The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.
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DNA mismatch repair: molecular mechanism, cancer, and ageingMagnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutSLarge conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.Mechanism of MutS searching for DNA mismatches and signaling repairDynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6.Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein.Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair.Global analysis of ion dependence unveils hidden steps in DNA binding and bending by integration host factor.Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D)Deciphering the mismatch recognition cycle in MutS and MSH2-MSH6 using normal-mode analysis.Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.MutL traps MutS at a DNA mismatch.Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication PathwaysConformational change in MSH2-MSH6 upon binding DNA coupled to ATPase activityMismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair.Application of stopped-flow kinetics methods to investigate the mechanism of action of a DNA repair protein.Single-Molecule FRET to Measure Conformational Dynamics of DNA Mismatch Repair Proteins.Single-molecule FRET TACKLE reveals highly dynamic mismatched DNA-MutS complexes.Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNAMutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.The role of nucleotide cofactor binding in cooperativity and specificity of MutS recognition.Slow conformational changes in MutS and DNA direct ordered transitions between mismatch search, recognition and signaling of DNA repair.Interaction studies of muts and mutl with DNA containing the major cisplatin lesion and its mismatched counterpart under equilibrium and nonequilibrium conditions.DnaN clamp zones provide a platform for spatiotemporal coupling of mismatch detection to DNA replication.Visualizing correlated motion with HDBSCAN clustering.Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS
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P2860
The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair.
description
2006 nî lūn-bûn
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2006年の論文
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2006年論文
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2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
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2006年论文
@wuu
2006年论文
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2006年论文
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name
The effects of nucleotides on ...... e activity in mismatch repair.
@en
type
label
The effects of nucleotides on ...... e activity in mismatch repair.
@en
prefLabel
The effects of nucleotides on ...... e activity in mismatch repair.
@en
P2860
P1476
The effects of nucleotides on ...... e activity in mismatch repair.
@en
P2093
Emily Jacobs-Palmer
Manju M Hingorani
P2860
P304
P356
10.1016/J.JMB.2006.11.092
P407
P577
2006-12-06T00:00:00Z