Structure of PolC reveals unique DNA binding and fidelity determinants - Wikidata - awgldk - TriplyDB

Structure of PolC reveals unique DNA binding and fidelity determinants

Structure of PolC reveals unique DNA binding and fidelity determinants

http://www.wikidata.org/entity/Q27653260

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Structural basis of high-fidelity DNA synthesis by yeast DNA polymerase delta ComEA is essential for the transfer of external DNA into the periplasm in naturally transformable Vibrio cholerae cells Watching DNA polymerase η make a phosphodiester bond Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis Structure of the PolIIIα-τc-DNA Complex Suggests an Atomic Model of the Replisome A structural role for the PHP domain in E. coli DNA polymerase III Structural Factors That Determine Selectivity of a High Fidelity DNA Polymerase for Deoxy-, Dideoxy-, and Ribonucleotides Capture of a third Mg²⁺ is essential for catalyzing DNA synthesis Identification of single-stranded and double-stranded DNA binding proteins based on protein structure An overview of Y-Family DNA polymerases and a case study of human DNA polymerase η Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography The N-terminal region of the bacterial DNA polymerase PolC features a pair of domains, both distantly related to domain V of the DNA polymerase III τ subunit.How a homolog of high-fidelity replicases conducts mutagenic DNA synthesis Structural comparison of DNA polymerase architecture suggests a nucleotide gateway to the polymerase active site.Distinct co-evolution patterns of genes associated to DNA polymerase III DnaE and PolC.Evidence for a non-catalytic ion-binding site in multiple RNA-dependent RNA polymerases.Kinetic characterization of exonuclease-deficient Staphylococcus aureus PolC, a C-family replicative DNA polymerase.Breaking the rules: bacteria that use several DNA polymerase IIIs.Bacterial replicases and related polymerases Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Clostridium difficile DNA polymerase IIIC: basis for activity of antibacterial compounds A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.Replicative DNA polymerases.Dynamics of site switching in DNA polymerase.A consensus view of DNA binding by the C family of replicative DNA polymerases Replisome structure and conformational dynamics underlie fork progression past obstacles.Error-prone DnaE2 Balances the Genome Mutation Rates in Myxococcus xanthus DK1622.Recognition of Watson-Crick base pairs: constraints and limits due to geometric selection and tautomerism.Structural diversity of the Y-family DNA polymerases.Selective in vivo and in vitro activities of 3,3'-4-nitrobenzylidene-bis-4-hydroxycoumarin against methicillin-resistant Staphylococcus aureus by inhibition of DNA polymerase III.The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Mechanism of polymerase collision release from sliding clamps on the lagging strand.DNA Replication in Mycobacterium tuberculosis.The rate of polymerase release upon filling the gap between Okazaki fragments is inadequate to support cycling during lagging strand synthesis Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair.cryo-EM structures of the E. coli replicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease and τ.Comprehensive analysis of DNA polymerase III α subunits and their homologs in bacterial genomes High-fidelity DNA replication in Mycobacterium tuberculosis relies on a trinuclear zinc center.Calcium-driven DNA synthesis by a high-fidelity DNA polymerase.2'-Deoxyribonucleoside phosphoramidate triphosphate analogues as alternative substrates for E. coli polymerase III.

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P2860

Structure of PolC reveals unique DNA binding and fidelity determinants

http://www.wikidata.org/entity/Q27653260

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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type

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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prefLabel

Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Proceedings of the National Academy of Sciences of the United States of America

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Structure of PolC reveals unique DNA binding and fidelity determinants

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Douglas R Davies

http://www.w3.org/2001/XMLSchema#string

James M Bullard

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Jeffrey Christensen

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Joseph W Guiles

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Louis S Green

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Nebojsa Janjic

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Ronald J Evans

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Thale C Jarvis

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Wendy K Ribble

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P2860

CELLULAR DNA REPLICASES: Components and Dynamics at the Replication Fork

A general two-metal-ion mechanism for catalytic RNA

Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.

Structure of a Sliding Clamp on DNA

Insights into the Replisome from the Structure of a Ternary Complex of the DNA Polymerase III α-Subunit

Structure of DNA polymerase I Klenow fragment bound to duplex DNA

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution

Structures of mismatch replication errors observed in a DNA polymerase

Visualizing polynucleotide polymerase machines at work

DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history.

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20695-700

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3963140

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10.1073/PNAS.0809989106

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52

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105

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23687977

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19106298

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2634937

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