Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity - Wikidata - awgldk - TriplyDB

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

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Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein.Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.Base-flipping mechanism in postmismatch recognition by MutS.Screening of candidate genes for primary open angle glaucoma.Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication Pathways Applying 6-methylisoxanthopterin-enhanced fluorescence to examine protein-DNA interactions in the picomolar range Roles for mismatch repair family proteins in promoting meiotic crossing over.Recognition of damaged DNA: structure and dynamic markers.Differential mismatch recognition specificities of eukaryotic MutS homologs, MutSα and MutSβ.ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates.DNA bending propensity in the presence of base mismatches: implications for DNA repair.

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Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

http://www.wikidata.org/entity/Q37263650

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on June 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

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Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity.

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label

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

@en

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity.

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prefLabel

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

@en

Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity.

@nl

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J.BPJ.2009.04.012

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Biophysical Journal

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Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity

@en

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Michael Feig

http://www.w3.org/2001/XMLSchema#string

Shayantani Mukherjee

http://www.w3.org/2001/XMLSchema#string

P2860

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

The alternating ATPase domains of MutS control DNA mismatch repair

Structure of the human MutSalpha DNA lesion recognition complex

DNA mismatch repair

DNA mismatch repair: functions and mechanisms

Deciphering the mismatch recognition cycle in MutS and MSH2-MSH6 using normal-mode analysis.

Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein.

Mechanisms in eukaryotic mismatch repair.

The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.

Direct observation of three conformations of MutS protein regulated by adenine nucleotides.

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scholarly article

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10.1016/J.BPJ.2009.04.012

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