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MutS mediates heteroduplex loop formation by a translocation mechanism

MutS mediates heteroduplex loop formation by a translocation mechanism

http://www.wikidata.org/entity/Q33887145

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hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA.Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle)hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci Mismatch repair proteins collaborate with methyltransferases in the repair of O(6)-methylguanine N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex Real-time observation of DNA looping dynamics of Type IIE restriction enzymes NaeI and NarI.Single-molecule views of MutS on mismatched DNA.New insights and challenges in mismatch repair: getting over the chromatin hurdle The alternating ATPase domains of MutS control DNA mismatch repair Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS The C-Terminal Domain of the MutL Homolog from Neisseria gonorrhoeae Forms an Inverted Homodimer Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition.Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination.New insights into the mechanism of DNA mismatch repair Identification of mismatch repair protein complexes in HeLa nuclear extracts and their interaction with heteroduplex DNA DNA mismatch repair and mutation avoidance pathways Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches Nucleotides and heteroduplex DNA preserve the active conformation of Pseudomonas aeruginosa MutS by preventing protein oligomerization The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism Mechanism of MutS searching for DNA mismatches and signaling repair Many ways to loop DNA.Dissecting protein-induced DNA looping dynamics in real time.Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6.Single-molecule imaging reveals target-search mechanisms during DNA mismatch repair.Mismatch repair inhibits homeologous recombination via coordinated directional unwinding of trapped DNA structures Oligomerization of a MutS mismatch repair protein from Thermus aquaticus.Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD.Transient mismatch repair gene transfection for functional analysis of genetic hMLH1 and hMSH2 variants.Regulation of replication protein A functions in DNA mismatch repair by phosphorylation.Interaction of MutS and Vsr: some dominant-negative mutS mutations that disable methyladenine-directed mismatch repair are active in very-short-patch repair.A 'Semi-Protected Oligonucleotide Recombination' Assay for DNA Mismatch Repair in vivo Suggests Different Modes of Repair for Lagging Strand Mismatches.Nuclear reorganization of DNA mismatch repair proteins in response to DNA damage.

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MutS mediates heteroduplex loop formation by a translocation mechanism

http://www.wikidata.org/entity/Q33887145

description

1997 nî lūn-bûn

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1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի հուլիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年學術文章

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name

MutS mediates heteroduplex loop formation by a translocation mechanism

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MutS mediates heteroduplex loop formation by a translocation mechanism

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label

MutS mediates heteroduplex loop formation by a translocation mechanism

@ast

MutS mediates heteroduplex loop formation by a translocation mechanism

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prefLabel

MutS mediates heteroduplex loop formation by a translocation mechanism

@ast

MutS mediates heteroduplex loop formation by a translocation mechanism

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The EMBO Journal

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MutS mediates heteroduplex loop formation by a translocation mechanism

@en

P2093

A Makhov

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

D J Allen

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

J D Griffith

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

J Taylor

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

M Grilley

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

P Modrich

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

R Thresher

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

P2860

Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs

Human strand-specific mismatch repair occurs by a bidirectional mechanism similar to that of the bacterial reaction

Mismatch repair in replication fidelity, genetic recombination, and cancer biology

GATC sequence and mismatch repair in Escherichia coli.

Effects of high levels of DNA adenine methylation on methyl-directed mismatch repair in Escherichia coli.

Requirement for d(GATC) sequences in Escherichia coli mutHLS mismatch correction

DNA mismatch correction in a defined system.

Dominant negative mutator mutations in the mutS gene of Escherichia coli

The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structures

Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities.

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4467-4476

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scholarly article

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10.1093/EMBOJ/16.14.4467

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14

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16

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1997-07-01T00:00:00Z

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13968826

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P698

9250691

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P932

1170073

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