| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.M202282200 |
| P698 | PubMed publication ID | 11986324 |
| P2093 | author name string | Ruchira Das Gupta | |
| Richard D Kolodner | |||
| Martin T Hess | |||
| P2860 | cites work | Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes | Q24290314 |
| The interaction of DNA mismatch repair proteins with human exonuclease I | Q24291370 | ||
| Activation of human MutS homologs by 8-oxo-guanine DNA damage | Q24292069 | ||
| Identification and characterization of Saccharomyces cerevisiae EXO1, a gene encoding an exonuclease that interacts with MSH2 | Q24314329 | ||
| hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6 | Q24323176 | ||
| hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci | Q24602221 | ||
| MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures | Q26778412 | ||
| Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily | Q27625340 | ||
| 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 | ||
| Raster3D: photorealistic molecular graphics | Q27860557 | ||
| XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density | Q27861034 | ||
| The Saccharomyces cerevisiae Msh2 protein specifically binds to duplex oligonucleotides containing mismatched DNA base pairs and insertions | Q38299752 | ||
| Analysis of yeast MSH2-MSH6 suggests that the initiation of mismatch repair can be separated into discrete steps | Q38308734 | ||
| Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA. | Q38320783 | ||
| hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha | Q38336441 | ||
| MutS and MutL activate DNA helicase II in a mismatch-dependent manner | Q38337755 | ||
| Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes | Q40022200 | ||
| One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease | Q41689635 | ||
| Novel dominant mutations in Saccharomyces cerevisiae MSH6. | Q41711225 | ||
| MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast | Q42427955 | ||
| DNA chain length dependence of formation and dynamics of hMutSalpha.hMutLalpha.heteroduplex complexes | Q43664681 | ||
| Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis | Q43675423 | ||
| Mismatch repair, molecular switches, and signal transduction | Q47787090 | ||
| Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit | Q50335571 | ||
| Photocross-linking of the NH2-terminal region of Taq MutS protein to the major groove of a heteroduplex DNA. | Q54558924 | ||
| Interaction of Escherichia coli MutS and MutL at a DNA mismatch | Q73923892 | ||
| Redundant exonuclease involvement in Escherichia coli methyl-directed mismatch repair | Q74064844 | ||
| The Escherichia coli MutL protein physically interacts with MutH and stimulates the MutH-associated endonuclease activity | Q77765360 | ||
| Dissociation of mismatch recognition and ATPase activity by hMSH2-hMSH3 | Q78037753 | ||
| The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs | Q27930815 | ||
| 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 | ||
| Saccharomyces cerevisiae MSH2, a mispaired base recognition protein, also recognizes Holliday junctions in DNA. | Q27932061 | ||
| 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 | ||
| 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 | ||
| Proliferating cell nuclear antigen and Msh2p-Msh6p interact to form an active mispair recognition complex | Q28142999 | ||
| The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch | Q28258968 | ||
| Biochemistry and genetics of eukaryotic mismatch repair | Q28282377 | ||
| Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs | Q28287503 | ||
| Isolation of an hMSH2-p160 Heterodimer That Restores DNA Mismatch Repair to Tumor Cells | Q28292781 | ||
| The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch | Q28610649 | ||
| hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA | Q28610839 | ||
| Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism | Q28610864 | ||
| Multiple functions of MutS- and MutL-related heterocomplexes | Q28776215 | ||
| Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair | Q29615027 | ||
| Mismatch repair in replication fidelity, genetic recombination, and cancer biology | Q29616483 | ||
| Subunit interactions in ABC transporters: towards a functional architecture | Q30175332 | ||
| Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysis | Q31852984 | ||
| Evidence for a physical interaction between the Escherichia coli methyl-directed mismatch repair proteins MutL and UvrD. | Q32108861 | ||
| Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein | Q33786744 | ||
| MutS mediates heteroduplex loop formation by a translocation mechanism | Q33887145 | ||
| Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae | Q33933718 | ||
| DNA mismatch repair genes and colorectal cancer | Q33947053 | ||
| DNA mismatch repair and genetic instability | Q34090778 | ||
| DNA mismatch repair: MutS structures bound to mismatches. | Q34141513 | ||
| DNA mismatch repair and cancer | Q34164892 | ||
| Replication of duplex DNA by bacteriophage T7 DNA polymerase and gene 4 protein is accompanied by hydrolysis of nucleoside 5'-triphosphates | Q35019336 | ||
| Mechanisms and biological effects of mismatch repair | Q37041860 | ||
| 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 | 28 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Saccharomyces cerevisiae | Q719725 |
| P304 | page(s) | 25545-25553 | |
| P577 | publication date | 2002-05-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP. | |
| P478 | volume | 277 |
| Q40762229 | ATP binding and hydrolysis by Saccharomyces cerevisiae Msh2-Msh3 are differentially modulated by mismatch and double-strand break repair DNA substrates |
| Q35690218 | Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System |
| Q38328409 | Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system. |
| Q39656345 | Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. |
| Q35880032 | Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D) |
| Q34270970 | Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene |
| Q34099011 | Both hMutSα and hMutSß DNA mismatch repair complexes participate in 5-fluorouracil cytotoxicity |
| Q78787215 | Current awareness on yeast |
| Q37602208 | DNA mismatch repair (MMR)-dependent 5-fluorouracil cytotoxicity and the potential for new therapeutic targets. |
| Q44353892 | Differential and simultaneous adenosine di- and triphosphate binding by MutS. |
| Q24337694 | Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites |
| Q40823475 | Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair |
| Q36436073 | Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair |
| Q33711830 | Eukaryotic Mismatch Repair in Relation to DNA Replication |
| Q41811704 | Genetic analyses of a hybrid cross between serotypes A and D strains of the human pathogenic fungus Cryptococcus neoformans |
| Q24629057 | Interaction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complex |
| Q36836991 | Interplay of DNA repair pathways controls methylation damage toxicity in Saccharomyces cerevisiae |
| Q36283640 | Mismatch repair |
| Q35164333 | Mismatch repair during homologous and homeologous recombination |
| 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 |
| Q28084645 | New insights into the mechanism of DNA mismatch repair |
| Q38029584 | Pathological assessment of mismatch repair gene variants in Lynch syndrome: past, present, and future |
| Q33800274 | Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry |
| Q28256131 | Prokaryotic DNA mismatch repair |
| Q27931230 | Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs |
| Q33640393 | Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair |
| Q27640375 | The alternating ATPase domains of MutS control DNA mismatch repair |
| Q44530427 | The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair |
| Q91595501 | The properties of Msh2-Msh6 ATP binding mutants suggest a signal amplification mechanism in DNA mismatch repair |
| Q44219222 | Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA. |
| Q29619405 | X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution |
Search more.