DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies.
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Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 HelicaseYeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNAKinetic model for the ATP-dependent translocation of Saccharomyces cerevisiae RSC along double-stranded DNA.Forward and reverse motion of single RecBCD molecules on DNA.Hexameric helicase deconstructed: interplay of conformational changes and substrate couplingKinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA.The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.Autoinhibition of Escherichia coli Rep monomer helicase activity by its 2B subdomain.PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps.General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwindingMechanism of nucleic acid unwinding by SARS-CoV helicase.Simultaneous binding to the tracking strand, displaced strand and the duplex of a DNA fork enhances unwinding by Dda helicaseSevere acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicaseDNA unwinding and protein displacement by superfamily 1 and superfamily 2 helicases.Interactions of the Escherichia coli DnaB-DnaC protein complex with nucleotide cofactors. 1. Allosteric conformational transitions of the complex.Unraveling helicase mechanisms one molecule at a timeTransient-State Kinetic Analysis of the RNA Polymerase I Nucleotide Incorporation Mechanism.Asymmetric regulation of bipolar single-stranded DNA translocation by the two motors within Escherichia coli RecBCD helicase.Fluorescence methods to study DNA translocation and unwinding kinetics by nucleic acid motors.Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD-DNA complexesKinetics of motor protein translocation on single-stranded DNA.E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation.Single-molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase.Insight into helicase mechanism and function revealed through single-molecule approaches.Influence of DNA end structure on the mechanism of initiation of DNA unwinding by the Escherichia coli RecBCD and RecBC helicases.Kinetics of DNA unwinding by the RecD2 helicase from Deinococcus radiodurans.Ensemble and single-molecule fluorescence-based assays to monitor DNA binding, translocation, and unwinding by iron-sulfur cluster containing helicases.A mechanistic study of helicases with magnetic traps.Structural and biochemical basis for the difference in the helicase activity of two different constructs of SARS-CoV helicase.Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities.Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexesThe primary and secondary translocase activities within E. coli RecBC helicase are tightly coupled to ATP hydrolysis by the RecB motorEscherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor.A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNAProcessive DNA Unwinding by RecBCD Helicase in the Absence of Canonical Motor Translocation.Structure and Mechanisms of SF1 DNA Helicases.Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase.Kinetic control of Mg2+-dependent melting of duplex DNA ends by Escherichia coli RecBC.The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity.
P2860
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P2860
DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@en
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@nl
type
label
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@en
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@nl
prefLabel
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@en
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@nl
P2093
P1476
DNA unwinding step-size of E. ...... quenched-flow kinetic studies.
@en
P2093
Aaron L Lucius
Alessandro Vindigni
Andrew F Taylor
Gerald R Smith
Janid A Ali
Razmic Gregorian
Timothy M Lohman
P304
P356
10.1016/S0022-2836(02)01067-7
P407
P577
2002-11-01T00:00:00Z