scholarly article | Q13442814 |
P2093 | author name string | Richard D Kolodner | |
Dan J Mazur | |||
Scarlet S Shell | |||
Victoria V Hargreaves | |||
Martin T Hess | |||
P2860 | cites work | The evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repair | Q24321288 |
hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6 | Q24323176 | ||
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 | ||
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 | ||
Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha. | Q27929951 | ||
A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition | Q27934451 | ||
The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations | Q27935158 | ||
exo1-Dependent mutator mutations: model system for studying functional interactions in mismatch repair | Q27935389 | ||
hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA | Q28138775 | ||
DNA mismatch repair and mutation avoidance pathways | Q28211143 | ||
The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch | Q28258968 | ||
Mechanisms and functions of DNA mismatch repair | Q28262719 | ||
Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs | Q28287503 | ||
DNA mismatch repair: functions and mechanisms | Q28296096 | ||
Isolation of MutSbeta from human cells and comparison of the mismatch repair specificities of MutSbeta and MutSalpha | Q28610863 | ||
Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair | Q29615027 | ||
A conserved MutS homolog connector domain interface interacts with MutL homologs | Q33552273 | ||
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 mismatch repair: the hands of a genome guardian. | Q34144865 | ||
Biochemical basis for dominant mutations in the Saccharomyces cerevisiae MSH6 gene | Q34270970 | ||
Restoration of mismatch repair to nuclear extracts of H6 colorectal tumor cells by a heterodimer of human MutL homologs | Q34554581 | ||
DNA mismatch repair: molecular mechanisms and biological function | Q35550610 | ||
Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins. | Q35865056 | ||
The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA | Q36026779 | ||
Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein | Q36359452 | ||
The multifaceted mismatch-repair system | Q36448284 | ||
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 | ||
Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA. | Q38320783 | ||
Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system. | Q38328409 | ||
Formation of a DNA mismatch repair complex mediated by ATP. | Q38347436 | ||
Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair | Q39656168 | ||
Identification of hMutLbeta, a heterodimer of hMLH1 and hPMS1. | Q40920177 | ||
Novel dominant mutations in Saccharomyces cerevisiae MSH6. | Q41711225 | ||
Distinct nucleotide binding/hydrolysis properties and molar ratio of MutSalpha and MutSbeta determine their differential mismatch binding activities | Q42081270 | ||
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 | ||
A biological network in Saccharomyces cerevisiae prevents the deleterious effects of endogenous oxidative DNA damage | Q43797761 | ||
The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair | Q44530427 | ||
Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA. | Q46462569 | ||
Isolation and characterization of the Escherichia coli mutH gene product. | Q54397103 | ||
Isolation and characterization of the Escherichia coli mutL gene product. | Q54734906 | ||
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 | ||
P433 | issue | 12 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | cell biology | Q7141 |
Saccharomyces cerevisiae | Q719725 | ||
P304 | page(s) | 9301-10 | |
P577 | publication date | 2010-03-19 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Interaction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complex | |
P478 | volume | 285 |
Q36540457 | A personal historical view of DNA mismatch repair with an emphasis on eukaryotic DNA mismatch repair |
Q37683114 | ATP alters the diffusion mechanics of MutS on mismatched DNA. |
Q35690218 | Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System |
Q35512872 | Base-flipping mechanism in postmismatch recognition by MutS. |
Q35880032 | Biochemical analysis of the human mismatch repair proteins hMutSα MSH2(G674A)-MSH6 and MSH2-MSH6(T1219D) |
Q30500132 | Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli |
Q57060631 | Coordinated protein and DNA conformational changes govern mismatch repair initiation by MutS |
Q37256043 | DNA conformations in mismatch repair probed in solution by X-ray scattering from gold nanocrystals. |
Q28709604 | DNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiae |
Q40823475 | Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair |
Q28534756 | Dominant mutations in S. cerevisiae PMS1 identify the Mlh1-Pms1 endonuclease active site and an exonuclease 1-independent mismatch repair pathway |
Q36436073 | Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair |
Q90647988 | Identification of Exo1-Msh2 interaction motifs in DNA mismatch repair and new Msh2-binding partners |
Q34120584 | Identifying targets of miR-143 using a SILAC-based proteomic approach |
Q45458727 | Interaction studies of muts and mutl with DNA containing the major cisplatin lesion and its mismatched counterpart under equilibrium and nonequilibrium conditions |
Q28264548 | Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling |
Q27659930 | Magnesium Coordination Controls the Molecular Switch Function of DNA Mismatch Repair Protein MutS |
Q36283640 | Mismatch repair |
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Q37691675 | Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex |
Q35165645 | Mlh2 is an accessory factor for DNA mismatch repair in Saccharomyces cerevisiae |
Q42409924 | MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA. |
Q28084645 | New insights into the mechanism of DNA mismatch repair |
Q27690911 | Postreplicative mismatch repair |
Q33800274 | Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry |
Q38005951 | Recognition of damaged DNA: structure and dynamic markers |
Q33556873 | Reconstitution of Saccharomyces cerevisiae DNA polymerase ε-dependent mismatch repair with purified proteins |
Q36540776 | Roles for mismatch repair family proteins in promoting meiotic crossing over |
Q28285134 | Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activities |
Q91595501 | The properties of Msh2-Msh6 ATP binding mutants suggest a signal amplification mechanism in DNA mismatch repair |
Q36162012 | The unstructured linker arms of Mlh1-Pms1 are important for interactions with DNA during mismatch repair |
Q37694831 | Two co-existing germline mutations P53 V157D and PMS2 R20Q promote tumorigenesis in a familial cancer syndrome |
Q36338245 | Visualization of eukaryotic DNA mismatch repair reveals distinct recognition and repair intermediates. |
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