Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA. - Wikidata - wikimedia - TriplyDB

Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA.

Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA.

http://www.wikidata.org/entity/Q38320783

about

Functional studies and homology modeling of Msh2-Msh3 predict that mispair recognition involves DNA bending and strand separation Interaction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complex DNA mismatch repair: molecular mechanism, cancer, and ageing Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex Human 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 events Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha.Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs Modulation of the DNA-binding activity of Saccharomyces cerevisiae MSH2-MSH6 complex by the high-mobility group protein NHP6A, in vitro DNA mismatch repair and mutation avoidance pathways Replicative DNA polymerase δ but not ε proofreads errors in Cis and in Trans Exonuclease 1-dependent and independent mismatch repair DNA replication fidelity and cancer The Saccharomyces cerevisiae Mlh1-Mlh3 heterodimer is an endonuclease that preferentially binds to Holliday junctions.Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiae Mismatch Repair proteins are recruited to replicating DNA through interaction with Proliferating Cell Nuclear Antigen (PCNA)Analysis of the DNA binding activity of BRCA1 and its modulation by the tumour suppressor p53.A conserved MutS homolog connector domain interface interacts with MutL homologs.Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.Vaccinia virus telomeres: interaction with the viral I1, I6, and K4 proteins Variation in efficiency of DNA mismatch repair at different sites in the yeast genome.Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.PMS2 endonuclease activity has distinct biological functions and is essential for genome maintenance.Both hMutSα and hMutSß DNA mismatch repair complexes participate in 5-fluorouracil cytotoxicity.Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene.The nucleotide binding dynamics of human MSH2-MSH3 are lesion dependent Differential correction of lagging-strand replication errors made by DNA polymerases {alpha} and {delta}Heterogeneous polymerase fidelity and mismatch repair bias genome variation and composition.Base composition of mononucleotide runs affects DNA polymerase slippage and removal of frameshift intermediates by mismatch repair in Saccharomyces cerevisiae Mismatch repair balances leading and lagging strand DNA replication fidelity.EXO1 and MSH6 are high-copy suppressors of conditional mutations in the MSH2 mismatch repair gene of Saccharomyces cerevisiae.Sequence composition and context effects on the generation and repair of frameshift intermediates in mononucleotide runs in Saccharomyces cerevisiae.Different roles of eukaryotic MutS and MutL complexes in repair of small insertion and deletion loops in yeast.Accumulation of recessive lethal mutations in Saccharomyces cerevisiae mlh1 mismatch repair mutants is not associated with gross chromosomal rearrangements.DNA mismatch repair: from structure to mechanism.Genome-wide survey of post-meiotic segregation during yeast recombination.Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System.Quantifying the contributions of base selectivity, proofreading and mismatch repair to nuclear DNA replication in Saccharomyces cerevisiae.

P2860

Q24619622-51B5062C-6F60-4422-8CD9-5CB32F68AA43 Q24629057-45DA485F-BB91-4C94-A8AB-6D9E3ECDB1FA Q24647002-D2E4A2CE-C7A8-4D2E-B207-85B2FB3B2562 Q24798955-74DA9082-B6EB-4D82-9B16-3EF845F2386E Q24812717-697345DD-CB8B-4824-9EAB-B15D15941607 Q24813835-56A149BB-6263-4656-9768-85CC3F124D63 Q27929951-559DA366-9D85-4AB4-A90C-1D088F0D3F46 Q27931230-4FEE80FF-FB16-4C11-8B0F-8A71172815AA Q27931842-7C7C0EE3-1F07-4B3D-B122-F09224429358 Q28211143-B8C882AE-E627-4262-87B4-C766F22EB2E4 Q28258327-73064819-ED58-4711-9F41-05DE4F7CFA8E Q28261787-9E1DF952-B2A6-4FFF-A899-0EC291E2C934 Q28295863-54B6A8B8-8D50-4A38-B414-20D72969EBF6 Q28306188-FD18F4EB-7186-445C-BE0A-6F1B6D8AB9A5 Q28359649-FCF5C225-4643-4A76-A6DC-E16C7B490FF0 Q28709604-E12B74F5-BD26-4DB3-A8E3-3E9709212BEE Q33305049-F1DECF83-D59F-4D72-8D98-4EC7D0B06798 Q33342762-78C1560F-0BC9-4BC4-9498-538D91D63A2E Q33552273-4600FC25-1266-4388-97D0-8B3473060092 Q33640393-2B19B959-942F-4415-949E-580234AA718A Q33800274-F9C7CFE7-546B-4FC4-8BBD-CFB854100019 Q33847472-E762EC79-4C53-4A0A-86FE-0C96EBFFAB60 Q33854065-03D70BF8-42C0-4666-B0FE-16FA97349976 Q33933718-DB3CD7A3-42B8-4400-A5DE-E3585858272D Q34068165-5AE23187-C9B6-4518-8A7A-A6CE03C4C605 Q34099011-85F29CCF-7824-4E2B-99C5-9D521AD303F3 Q34270970-E04E1DB0-D994-4CDB-95E9-9C019B190CA0 Q34315757-9ED8CB25-B61B-4DA6-8EE7-7E57D2213302 Q34396924-D05217F3-2325-40B9-89E4-AB9EF2DEE7CC Q34439328-62625068-0996-49A3-B0C2-D510EECC4EC9 Q34443496-CB117158-D4F6-449E-8C74-168C8812C015 Q34446700-25961316-3479-4907-92EF-D1A9D0F7AEC3 Q34609730-19C974FF-A8FE-4C58-89EF-E019DA5382DC Q34610604-17079372-DB61-4CEA-9E9C-99675EE8504B Q35034387-6D0CF9C9-FFF0-43F7-8642-CB882397634A Q35038676-9BBE0535-EFEA-4E2C-A191-9351F121179D Q35132526-A140AE8B-BE7E-4A8D-AD87-74E0C237D9FF Q35557763-C7D647E3-7399-4F06-8569-B7A93617919A Q35690218-CD1CC02C-2F80-4163-88FF-94D88CD2207A Q35734815-B937ABBD-7480-4287-BB06-97BD8F4D901D

