Presteady-state analysis of a single catalytic turnover by Escherichia coli uracil-DNA glycosylase reveals a "pinch-pull-push" mechanism.
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Base flipping in tn10 transposition: an active flip and capture mechanismKinetics of substrate recognition and cleavage by human 8-oxoguanine-DNA glycosylaseAccessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repairCrystal structure and functional insights into uracil-DNA glycosylase inhibition by phage 29 DNA mimic protein p56Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminal domainDissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylaseUracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognitionMutational analysis of arginine 276 in the leucine-loop of human uracil-DNA glycosylase.Mutations at Arginine 276 transform human uracil-DNA glycosylase into a single-stranded DNA-specific uracil-DNA glycosylase.Substitution of active site tyrosines with tryptophan alters the free energy for nucleotide flipping by human alkyladenine DNA glycosylase.Mechanistic insights into editing-site specificity of ADARs.Uncoupling of nucleotide flipping and DNA bending by the t4 pyrimidine dimer DNA glycosylase.Steady-state, pre-steady-state, and single-turnover kinetic measurement for DNA glycosylase activity.Detection of damaged DNA bases by DNA glycosylase enzymes.Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.Conformational Dynamics of DNA Repair by Escherichia coli Endonuclease IIINucleotide flipping by restriction enzymes analyzed by 2-aminopurine steady-state fluorescence.Structural evidence of a passive base-flipping mechanism for beta-glucosyltransferase.Pre-steady-state kinetics shows differences in processing of various DNA lesions by Escherichia coli formamidopyrimidine-DNA glycosylase.A dimeric mechanism for contextual target recognition by MutY glycosylase.Crystal structure of mimivirus uracil-DNA glycosylase.Catalytic mechanism of Escherichia coli endonuclease VIII: roles of the intercalation loop and the zinc fingerEnzymatic excision of uracil residues in nucleosomes depends on the local DNA structure and dynamics.Kinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by human alkyladenine DNA glycosylase.Mechanisms of base selection by the Escherichia coli mispaired uracil glycosylase.Observing an induced-fit mechanism during sequence-specific DNA methylation.Base-flipping dynamics in a DNA hairpin processing reaction.A rapid reaction analysis of uracil DNA glycosylase indicates an active mechanism of base flippingDynamics of RNA modification by a multi-site-specific tRNA methyltransferase.The coupling of tight DNA binding and base flipping: identification of a conserved structural motif in base flipping enzymes.A structurally conserved motif in γ-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping.
P2860
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P2860
Presteady-state analysis of a single catalytic turnover by Escherichia coli uracil-DNA glycosylase reveals a "pinch-pull-push" mechanism.
description
2002 nî lūn-bûn
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name
Presteady-state analysis of a ...... a "pinch-pull-push" mechanism.
@en
type
label
Presteady-state analysis of a ...... a "pinch-pull-push" mechanism.
@en
prefLabel
Presteady-state analysis of a ...... a "pinch-pull-push" mechanism.
@en
P2093
P2860
P356
P1476
Presteady-state analysis of a ...... a "pinch-pull-push" mechanism.
@en
P2093
Amy J Lundquist
Andrew S Bernards
Dale W Mosbaugh
Isaac Wong
P2860
P304
19424-19432
P356
10.1074/JBC.M201198200
P407
P577
2002-03-20T00:00:00Z