| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M103148200 |
| P698 | PubMed publication ID | 11371566 |
| P2093 | author name string | C Du | |
| S Nayak | |||
| M J Schofield | |||
| P Hsieh | |||
| T H Scott | |||
| P2860 | cites work | 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 | ||
| Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn | Q27734267 | ||
| Superfamily of UvrA-related NTP-binding proteins. Implications for rational classification of recombination/repair systems | Q27932359 | ||
| Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex | Q27932428 | ||
| MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp | Q27935260 | ||
| Eukaryotic DNA mismatch repair | Q27939116 | ||
| ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes | Q27939412 | ||
| hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA | Q28138775 | ||
| The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch | Q28258968 | ||
| The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch | Q28610649 | ||
| ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair | Q28610858 | ||
| Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism | Q28610864 | ||
| Mismatch repair in replication fidelity, genetic recombination, and cancer biology | Q29616483 | ||
| Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysis | Q31852984 | ||
| A quantitative UV laser footprinting analysis of the interaction of IHF with specific binding sites: re-evaluation of the effective concentration of IHF in the cell. | Q31962481 | ||
| MutS mediates heteroduplex loop formation by a translocation mechanism | Q33887145 | ||
| Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases | Q33888460 | ||
| DNA mismatch repair and genetic instability | Q34090778 | ||
| The Escherichia coli MutL protein stimulates binding of Vsr and MutS to heteroduplex DNA. | Q34657088 | ||
| ATP hydrolysis-dependent formation of a dynamic ternary nucleoprotein complex with MutS and MutL. | Q34712687 | ||
| Dominant negative mutator mutations in the mutS gene of Escherichia coli | Q34726651 | ||
| The DNA binding properties of the MutL protein isolated from Escherichia coli | Q35919359 | ||
| ATP-hydrolysis-dependent conformational switch modulates the stability of MutS-mismatch complexes | Q38316177 | ||
| MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast | Q42427955 | ||
| Interaction of MutS protein with the major and minor grooves of a heteroduplex DNA. | Q54565774 | ||
| Dissection of the Sequence Specificity of the Holliday Junction Endonuclease CCE1† | Q63383891 | ||
| Modulation of MutS ATP hydrolysis by DNA cofactors | Q73543806 | ||
| The MutL ATPase is required for mismatch repair | Q73586223 | ||
| Eukaryotic mismatch repair: an update | Q77753605 | ||
| The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity | Q77765360 | ||
| P433 | issue | 30 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| P1104 | number of pages | 9 | |
| P304 | page(s) | 28291-28299 | |
| P577 | publication date | 2001-05-22 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Interaction of Escherichia coli MutS and MutL at a DNA mismatch | |
| P478 | volume | 276 |
| Q40762229 | ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates |
| Q33506407 | Adenosine triphosphate stimulates Aquifex aeolicus MutL endonuclease activity |
| Q24300627 | Analysis of the human MutLalpha.MutSalpha complex |
| Q39656345 | Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. |
| Q38295596 | Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. |
| Q38254948 | Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair. |
| Q36597002 | Beta clamp directs localization of mismatch repair in Bacillus subtilis |
| Q36359452 | Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein |
| Q40744193 | Contribution of human mlh1 and pms2 ATPase activities to DNA mismatch repair |
| Q35928818 | Coupling distant sites in DNA during DNA mismatch repair. |
| Q36884849 | DNA Mismatch Repair Interacts with CAF-1- and ASF1A-H3-H4-dependent Histone (H3-H4)2 Tetramer Deposition |
| Q34385782 | DNA bending and unbending by MutS govern mismatch recognition and specificity |
| Q37256043 | DNA conformations in mismatch repair probed in solution by X-ray scattering from gold nanocrystals. |
| Q24647002 | DNA mismatch repair: molecular mechanism, cancer, and ageing |
| Q24815928 | Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions |
| Q44353892 | Differential and simultaneous adenosine di- and triphosphate binding by MutS. |
| Q75223553 | Direct IBD mapping: identical-by-descent mapping without genotyping |
| Q27679146 | Distinct Structural Alterations in Proliferating Cell Nuclear Antigen Block DNA Mismatch Repair |
| Q45962906 | DnaN clamp zones provide a platform for spatiotemporal coupling of mismatch detection to DNA replication. |
| Q38289639 | Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP. |
| Q37210972 | Dual daughter strand incision is processive and increases the efficiency of DNA mismatch repair |
| Q34545259 | Easy DNA modeling and more with GraphiteLifeExplorer |
