Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP.
about
Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sitesInteraction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complexThe alternating ATPase domains of MutS control DNA mismatch repairSaccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairsNew insights into the mechanism of DNA mismatch repairSaccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.Eukaryotic Mismatch Repair in Relation to DNA ReplicationProbing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.Both hMutSα and hMutSß DNA mismatch repair complexes participate in 5-fluorouracil cytotoxicity.Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene.Mismatch repair during homologous and homeologous recombinationActivation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System.Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D)MutL traps MutS at a DNA mismatch.Mismatch repairEngineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.Interplay of DNA repair pathways controls methylation damage toxicity in Saccharomyces cerevisiaeDNA mismatch repair (MMR)-dependent 5-fluorouracil cytotoxicity and the potential for new therapeutic targets.Pathological assessment of mismatch repair gene variants in Lynch syndrome: past, present, and future.Modern aspects of the structural and functional organization of the DNA mismatch repair system.Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system.Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA.ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates.Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair.Genetic analyses of a hybrid cross between serotypes A and D strains of the human pathogenic fungus Cryptococcus neoformans.Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA.Differential and simultaneous adenosine di- and triphosphate binding by MutS.
P2860
Q24337694-C218A947-E451-4C05-B169-A833437F94E0Q24629057-6129A319-715D-4F42-BC54-8C11C6C8320FQ27640375-E9CE6064-CB4F-4F71-A5D2-67CB0E87D93DQ27931230-9F52F797-79E2-4D7B-A74C-7B1702237BF1Q28084645-F5AA23C8-516C-4308-BECB-56F29DCE8645Q33640393-5F97A610-FB29-463F-A3B2-A7B50308D10EQ33711830-B56A7E1E-36CC-4D03-88C9-20EF15DC2F10Q33800274-87707FBF-63F8-4EF2-91C4-5AADDAF8F958Q34099011-930E8966-FCAD-4996-BB8A-25BEA0CE139AQ34270970-5ECA86C5-78FA-4E39-A522-BD5D9B8AD63EQ35164333-B12CEF28-DD76-45AB-8A2B-2E57CCF19CC4Q35690218-03FE82D9-AB31-4961-A87A-5D1365ECF3F9Q35880032-8D4C654D-AD2D-4273-9F45-F5393D24F414Q36055693-B046F560-1D5F-498A-BDD7-E01F19AAF0BEQ36283640-FBC9737B-171F-4471-9302-08ADB1F75843Q36436073-691DEF61-831F-4CE5-8C13-60D38C19DB93Q36836991-6F5FF3D7-43DF-4718-9201-FCF8582CF789Q37602208-977BD97C-85B1-4D9C-B131-BAD9F29157FCQ38029584-5BBBA806-3C4D-46C2-ABA9-9376A19EF9D6Q38168515-DD638CF2-F7CB-4CC9-A207-00D739B2DE66Q38328409-6BF719AC-CFB6-4DC1-95B3-96CC602EAA94Q39656345-91DA388B-8AEB-44B1-B7EF-B3170D4EB08DQ40762229-B7EB034D-3E9A-4F3D-9485-53DBAB07604CQ40823475-3D33D6E5-4173-453D-8028-7E00E060D592Q41811704-5141FBB2-7BBE-40D5-94BB-6431BFE3F7AAQ44219222-1288432A-4921-442B-B0E5-355756FC88BBQ44353892-4CEE73EB-B445-445A-A446-DEBC8D954D9D
P2860
Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Dominant Saccharomyces cerevis ...... 2-Msh6 in the presence of ATP.
@en
type
label
Dominant Saccharomyces cerevis ...... 2-Msh6 in the presence of ATP.
@en
prefLabel
Dominant Saccharomyces cerevis ...... 2-Msh6 in the presence of ATP.
@en
P2093
P2860
P356
P1476
Dominant Saccharomyces cerevis ...... 2-Msh6 in the presence of ATP.
@en
P2093
Martin T Hess
Richard D Kolodner
Ruchira Das Gupta
P2860
P304
25545-25553
P356
10.1074/JBC.M202282200
P407
P577
2002-05-01T00:00:00Z