A peptide switch regulates DNA polymerase processivity. - Wikidata - wikimedia - TriplyDB

A peptide switch regulates DNA polymerase processivity.

A peptide switch regulates DNA polymerase processivity.

http://www.wikidata.org/entity/Q34383032

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Clamp loader ATPases and the evolution of DNA replication machinery.Structure of a small-molecule inhibitor of a DNA polymerase sliding clamp Insights into the Replisome from the Structure of a Ternary Complex of the DNA Polymerase III α-Subunit Structure of the PolIIIα-τc-DNA Complex Suggests an Atomic Model of the Replisome Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast Dpb2p, a noncatalytic subunit of DNA polymerase epsilon, contributes to the fidelity of DNA replication in Saccharomyces cerevisiae.Essential roles for imuA'- and imuB-encoded accessory factors in DnaE2-dependent mutagenesis in Mycobacterium tuberculosis Coordinating DNA polymerase traffic during high and low fidelity synthesis.Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter spp Timing, coordination, and rhythm: acrobatics at the DNA replication fork.Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair.dnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit Gene 5.5 protein of bacteriophage T7 in complex with Escherichia coli nucleoid protein H-NS and transfer RNA masks transfer RNA priming in T7 DNA replication.Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.DNA replication fidelity in Escherichia coli: a multi-DNA polymerase affair.DNA repair and genome maintenance in Bacillus subtilis.Replisome architecture and dynamics in Escherichia coli.Role of accessory DNA polymerases in DNA replication in Escherichia coli: analysis of the dnaX36 mutator mutant.Dynamics of loading the Escherichia coli DNA polymerase processivity clamp.A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.A single subunit directs the assembly of the Escherichia coli DNA sliding clamp loader.Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis Steric gate variants of UmuC confer UV hypersensitivity on Escherichia coli.Cycling of the E. coli lagging strand polymerase is triggered exclusively by the availability of a new primer at the replication fork Regulation of interactions with sliding clamps during DNA replication and repair.Replication-fork dynamics.Maturation of bacteriophage T4 lagging strand fragments depends on interaction of T4 RNase H with T4 32 protein rather than the T4 gene 45 clamp.Mechanism of polymerase collision release from sliding clamps on the lagging strand.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.Binding Affinities among DNA Helicase-Primase, DNA Polymerase, and Replication Intermediates in the Replisome of Bacteriophage T7.Competition of bacteriophage polypeptides with native replicase proteins for binding to the DNA sliding clamp reveals a novel mechanism for DNA replication arrest in Staphylococcus aureus.Conserved interactions in the Staphylococcus aureus DNA PolC chromosome replication machine.Screening of E. coli β-clamp Inhibitors Revealed that Few Inhibit Helicobacter pylori More Effectively: Structural and Functional Characterization.Primer utilization by DNA polymerase alpha-primase is influenced by its interaction with Mcm10p.Targeting the β-clamp in Helicobacter pylori with FDA-approved drugs reveals micromolar inhibition by diflunisal.A clamp-like biohybrid catalyst for DNA oxidation.Mutator mutants of Escherichia coli carrying a defect in the DNA polymerase III tau subunit.

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P2860

A peptide switch regulates DNA polymerase processivity.

http://www.wikidata.org/entity/Q34383032

description

2003 nî lūn-bûn

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2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի նոյեմբերին հրատարակված գիտական հոդված

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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

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2003年論文

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2003年論文

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2003年论文

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name

A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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type

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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A peptide switch regulates DNA polymerase processivity.

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

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A peptide switch regulates DNA polymerase processivity.

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Francisco J López de Saro

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

Mike O'Donnell

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

Roxana E Georgescu

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

P2860

The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo

Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex

Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III

Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp

Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA

The puzzle of PCNA's many partners.

A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems.

DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine.

Polymerases and the replisome: machines within machines.

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