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The alternating ATPase domains of MutS control DNA mismatch repair

The alternating ATPase domains of MutS control DNA mismatch repair

http://www.wikidata.org/entity/Q27640375

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hMSH4-hMSH5 adenosine nucleotide processing and interactions with homologous recombination machinery Single-molecule views of MutS on mismatched DNA.Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.Postreplicative mismatch repair.Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.DNA mismatch repair in eukaryotes and bacteria Mechanism of MutS searching for DNA mismatches and signaling repair Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.The nucleotide binding dynamics of human MSH2-MSH3 are lesion dependent G-quadruplex recognition activities of E. Coli MutS.MutS switches between two fundamentally distinct clamps during mismatch repair.Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes Cysteine accessibility probes timing and extent of NBD separation along the dimer interface in gating CFTR channels.Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.Mre11-Rad50 complex crystals suggest molecular calisthenics.Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.Base-flipping mechanism in postmismatch recognition by MutS.Hijacking of the mismatch repair system to cause CAG expansion and cell death in neurodegenerative disease.Deciphering the mismatch recognition cycle in MutS and MSH2-MSH6 using normal-mode analysis.Role of ATP binding and hydrolysis in the gating of the cystic fibrosis transmembrane conductance regulator Mismatch repair Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein.DNA mismatch repair system. Classical and fresh roles.Structure and function of ABC transporters.Conformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activity DNA repair pathways in trypanosomatids: from DNA repair to drug resistance.ATP alters the diffusion mechanics of MutS on mismatched DNA.Structure of ABC transporters.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.Dual role of MutS glutamate 38 in DNA mismatch discrimination and in the authorization of repair.Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair.Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA.(CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition.The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response Hydrolytically deficient MutS E694A is defective in the MutL-dependent activation of MutH and in the mismatch-dependent assembly of the MutS.MutL.heteroduplex complex.Cadmium inhibits the functions of eukaryotic MutS complexes.

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The alternating ATPase domains of MutS control DNA mismatch repair

http://www.wikidata.org/entity/Q27640375

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

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2003年学术文章

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2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

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name

The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

@ast

The alternating ATPase domains of MutS control DNA mismatch repair

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The alternating ATPase domains of MutS control DNA mismatch repair

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The EMBO Journal

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The alternating ATPase domains of MutS control DNA mismatch repair

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P2093

Herrie H K Winterwerp

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

Meindert H Lamers

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

Titia K Sixma

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

P2860

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

A phylogenomic study of the MutS family of proteins

Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis

The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

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

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746-756

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scholarly article

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10.1093/EMBOJ/CDG064

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3

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22

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2003-02-01T00:00:00Z

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8427716

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12554674

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140748

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