P2860

Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA.

http://www.wikidata.org/entity/Q38320783

description

1999 nî lūn-bûn

@nan

1999年の論文

@ja

1999年学术文章

@wuu

1999年学术文章

@zh-cn

1999年学术文章

@zh-hans

1999年学术文章

@zh-my

1999年学术文章

@zh-sg

1999年學術文章

@yue

1999年學術文章

@zh

1999年學術文章

@zh-hant

name

Biochemical characterization o ...... ex and mispaired bases in DNA.

@en

type

label

Biochemical characterization o ...... ex and mispaired bases in DNA.

@en

prefLabel

Biochemical characterization o ...... ex and mispaired bases in DNA.

@en

P1433

Q38320783-D573CC17-9D27-4271-AC20-20EFB6F2B0A6

P1476

Q38320783-FBC8B2FA-B0F1-4557-8F21-F92328A426C8

P2093

Q38320783-1CA207CB-7D31-4633-B67B-CE79B7DDA2C4

Q38320783-30A4C2DF-CF9A-4DB8-A2A7-ACF52B4FF1CD

P2860

Q38320783-019B1EEF-A13E-4372-AB11-09D07EB3640A

Q38320783-0306C7CC-F353-4DFC-9949-652FC587D8CB

Q38320783-0484DE7B-02BF-491B-AB9B-141C298AAADA

Q38320783-0C47D22D-1B31-40FE-B422-2CD661186A7C

Q38320783-11CF0E6F-8787-4065-9162-E2E0B250A9C4

Q38320783-140DFAA7-A261-4BE2-9A36-474F4D809EEB

Q38320783-1B49BD5D-FF91-4551-BEF7-2E605C043344

Q38320783-1F8F427A-DAB1-4CDA-9DE2-63F019155F8B

Q38320783-2998B350-9A01-4339-8688-16BE009DE223

Q38320783-2A23D810-6797-4F5F-A1C5-FF74D69E8400

P304

Q38320783-2817A7BD-BDDB-4296-B5EB-BD76F36D4BE1

P31

Q38320783-04C34923-1D82-44D0-B410-C3B2ACFC45BB

P356

Q38320783-A51A2674-CDA6-487B-9CC3-FA19635FF501

P407

Q38320783-D3DCE0A3-CE61-45E3-AAD5-5FB7828B8B68

P433

Q38320783-B3A2C6BA-B44E-4954-B1E1-56E1B72A501D

P478

Q38320783-92A91DED-987A-4C30-9529-D28CC9960ABB

P577

Q38320783-AEFF8F40-B319-4C25-9018-04E9752C58B3

P5875

Q38320783-C65066B4-E707-4B45-A4F0-EAD98D4C7BAF

P698

Q38320783-9C7C0548-1828-41D3-AD64-EEA6CAC06739

P356

JBC.274.38.26668

P1433

Journal of Biological Chemistry

P1476

Biochemical characterization o ...... ex and mispaired bases in DNA.

@en

P2093

Kolodner RD

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

Marsischky GT

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

P2860

Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer.

Cloning and expression analysis of a meiosis-specific MutS homolog: the human MSH4 gene

Mutation of MSH3 in endometrial cancer and evidence for its functional role in heteroduplex repair

hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6

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 yeast

Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition.

Saccharomyces cerevisiae MSH2, a mispaired base recognition protein, also recognizes Holliday junctions in DNA.

Heteroduplex DNA correction in Saccharomyces cerevisiae is mismatch specific and requires functional PMS genes.

Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3.

P304

26668-26682

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

P31

scholarly article

P356

10.1074/JBC.274.38.26668

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

P407

P433

38

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

P478

274

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

P577

1999-09-01T00:00:00Z

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

P5875

238316250

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

P698

10480869

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