| scholarly article | Q13442814 |
| P2093 | author name string | Manju M Hingorani | |
| P2860 | cites work | PCNA function in the activation and strand direction of MutLα endonuclease in mismatch repair | Q24606670 |
| Mechanism of mismatch recognition revealed by human MutSβ bound to unpaired DNA loops | Q24614021 | ||
| A tale of tails: insights into the coordination of 3' end processing during homologous recombination | Q24629623 | ||
| Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions | Q24815928 | ||
| The conserved molecular machinery in DNA mismatch repair enzyme structures | Q26770149 | ||
| Single-molecule views of MutS on mismatched DNA. | Q26999680 | ||
| Structure and dynamics of molecular networks: a novel paradigm of drug discovery: a comprehensive review | Q27008867 | ||
| Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair | Q27617873 | ||
| Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA | Q27627633 | ||
| The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch | Q27627644 | ||
| Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair | Q27629464 | ||
| Structure and function of the N-terminal 40 kDa fragment of human PMS2: a monomeric GHL ATPase | Q27635053 | ||
| The alternating ATPase domains of MutS control DNA mismatch repair | Q27640375 | ||
| Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair | Q27640487 | ||
| Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates | Q27641807 | ||
| Structure of the human MutSalpha DNA lesion recognition complex | Q27644980 | ||
| Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS | Q27659930 | ||
| Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation | Q27678892 | ||
| Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site | Q27684073 | ||
| Postreplicative mismatch repair | Q27690911 | ||
| Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis | Q27766073 | ||
| ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes | Q27939412 | ||
| New insights into the mechanism of DNA mismatch repair | Q28084645 | ||
| hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA | Q28138775 | ||
| DNA mismatch repair | Q28256190 | ||
| The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch | Q28258968 | ||
| Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling | Q28264548 | ||
| DNA mismatch repair: functions and mechanisms | Q28296096 | ||
| Mechanism of MutS searching for DNA mismatches and signaling repair | Q28756121 | ||
| Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6. | Q30496957 | ||
| Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli | Q30500132 | ||
| Single-molecule imaging reveals target-search mechanisms during DNA mismatch repair | Q30528236 | ||
| Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair | Q33640393 | ||
| Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha | Q33645614 | ||
| Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein | Q33786744 | ||
| Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry | Q33800274 | ||
| Repair of a mismatch is influenced by the base composition of the surrounding nucleotide sequence | Q33952892 | ||
| DNA mismatch repair and genetic instability | Q34090778 | ||
| Visualizing one-dimensional diffusion of eukaryotic DNA repair factors along a chromatin lattice | Q34193203 | ||
| The nucleotide binding dynamics of human MSH2-MSH3 are lesion dependent | Q34315757 | ||
| DNA bending and unbending by MutS govern mismatch recognition and specificity | Q34385782 | ||
| The Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA. | Q34657088 | ||
| MutS switches between two fundamentally distinct clamps during mismatch repair | Q34698570 | ||
| Single molecule studies of DNA mismatch repair | Q35027619 | ||
| Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS. | Q35246382 | ||
| Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS. | Q35259130 | ||
| Conformational trapping of mismatch recognition complex MSH2/MSH3 on repair-resistant DNA loops | Q35409526 | ||
| Hijacking of the mismatch repair system to cause CAG expansion and cell death in neurodegenerative disease | Q35547560 | ||
| Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6 | Q35562811 | ||
| Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D) | Q35880032 | ||
| Deciphering the mismatch recognition cycle in MutS and MSH2-MSH6 using normal-mode analysis | Q35885592 | ||
| MutL traps MutS at a DNA mismatch | Q36055693 | ||
| The unstructured linker arms of Mlh1-Pms1 are important for interactions with DNA during mismatch repair | Q36162012 | ||
| Lynch syndrome genes | Q36246487 | ||
| Visualization of eukaryotic DNA mismatch repair reveals distinct recognition and repair intermediates. | Q36338245 | ||
| Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein | Q36359452 | ||
