Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
about
Refining the role of PMS2 in Lynch syndrome: germline mutational analysis improved by comprehensive assessment of variantsDNA triplet repeat expansion and mismatch repairStructure of the endonuclease domain of MutL: unlicensed to cut.Postreplicative mismatch repair.DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiaeChemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.A conserved MutS homolog connector domain interface interacts with MutL homologs.MutLalpha and proliferating cell nuclear antigen share binding sites on MutSbeta.C-terminal fluorescent labeling impairs functionality of DNA mismatch repair proteins.A novel and rapid method of determining the effect of unclassified MLH1 genetic variants on differential allelic expressionDNA methyltransferases, DNA damage repair, and cancerChimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins.The sliding clamp tethers the endonuclease domain of MutL to DNACharacterization of a highly conserved binding site of Mlh1 required for exonuclease I-dependent mismatch repair.Elucidating the clinical significance of two PMS2 missense variants coexisting in a family fulfilling hereditary cancer criteria.Functional testing strategy for coding genetic variants of unclear significance in MLH1 in Lynch syndrome diagnosis.Determining the functional significance of mismatch repair gene missense variants using biochemical and cellular assays.Rapid generation of rice mutants via the dominant negative suppression of the mismatch repair protein OsPMS1.Identification of Lynch syndrome mutations in the MLH1-PMS2 interface that disturb dimerization and mismatch repair.Evaluation of the MLH1 I219V alteration in DNA mismatch repair activity and ulcerative colitis.Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNAMissense variants in hMLH1 identified in patients from the German HNPCC consortium and functional studies.Comprehensive functional assessment of MLH1 variants of unknown significance.Trapping and visualizing intermediate steps in the mismatch repair pathway in vivo.The MLH1 ATPase domain is needed for suppressing aberrant formation of interstitial telomeric sequences.
P2860
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P2860
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
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2006 nî lūn-bûn
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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@ast
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@en
type
label
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@ast
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@en
prefLabel
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@ast
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@en
P2093
P2860
P50
P356
P1476
Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.
@en
P2093
Christoph Welsch
Guido Plotz
Jochen Raedle
Luis Giron-Monzon
Mario Albrecht
Peter Friedhoff
Ricardo M Biondi
P2860
P304
P356
10.1093/NAR/GKL944
P407
P577
2006-11-28T00:00:00Z