UvrD controls the access of recombination proteins to blocked replication forks
about
Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systemsComparative genomics and molecular dynamics of DNA repeats in eukaryotesMolecular traffic jams on DNAStructure and Biochemical Activities of Escherichia coli MgsARotations of the 2B Sub-domain of E. coli UvrD Helicase/Translocase Coupled to Nucleotide and DNA BindingThe C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forksFunctional characterization of UvrD helicases from Haemophilus influenzae and Helicobacter pyloriA major role of the RecFOR pathway in DNA double-strand-break repair through ESDSA in Deinococcus radioduransPcrA-mediated disruption of RecA nucleoprotein filaments--essential role of the ATPase activity of RecAruvA Mutants that resolve Holliday junctions but do not reverse replication forksEscherichia coli genes affecting recipient ability in plasmid conjugation: are there any?DNA flap creation by the RarA/MgsA protein of Escherichia coliLow efficiency of homology-facilitated illegitimate recombination during conjugation in Escherichia coli.Stalled replication fork repair and misrepair during thymineless death in Escherichia coli.PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps.Mechanism of nucleic acid unwinding by SARS-CoV helicase.Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicaseHelicase-inactivating mutations as a basis for dominant negative phenotypes.UvrD2 is essential in Mycobacterium tuberculosis, but its helicase activity is not required.CTXφ Replication Depends on the Histone-Like HU Protein and the UvrD HelicaseDirected Evolution of RecA Variants with Enhanced Capacity for Conjugational RecombinationResolving Holliday junctions with Escherichia coli UvrD helicaseImportant role for Mycobacterium tuberculosis UvrD1 in pathogenesis and persistence apart from its function in nucleotide excision repair.UvrD Participation in Nucleotide Excision Repair Is Required for the Recovery of DNA Synthesis following UV-Induced Damage in Escherichia coli.Replication-transcription conflicts in bacteria.DNA Metabolism in Balance: Rapid Loss of a RecA-Based Hyperrec PhenotypeCharacterization of the mycobacterial NER system reveals novel functions of the uvrD1 helicaseTolerance of Escherichia coli to fluoroquinolone antibiotics depends on specific components of the SOS response pathway.Suppression of constitutive SOS expression by recA4162 (I298V) and recA4164 (L126V) requires UvrD and RecX in Escherichia coli K-12.What happens when replication and transcription complexes collide?SOS, the formidable strategy of bacteria against aggressions.Comparative genomics of the DNA damage-inducible network in the Patescibacteria.The inactivation of rfaP, rarA or sspA gene improves the viability of the Escherichia coli DNA polymerase III holD mutant.Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.25 years on and no end in sight: a perspective on the role of RecG proteinActive displacement of RecA filaments by UvrD translocase activity.Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase.Promoting and avoiding recombination: contrasting activities of the Escherichia coli RuvABC Holliday junction resolvase and RecG DNA translocase.A RecB-like helicase in Helicobacter pylori is important for DNA repair and host colonization.RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases.
P2860
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P2860
UvrD controls the access of recombination proteins to blocked replication forks
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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name
UvrD controls the access of recombination proteins to blocked replication forks
@ast
UvrD controls the access of recombination proteins to blocked replication forks
@en
type
label
UvrD controls the access of recombination proteins to blocked replication forks
@ast
UvrD controls the access of recombination proteins to blocked replication forks
@en
prefLabel
UvrD controls the access of recombination proteins to blocked replication forks
@ast
UvrD controls the access of recombination proteins to blocked replication forks
@en
P2860
P356
P1433
P1476
UvrD controls the access of recombination proteins to blocked replication forks
@en
P2093
Bénédicte Michel
P2860
P304
P356
10.1038/SJ.EMBOJ.7601804
P407
P577
2007-07-19T00:00:00Z