| Antibody diversification caused by disrupted mismatch repair and promiscuous DNA polymerases | Q36540495 | ||
| Mismatch repair defects and Lynch syndrome: The role of the basic scientist in the battle against cancer | Q36540568 | ||
| Roles for mismatch repair family proteins in promoting meiotic crossing over | Q36540776 | ||
| Saccharomyces cerevisiae MutLalpha is a mismatch repair endonuclease | Q36549257 | ||
| Endonuclease activities of MutLα and its homologs in DNA mismatch repair | Q36764079 | ||
| The origin of allosteric functional modulation: multiple pre-existing pathways | Q37359180 | ||
| Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair | Q37592729 | ||
| ATP alters the diffusion mechanics of MutS on mismatched DNA. | Q37683114 | ||
| Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex | Q37691675 | ||
| Pathological assessment of mismatch repair gene variants in Lynch syndrome: past, present, and future | Q38029584 | ||
| Evolution of the methyl directed mismatch repair system in Escherichia coli. | Q38255035 | ||
| The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition | Q38295775 | ||
| Dual role of MutS glutamate 38 in DNA mismatch discrimination and in the authorization of repair. | Q38316881 | ||
| Detection of high-affinity and sliding clamp modes for MSH2-MSH6 by single-molecule unzipping force analysis | Q38317910 | ||
| Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA. | Q38320783 | ||
| Insights from a decade of biophysical studies on MutL: Roles in strand discrimination and mismatch removal. | Q38363291 | ||
| Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes | Q38739461 | ||
| Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair | Q39656168 | ||
| Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. | Q39656345 | ||
| Single-molecule FRET TACKLE reveals highly dynamic mismatched DNA-MutS complexes | Q40124687 | ||
| The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair | Q41860625 | ||
| Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNA | Q41884304 | ||
| Stoichiometry of MutS and MutL at unrepaired mismatches in vivo suggests a mechanism of repair | Q42160273 | ||
| MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA. | Q42409924 | ||
| Slow conformational changes in MutS and DNA direct ordered transitions between mismatch search, recognition and signaling of DNA repair | Q42929083 | ||
| Network approach for capturing ligand-induced subtle global changes in protein structures | Q43995947 | ||
| Differential and simultaneous adenosine di- and triphosphate binding by MutS. | Q44353892 | ||
| Mispair specificity of methyl-directed DNA mismatch correction in vitro | Q44909730 | ||
| ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes. | Q45009204 | ||
| DnaN clamp zones provide a platform for spatiotemporal coupling of mismatch detection to DNA replication. | Q45962906 | ||
| Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA. | Q46462569 | ||
| Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit | Q50335571 | ||
| Endonucleolytic function of MutLalpha in human mismatch repair | Q50335575 | ||
| Hereditary colorectal cancer | Q73088287 | ||
| Interaction of Escherichia coli MutS and MutL at a DNA mismatch | Q73923892 | ||
| A simple fluorescent method for detecting mismatched DNAs using a MutS-fluorophore conjugate | Q80023309 | ||
| Probing the allosteric mechanism in pyrrolysyl-tRNA synthetase using energy-weighted network formalism | Q84296675 | ||
| P921 | main subject | DNA mismatch repair | Q2984243 |
| P304 | page(s) | 24-31 | |
| P577 | publication date | 2015-12-02 | |
| P1433 | published in | DNA Repair | Q3894086 |
| P1476 | title | Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair | |
| P478 | volume | 38 |
| Q97423483 | A Novel Splice-Site Mutation in MSH2 Is Associated With the Development of Lynch Syndrome |
| Q92963099 | Bending of DNA duplexes with mutation motifs |
| Q57060631 | Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS |
| Q41216018 | DNA mutation motifs in the genes associated with inherited diseases. |
| Q36764079 | Endonuclease activities of MutLα and its homologs in DNA mismatch repair |
| Q33711830 | Eukaryotic Mismatch Repair in Relation to DNA Replication |
| Q30841579 | Evolutionary Covariance Combined with Molecular Dynamics Predicts a Framework for Allostery in the MutS DNA Mismatch Repair Protein |
| Q47356334 | Mechanism of formation of a toroid around DNA by the mismatch sensor protein. |
| Q93079487 | Mismatch Recognition by Saccharomyces cerevisiae Msh2-Msh6: Role of Structure and Dynamics |
| Q36540776 | Roles for mismatch repair family proteins in promoting meiotic crossing over |
| Q39237485 | Single-Molecule FRET to Measure Conformational Dynamics of DNA Mismatch Repair Proteins |
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