The Escherichia coli RecQ helicase functions as a monomer.
about
Different quaternary structures of human RECQ1 are associated with its dual enzymatic activityStructural and functional analyses of disease-causing missense mutations in Bloom syndrome proteinThe RecQ DNA helicases in DNA repairAnalysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein ARecQ helicase translocates along single-stranded DNA with a moderate processivity and tight mechanochemical couplingActive and passive mechanisms of helicasesStructural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicaseCoupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: role of a highly conserved aromatic-rich sequenceSingle-molecule visualization of RecQ helicase reveals DNA melting, nucleation, and assembly are required for processive DNA unwinding.High-resolution structure of the E.coli RecQ helicase catalytic coreSingle-molecule assay reveals strand switching and enhanced processivity of UvrDMutual inhibition of RecQ molecules in DNA unwinding.Identification of a coiled coil in werner syndrome protein that facilitates multimerization and promotes exonuclease processivityJunction of RecQ helicase biochemistry and human disease.Mechanisms of helicases.Sit down, relax and unwind: structural insights into RecQ helicase mechanisms.DNA repair and replication fork helicases are differentially affected by alkyl phosphotriester lesion.Mycobacterium smegmatis RqlH defines a novel clade of bacterial RecQ-like DNA helicases with ATP-dependent 3'-5' translocase and duplex unwinding activitiesThe arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.Fine tuning of a DNA fork by the RecQ helicase.Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stabilityEvidence for a functional dimeric form of the PcrA helicase in DNA unwindingMechanistic insight into cadmium-induced inactivation of the Bloom protein.A nucleotide-dependent and HRDC domain-dependent structural transition in DNA-bound RecQ helicase.RecQ helicases: multiple structures for multiple functions?The DNA binding properties of the Escherichia coli RecQ helicase.Multiple Escherichia coli RecQ helicase monomers cooperate to unwind long DNA substrates: a fluorescence cross-correlation spectroscopy study.Biochemical and kinetic characterization of the DNA helicase and exonuclease activities of werner syndrome protein.3'-Terminated Overhangs Regulate DNA Double-Strand Break Processing in Escherichia coli.A prominent β-hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formation.The Werner syndrome protein binds replication fork and holliday junction DNAs as an oligomer.The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding.The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity.RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.Helicase Stepping Investigated with One-Nucleotide Resolution Fluorescence Resonance Energy Transfer.
P2860
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P2860
The Escherichia coli RecQ helicase functions as a monomer.
description
2003 nî lūn-bûn
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2003年の論文
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name
The Escherichia coli RecQ helicase functions as a monomer.
@en
The Escherichia coli RecQ helicase functions as a monomer.
@nl
type
label
The Escherichia coli RecQ helicase functions as a monomer.
@en
The Escherichia coli RecQ helicase functions as a monomer.
@nl
prefLabel
The Escherichia coli RecQ helicase functions as a monomer.
@en
The Escherichia coli RecQ helicase functions as a monomer.
@nl
P2093
P2860
P356
P1476
The Escherichia coli RecQ helicase functions as a monomer.
@en
P2093
Ai Hua Zhang
Christian Auclair
Eric Deprez
Hou Qiang Xu
Jean-Claude Brochon
Moncef M Ladjimi
Patrick Tauc
Xu Guang Xi
P2860
P304
34925-34933
P356
10.1074/JBC.M303581200
P407
P577
2003-06-12T00:00:00Z