| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0022-2836(03)00694-6 |
| P698 | PubMed publication ID | 12875840 |
| P2093 | author name string | Barbara Studamire | |
| Eric Alani | |||
| Amanda Wraith Kijas | |||
| P2860 | cites work | Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes | Q24290314 |
| hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci | Q24602221 | ||
| A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 | ||
| 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 | ||
| Escherichia coli MutL loads DNA helicase II onto DNA. | Q38308417 | ||
| Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete steps | Q38308734 | ||
| hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha | Q38336441 | ||
| Mismatch-, MutS-, MutL-, and helicase II-dependent unwinding from the single-strand break of an incised heteroduplex | Q38337751 | ||
| MutS and MutL activate DNA helicase II in a mismatch-dependent manner | Q38337755 | ||
| Mlh1 is unique among mismatch repair proteins in its ability to promote crossing-over during meiosis | Q38344945 | ||
| MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast | Q42427955 | ||
| Purification of eukaryotic MutL homologs from Saccharomyces cerevisiae using self-affinity technology. | Q42427963 | ||
| HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions | Q44068446 | ||
| Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA. | Q44219222 | ||
| Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6. | Q44267641 | ||
| Modulation of MutS ATP hydrolysis by DNA cofactors | Q73543806 | ||
| Interaction of Escherichia coli MutS and MutL at a DNA mismatch | Q73923892 | ||
| The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity | Q77765360 | ||
| 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 | ||
| Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis | Q27766073 | ||
| The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs | Q27930815 | ||
| Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination | Q27931976 | ||
| Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition. | Q27932001 | ||
| Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair | Q27932017 | ||
| Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex | Q27932428 | ||
| A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition | Q27934451 | ||
| The Saccharomyces cerevisiae Msh2 mismatch repair protein localizes to recombination intermediates in vivo. | Q27935147 | ||
| MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp | Q27935260 | ||
| Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination | Q27938377 | ||
| Evidence for involvement of yeast proliferating cell nuclear antigen in DNA mismatch repair | Q27938608 | ||
| 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 | ||
| Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction | Q27939611 | ||
| Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis | Q27939891 | ||
| hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA | Q28138775 | ||
| Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex | Q28142999 | ||
| DNA mismatch repair and mutation avoidance pathways | Q28211143 | ||
| The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch | Q28258968 | ||
| 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 | ||
| Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD. | Q32108861 | ||
| Mammalian DNA mismatch repair | Q33847720 | ||
| MutS mediates heteroduplex loop formation by a translocation mechanism | Q33887145 | ||
| 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 | Q34123282 | ||
| DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers | Q34835637 | ||
| DNA curvature and deformation in protein-DNA complexes: a step in the right direction | Q36085445 | ||
| Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP. | Q38289639 | ||
| Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. | Q38295596 | ||
| The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition | Q38295775 | ||
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | DNA mismatch repair | Q2984243 |
| P304 | page(s) | 123-138 | |
| P577 | publication date | 2003-08-01 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair | |
| P478 | volume | 331 |
| Q36677284 | A Delicate Balance Between Repair and Replication Factors Regulates Recombination Between Divergent DNA Sequences in Saccharomyces cerevisiae |
| Q34573320 | A role for DNA mismatch repair protein Msh2 in error-prone double-strand-break repair in mammalian chromosomes |
| Q40762229 | ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates |
| Q36315875 | Accurate homologous recombination is a prominent double-strand break repair pathway in mammalian chromosomes and is modulated by mismatch repair protein Msh2. |
| Q27938988 | Analysis of the functional domains of the mismatch repair homologue Msh1p and its role in mitochondrial genome maintenance. |
| Q24300627 | Analysis of the human MutLalpha.MutSalpha complex |
| Q38328409 | Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system. |
| Q40823475 | Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair |
| Q34570828 | Distinct roles for the Saccharomyces cerevisiae mismatch repair proteins in heteroduplex rejection, mismatch repair and nonhomologous tail removal |
| Q27659620 | Functional residues on the surface of the N-terminal domain of yeast Pms1 |
| Q33701780 | Genetic Analysis of Baker's Yeast Msh4-Msh5 Reveals a Threshold Crossover Level for Meiotic Viability |
| Q36990847 | Microarray based analysis of temperature and oxidative stress induced messenger RNA in Schistosoma mansoni |
| Q28305501 | Mlh1-Mlh3, a meiotic crossover and DNA mismatch repair factor, is a Msh2-Msh3-stimulated endonuclease |
| Q38168515 | Modern aspects of the structural and functional organization of the DNA mismatch repair system |
| Q38271431 | Multiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I. |
| Q37308166 | Reciprocal regulation of nuclear import of the yeast MutSalpha DNA mismatch repair proteins Msh2 and Msh6. |
| Q35653058 | Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition |
| Q47317424 | Sub-cellular localization analysis of MSH6 missense mutations does not reveal an overt MSH6 nuclear transport impairment |
| Q36162012 | The unstructured linker arms of Mlh1-Pms1 are important for interactions with DNA during mismatch repair |
| Q50724526 | Trapping and visualizing intermediate steps in the mismatch repair pathway in vivo. |
| Q28253087 | Variation in crossover frequencies perturb crossover assurance without affecting meiotic chromosome segregation in Saccharomyces cerevisiae |
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