Novel dominant mutations in Saccharomyces cerevisiae MSH6.
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ATR kinase activation mediated by MutSalpha and MutLalpha in response to cytotoxic O6-methylguanine adductsFunctional studies and homology modeling of Msh2-Msh3 predict that mispair recognition involves DNA bending and strand separationInteraction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complexDNA mismatch repair: molecular mechanism, cancer, and ageingCadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complexSaccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairsexo1-Dependent mutator mutations: model system for studying functional interactions in mismatch repair.DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiaeA conserved MutS homolog connector domain interface interacts with MutL homologs.Reconstitution of Saccharomyces cerevisiae DNA polymerase ε-dependent mismatch repair with purified proteins.Functional analysis of human mismatch repair gene mutations identifies weak alleles and polymorphisms capable of polygenic interactions.Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein.Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.Polymorphisms of the human UDP-glucuronosyltransferase (UGT) 1A7 gene in colorectal cancer.Isolation and characterization of point mutations in mismatch repair genes that destabilize microsatellites in yeast.Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene.DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers.Hereditary ovarian carcinoma: heterogeneity, molecular genetics, pathology, and management.Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition.Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System.Low prevalence of germline hMSH6 mutations in colorectal cancer families from SpainBiochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D)Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.A personal historical view of DNA mismatch repair with an emphasis on eukaryotic DNA mismatch repair.Regulation of the human MSH6 gene by the Sp1 transcription factor and alteration of promoter activity and expression by polymorphisms.A saccharomyces cerevisiae RNase H2 interaction network functions to suppress genome instabilityMultiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I.Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP.Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6.The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition.Isolation and characterization of new proliferating cell nuclear antigen (POL30) mutator mutants that are defective in DNA mismatch repair.The MLH1 D132H variant is associated with susceptibility to sporadic colorectal cancer.
P2860
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P2860
Novel dominant mutations in Saccharomyces cerevisiae MSH6.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Novel dominant mutations in Saccharomyces cerevisiae MSH6.
@en
type
label
Novel dominant mutations in Saccharomyces cerevisiae MSH6.
@en
prefLabel
Novel dominant mutations in Saccharomyces cerevisiae MSH6.
@en
P2860
P356
P1433
P1476
Novel dominant mutations in Saccharomyces cerevisiae MSH6.
@en
P2093
Das Gupta R
Kolodner RD
P2860
P2888
P356
10.1038/71684
P407
P577
2000-01-01T00:00:00Z
P6179
1044262175