hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
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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 MLH1Multiple mutations and frameshifts are the hallmark of defective hPMS2 in pZ189-transfected human tumor cellsHuman exonuclease I is required for 5' and 3' mismatch repairDNA polymerase delta is required for human mismatch repair in vitroEvidence for involvement of HMGB1 protein in human DNA mismatch repairDifferential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sitesPhysical and functional interactions between Werner syndrome helicase and mismatch-repair initiation factorsThe interacting domains of three MutL heterodimers in man: hMLH1 interacts with 36 homologous amino acid residues within hMLH3, hPMS1 and hPMS2hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication fociMechanism of mismatch recognition revealed by human MutSĪ² bound to unpaired DNA loopsFunctional studies and homology modeling of Msh2-Msh3 predict that mispair recognition involves DNA bending and strand separationMismatch repair deficiency associated with overexpression of the MSH3 geneRole of APC and DNA mismatch repair genes in the development of colorectal cancers.Activation of the DNA Damage Response by RNA VirusesDNA triplet repeat expansion and mismatch repairCausal link between microsatellite instability and hMRE11 dysfunction in human cancersFunctional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.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 repairexo1-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.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 agentsExonuclease 1-dependent and independent mismatch repairCharacterization of the interactome of the human MutL homologues MLH1, PMS1, and PMS2Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activitiesThe Eukaryotic Mismatch Recognition Complexes Track with the Replisome during DNA SynthesisElevated mutant frequencies and predominance of G:C to A:T transition mutations in Msh6(-/-) small intestinal epitheliumThe role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switchPartial reconstitution of human DNA mismatch repair in vitro: characterization of the role of human replication protein ADHFR/MSH3 amplification in methotrexate-resistant cells alters the hMutSalpha/hMutSbeta ratio and reduces the efficiency of base-base mismatch repairIsolation of MutSbeta from human cells and comparison of the mismatch repair specificities of MutSbeta and MutSalphaGenetic Instability Caused by Loss of MutS Homologue 3 in Human Colorectal CancerRole of DNA mismatch repair and p53 in signaling induction of apoptosis by alkylating agents.Oligomerization of a MutS mismatch repair protein from Thermus aquaticus.Mismatch Repair proteins are recruited to replicating DNA through interaction with Proliferating Cell Nuclear Antigen (PCNA)Mutation rates of TGFBR2 and ACVR2 coding microsatellites in human cells with defective DNA mismatch repair.
P2860
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P2860
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
description
1996 Õ©ÕøÖÕ”ÕÆÕ”Õ¶Õ« ÕÕ„ÕŗÕæÕ„Õ“Õ¢Õ„ÖÕ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕøÖÕ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ ÕµÖ
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@hyw
1996 Õ©Õ¾Õ”ÕÆÕ”Õ¶Õ« Õ½Õ„ÕŗÕæÕ„Õ“Õ¢Õ„ÖÕ«Õ¶ Õ°ÖÕ”ÕæÕ”ÖÕ”ÕÆÕ¾Õ”Õ® Õ£Õ«ÕæÕ”ÕÆÕ”Õ¶ Õ°ÕøÕ¤Õ¾Õ”Õ®
@hy
artĆculu cientĆficu espublizĆ”u en 1996
@ast
im September 1996 verƶffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedeckĆ½ ÄlĆ”nok (publikovanĆ½ 1996/09/01)
@sk
vÄdeckĆ½ ÄlĆ”nek publikovanĆ½ v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/09/01)
@nl
Š½Š°ŃŠŗŠ¾Š²Š° ŃŃŠ°ŃŃŃ, Š¾ŠæŃŠ±Š»ŃŠŗŠ¾Š²Š°Š½Š° Ń Š²ŠµŃŠµŃŠ½Ń 1996
@uk
Ł
ŁŲ§ŁŲ© Ų¹ŁŁ
ŁŲ© (ŁŲ“Ų±ŲŖ ŁŁ Ų³ŲØŲŖŁ
ŲØŲ± 1996)
@ar
name
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@ast
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@en
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@nl
type
label
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@ast
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@en
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@nl
prefLabel
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@ast
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@en
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@nl
P2093
P1433
P1476
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
@en
P2093
E. Nakajima
I. Iaccarino
J. Jiricny
M. Ikejima
T. Shimada
P304
1181ā1184
P356
10.1016/S0960-9822(02)70685-4
P407
P577
1996-09-01T00:00:00Z