Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.
about
High-Resolution X-Ray Structure of the Trimeric Scar/WAVE-Complex Precursor Brk1Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.Postreplicative mismatch repair.New insights into the mechanism of DNA mismatch repairExonuclease 1-dependent and independent mismatch repairLarge conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein.Easy DNA modeling and more with GraphiteLifeExplorer.Analysis of the interaction interfaces of the N-terminal domain from Pseudomonas aeruginosa MutLIs thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system?Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.Base-flipping mechanism in postmismatch recognition by MutS.Atomic force microscopy captures the initiation of methyl-directed DNA mismatch repair.The sliding clamp tethers the endonuclease domain of MutL to DNAEngineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.DNA conformations in mismatch repair probed in solution by X-ray scattering from gold nanocrystals.ATP alters the diffusion mechanics of MutS on mismatched DNA.Modern aspects of the structural and functional organization of the DNA mismatch repair system.Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.Slow conformational changes in MutS and DNA direct ordered transitions between mismatch search, recognition and signaling of DNA repair.Trapping and visualizing intermediate steps in the mismatch repair pathway in vivo.MutS stimulates the endonuclease activity of MutL in an ATP-hydrolysis-dependent manner.The MLH1 ATPase domain is needed for suppressing aberrant formation of interstitial telomeric sequences.
P2860
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P2860
Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.
description
2011 nî lūn-bûn
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2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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name
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@ast
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@en
type
label
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@ast
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@en
prefLabel
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@ast
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@en
P2093
P2860
P356
P1476
Chemical trapping of the dynam ...... ch repair in Escherichia coli.
@en
P2093
Andreas D Marx
Annet Reumer
Damien Lariviere
Ines Winkler
Michele Cristovao
Peter Friedhoff
Roger J Heinze
Titia K Sixma
P2860
P304
17326-17337
P356
10.1074/JBC.M110.187641
P407
P50
P577
2011-03-15T00:00:00Z