catalytic mechanism of the nucleotidyl transfer reaction in human DNA polymerase κ elucidates error-free bypass of a bulky DNA lesion.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
name
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@ast
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@en
type
label
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@ast
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@en
prefLabel
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@ast
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@en
P2093
P2860
P356
P1476
Preferred WMSA catalytic mecha ...... bypass of a bulky DNA lesion.
@en
P2093
Lee Lior-Hoffmann
Lihua Wang
Nicholas E Geacintov
Shenglong Wang
Suse Broyde
Yingkai Zhang
P2860
P304
P356
10.1093/NAR/GKS653
P407
P577
2012-07-05T00:00:00Z