Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
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Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer.MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1Elevated levels of mutation in multiple tissues of mice deficient in the DNA mismatch repair gene Pms2HNPCC mutations in the human DNA mismatch repair gene hMLH1 influence assembly of hMutLalpha and hMLH1-hEXO1 complexesHuman exonuclease I is required for 5' and 3' mismatch repairMSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylationDNA polymerase delta is required for human mismatch repair in vitroCharacterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cellsEvidence for involvement of HMGB1 protein in human DNA mismatch repairhMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sitesThe histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSĪ±Association of hereditary nonpolyposis colorectal cancer-related tumors displaying low microsatellite instability with MSH6 germline mutations.hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication fociDNA mismatch repair: molecular mechanism, cancer, and ageingThe MutSalpha-proliferating cell nuclear antigen interaction in human DNA mismatch repairMismatch repair deficiency associated with overexpression of the MSH3 geneRecognition and binding of mismatch repair proteins at an oncogenic hot spotHuman AP endonuclease suppresses DNA mismatch repair activity leading to microsatellite instability.Lack of MSH2 involvement differentiates V(D)J recombination from other non-homologous end joining eventsPCNA-MutSalpha-mediated binding of MutLalpha to replicative DNA with mismatched bases to induce apoptosis in human cellsActivation of the DNA Damage Response by RNA VirusesDNA triplet repeat expansion and mismatch repairFunctional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs.Conserved properties between functionally distinct MutS homologs in yeastGenetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repairA mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition.'Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday junctions and facilitates their cleavage by phage resolution enzymes.The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations.exo1-Dependent mutator mutations: model system for studying functional interactions in mismatch repair.Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination.Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair.ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes.Identification of mismatch repair protein complexes in HeLa nuclear extracts and their interaction with heteroduplex DNANuclear translocation of mismatch repair proteins MSH2 and MSH6 as a response of cells to alkylating agentsRepair of double-strand breaks by homologous recombination in mismatch repair-defective mammalian cellsDNA mismatch repair and mutation avoidance pathwaysAdenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1
P2860
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P2860
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
description
1995 nĆ® lÅ«n-bĆ»n
@nan
1995 Õ©ÕøÖÕ”ÕÆÕ”Õ¶Õ« Õ
ÕøÖÕ¶Õ«Õ½Õ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕøÖÕ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ ÕµÖ
Õ¤ÕøÖÕ”Õ®
@hyw
1995 Õ©Õ¾Õ”ÕÆÕ”Õ¶Õ« Õ°ÕøÖÕ¶Õ«Õ½Õ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕ¾Õ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ Õ°ÕøÕ¤Õ¾Õ”Õ®
@hy
1995幓ć®č«ę
@ja
1995幓č«ę
@yue
1995幓č«ę
@zh-hant
1995幓č«ę
@zh-hk
1995幓č«ę
@zh-mo
1995幓č«ę
@zh-tw
1995幓č®ŗę
@wuu
name
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@ast
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@en
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@nl
type
label
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@ast
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@en
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@nl
prefLabel
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@ast
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@en
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@nl
P2093
P3181
P356
P1433
P1476
Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells
@en
P2093
P304
P3181
P356
10.1126/SCIENCE.7604264
P407
P577
1995-06-30T00:00:00Z