| Q30499557 | Electrochemical detection of mismatched DNA using a MutS probe |
| Q34425450 | Functional interactions and signaling properties of mammalian DNA mismatch repair proteins |
| Q33343475 | Human MutLalpha: the jack of all trades in MMR is also an endonuclease |
| Q33224078 | Human mismatch repair: reconstitution of a nick-directed bidirectional reaction |
| Q44594090 | Hydrolytically Deficient MutS E694A Is Defective in the MutL-dependent Activation of MutH and in the Mismatch-dependent Assembly of the MutS · MutL · Heteroduplex Complex |
| Q33246717 | Identifying an interaction site between MutH and the C-terminal domain of MutL by crosslinking, affinity purification, chemical coding and mass spectrometry |
| Q28756121 | Mechanism of MutS searching for DNA mismatches and signaling repair |
| Q38254881 | Mismatch binding, ADP-ATP exchange and intramolecular signaling during mismatch repair |
| Q39656168 | Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair |
| Q34660590 | Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork |
| Q44447213 | Mismatch repair in human nuclear extracts: effects of internal DNA-hairpin structures between mismatches and excision-initiation nicks on mismatch correction and mismatch-provoked excision |
| Q38168515 | Modern aspects of the structural and functional organization of the DNA mismatch repair system |
| Q44522189 | Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair |
| Q36055693 | MutL traps MutS at a DNA mismatch |
| Q83322974 | MutL-catalyzed ATP hydrolysis is required at a post-UvrD loading step in methyl-directed mismatch repair |
| Q34698570 | MutS switches between two fundamentally distinct clamps during mismatch repair |
| Q56896392 | MutS-mediated enrichment of mutated DNA produced by directed evolution in vitro |
| Q42409924 | MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA. |
| Q36048384 | Mutations in the DNA mismatch repair proteins MutS and MutL of oxazolidinone-resistant or -susceptible Enterococcus faecium |
| Q34123282 | Mutations within the hMLH1 and hPMS2 subunits of the human MutLalpha mismatch repair factor affect its ATPase activity, but not its ability to interact with hMutSalpha |
| Q24679608 | N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha |
| Q41479268 | Nucleosome remodeling by hMSH2-hMSH6. |
| Q30938171 | Overexpression and purification of isotopically labeled Escherichia coli MutH for NMR studies |
| Q28256131 | Prokaryotic DNA mismatch repair |
| Q35879662 | Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair |
| Q36294768 | Reconstitution of the very short patch repair pathway from Escherichia coli |
| Q35653058 | Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition |
| Q27931230 | Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs |
| Q40921833 | Signaling from DNA mispairs to mismatch-repair excision sites despite intervening blockades |
| Q35027619 | Single molecule studies of DNA mismatch repair |
| Q39237485 | Single-Molecule FRET to Measure Conformational Dynamics of DNA Mismatch Repair Proteins |
| Q26999680 | Single-molecule views of MutS on mismatched DNA. |
| Q39731504 | Site-specific protein modification to identify the MutL interface of MutH. |
| Q50069592 | Spontaneous conversion between mutL and 6 bpDeltamutL in Salmonella typhimurium LT7: association with genome diversification and possible roles in bacterial adaptation |
| Q42160273 | Stoichiometry of MutS and MutL at unrepaired mismatches in vivo suggests a mechanism of repair |
| Q28285134 | Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activities |
| Q37592729 | Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair |
| Q38295775 | The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition |
| Q42094076 | The Presence of the DNA Repair Genes mutM, mutY, mutL, and mutS is Related to Proteome Size in Bacterial Genomes. |
| Q35100583 | The UvrD helicase and its modulation by the mismatch repair protein MutL. |
| Q27640375 | The alternating ATPase domains of MutS control DNA mismatch repair |
| Q26770149 | The conserved molecular machinery in DNA mismatch repair enzyme structures |
| Q44530427 | The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair |
| Q41860625 | The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair |
| Q35829125 | The frequency and structure of recombinant products is determined by the cellular level of MutL. |
| Q34533276 | The mechanism of mismatch repair and the functional analysis of mismatch repair defects in Lynch syndrome |
| Q42572300 | The role of nucleotide cofactor binding in cooperativity and specificity of MutS recognition |
| Q90622154 | The unstructured linker arms of MutL enable GATC site incision beyond roadblocks during initiation of DNA mismatch repair |
| Q44219222 | Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA. |
| Q43846779 | Visualization of mismatch repair in bacterial cells |
| Q37592119 | Visualizing the Path of DNA through Proteins Using DREEM Imaging |
| Q24292227 | hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA. |
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