RuvAB is essential for replication forks reversal in certain replication mutants. - Wikidata - wikimedia - TriplyDB

RuvAB is essential for replication forks reversal in certain replication mutants.

RuvAB is essential for replication forks reversal in certain replication mutants.

http://www.wikidata.org/entity/Q34410893

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I came to a fork in the DNA and there was RecG Analysis of the SOS response of Vibrio and other bacteria with multiple chromosomes.ruvA Mutants that resolve Holliday junctions but do not reverse replication forks Low efficiency of homology-facilitated illegitimate recombination during conjugation in Escherichia coli.Replication fork reversal after replication-transcription collision.Regression of replication forks stalled by leading-strand template damage: I. Both RecG and RuvAB catalyze regression, but RuvC cleaves the holliday junctions formed by RecG preferentially.ssb gene duplication restores the viability of ΔholC and ΔholD Escherichia coli mutants In silico identification of a multi-functional regulatory protein involved in Holliday junction resolution in bacteria.Escherichia coli radD (yejH) gene: a novel function involved in radiation resistance and double-strand break repair.Topological locking restrains replication fork reversal.Functions that Protect Escherichia coli from Tightly Bound DNA-Protein Complexes Created by Mutant EcoRII Methyltransferase.Functional analysis of DNA replication fork reversal catalyzed by Mycobacterium tuberculosis RuvAB proteins.Inactivation of the DnaB helicase leads to the collapse and degradation of the replication fork: a comparison to UV-induced arrest.UvrD controls the access of recombination proteins to blocked replication forks Cleavage of stalled forks by fission yeast Mus81/Eme1 in absence of DNA replication checkpoint Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair Characterization of Plasmodium falciparum ATP-dependent DNA helicase RuvB3.Replication fork reversal and the maintenance of genome stability Homologous recombination as a replication fork escort: fork-protection and recovery.Mycobacterium tuberculosis RecG protein but not RuvAB or RecA protein is efficient at remodeling the stalled replication forks: implications for multiple mechanisms of replication restart in mycobacteria RecG controls DNA amplification at double-strand breaks and arrested replication forks.Replication Restart in Bacteria.The inactivation of rfaP, rarA or sspA gene improves the viability of the Escherichia coli DNA polymerase III holD mutant.Interaction of branch migration translocases with the Holliday junction-resolving enzyme and their implications in Holliday junction resolution.Structure and Function of a Novel ATPase that Interacts with Holliday Junction Resolvase Hjc and Promotes Branch Migration.RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases.UvrD and UvrD252 counteract RecQ, RecJ, and RecFOR in a rep mutant of Escherichia coli.Expansion of CAG repeats in Escherichia coli is controlled by single-strand DNA exonucleases of both polarities.Plasmodium falciparum RuvB proteins: Emerging importance and expectations beyond cell cycle progression.Formation of a stable RuvA protein double tetramer is required for efficient branch migration in vitro and for replication fork reversal in vivo.ruvA and ruvB mutants specifically impaired for replication fork reversal.The structure-specific endonuclease Mus81 contributes to replication restart by generating double-strand DNA breaks.Replication arrest is a major threat to growth at low temperature in Antarctic Pseudomonas syringae Lz4W.Replication fork reversal occurs spontaneously after digestion but is constrained in supercoiled domains.The DinG protein from Escherichia coli is a structure-specific helicase.Replication Fork Breakage and Restart in Escherichia coli

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P2860

RuvAB is essential for replication forks reversal in certain replication mutants.

http://www.wikidata.org/entity/Q34410893

description

2006 nî lūn-bûn

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2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

RuvAB is essential for replication forks reversal in certain replication mutants.

@ast

RuvAB is essential for replication forks reversal in certain replication mutants.

@en

RuvAB is essential for replication forks reversal in certain replication mutants.

@nl

type

label

RuvAB is essential for replication forks reversal in certain replication mutants.

@ast

RuvAB is essential for replication forks reversal in certain replication mutants.

@en

RuvAB is essential for replication forks reversal in certain replication mutants.

@nl

prefLabel

RuvAB is essential for replication forks reversal in certain replication mutants.

@ast

RuvAB is essential for replication forks reversal in certain replication mutants.

@en

RuvAB is essential for replication forks reversal in certain replication mutants.

@nl

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SJ.EMBOJ.7600941

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The EMBO Journal

P1476

RuvAB is essential for replication forks reversal in certain replication mutants

@en

P2093

Bénédicte Michel

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Maria-Jose Flores

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Mirjana Petranovic

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P2860

Comparative and evolutionary analysis of the bacterial homologous recombination systems

RAD51C is required for Holliday junction processing in mammalian cells

The structure of Escherichia coli RusA endonuclease reveals a new Holliday junction DNA binding fold

Functional overlap between Sgs1-Top3 and the Mms4-Mus81 endonuclease

Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects

Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis

Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda

Role of PriA in replication fork reactivation in Escherichia coli.

Replication fork arrest and DNA recombination.

PriA and phage T4 gp59: factors that promote DNA replication on forked DNA substrates microreview.

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596-604

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16424908

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