scholarly article | Q13442814 |
P2093 | author name string | P Modrich | |
K P Bjornson | |||
L J Blackwell | |||
P2860 | cites work | hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6 | Q24323176 |
An Algorithm for Least-Squares Estimation of Nonlinear Parameters | Q26778383 | ||
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 | ||
Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex | Q27932428 | ||
ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes | Q27939412 | ||
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 | ||
GTBP, a 160-kilodalton protein essential for mismatch-binding activity in human cells | Q28292790 | ||
hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA | Q28610839 | ||
DHFR/MSH3 amplification in methotrexate-resistant cells alters the hMutSalpha/hMutSbeta ratio and reduces the efficiency of base-base mismatch repair | Q28610848 | ||
Isolation of MutSbeta from human cells and comparison of the mismatch repair specificities of MutSbeta and MutSalpha | Q28610863 | ||
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 | ||
Strand-specific mismatch correction in nuclear extracts of human and Drosophila melanogaster cell lines | Q33720790 | ||
MutS mediates heteroduplex loop formation by a translocation mechanism | Q33887145 | ||
Restoration of mismatch repair to nuclear extracts of H6 colorectal tumor cells by a heterodimer of human MutL homologs | Q34554581 | ||
Dominant negative mutator mutations in the mutS gene of Escherichia coli | Q34726651 | ||
Repair of DNA heteroduplexes containing small heterologous sequences in Escherichia coli | Q36856385 | ||
Mechanisms and biological effects of mismatch repair | Q37041860 | ||
Methyl-directed repair of DNA base-pair mismatches in vitro | Q37344016 | ||
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 | ||
Molecular matchmakers | Q40885529 | ||
DNA-replication fidelity, mismatch repair and genome instability in cancer cells | Q41016785 | ||
Hypermutability and mismatch repair deficiency in RER+ tumor cells | Q41508298 | ||
MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast | Q42427955 | ||
Kinetic parameters of the translocation of bacteriophage T4 gene 41 protein helicase on single-stranded DNA. | Q44586872 | ||
MSH6, a Saccharomyces cerevisiae protein that binds to mismatches as a heterodimer with MSH2. | Q48065235 | ||
Kinetic theory of ATP-driven translocases on one-dimensional polymer lattices. | Q52381235 | ||
P433 | issue | 48 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 32049-32054 | |
P577 | publication date | 1998-11-01 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | DNA-dependent activation of the hMutSalpha ATPase | |
P478 | volume | 273 |
Q41792406 | (CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition |
Q37683114 | ATP alters the diffusion mechanics of MutS on mismatched DNA. |
Q38316177 | ATP-hydrolysis-dependent conformational switch modulates the stability of MutS-mismatch complexes |
Q39156478 | Acidic tumor microenvironment downregulates hMLH1 but does not diminish 5-fluorouracil chemosensitivity |
Q33857078 | Adenine excisional repair function of MYH protein on the adenine:8-hydroxyguanine base pair in double-stranded DNA. |
Q28359649 | Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches |
Q24300627 | Analysis of the human MutLalpha.MutSalpha complex |
Q34099011 | Both hMutSα and hMutSß DNA mismatch repair complexes participate in 5-fluorouracil cytotoxicity |
Q24798955 | Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex |
Q35910253 | Chromosomal directionality of DNA mismatch repair in Escherichia coli |
Q34334316 | Colon cancer associated genes exhibit signatures of positive selection at functionally significant positions |
Q57784307 | Coordinating Multi-Protein Mismatch Repair by Managing Diffusion Mechanics on the DNA |
Q27640487 | Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair |
Q37602208 | DNA mismatch repair (MMR)-dependent 5-fluorouracil cytotoxicity and the potential for new therapeutic targets. |
Q34141513 | DNA mismatch repair: MutS structures bound to mismatches. |
Q44353892 | Differential and simultaneous adenosine di- and triphosphate binding by MutS. |
Q78037753 | Dissociation of mismatch recognition and ATPase activity by hMSH2-hMSH3 |
Q42081270 | Distinct nucleotide binding/hydrolysis properties and molar ratio of MutSalpha and MutSbeta determine their differential mismatch binding activities |
Q44068446 | HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions |
Q36968380 | Hereditary cancer-associated missense mutations in hMSH6 uncouple ATP hydrolysis from DNA mismatch binding |
Q35562811 | Human MSH2 (hMSH2) protein controls ATP processing by hMSH2-hMSH6 |
Q28608973 | Mechanisms of human DNA repair: an update |
Q43990123 | Mismatch repair in human nuclear extracts. Time courses and ATP requirements for kinetically distinguishable steps leading to tightly controlled 5' to 3' and aphidicolin-sensitive 3' to 5' mispair-provoked excision |
Q34293069 | Molecular mechanisms of DNA mismatch repair |
Q33799870 | MutLalpha and proliferating cell nuclear antigen share binding sites on MutSbeta |
Q24679608 | N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha |
Q28610864 | Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism |
Q34272353 | PCR candidate region mismatch scanning: adaptation to quantitative, high-throughput genotyping |
Q27690911 | Postreplicative mismatch repair |
Q42386247 | Production of truncated MBD4 protein by frameshift mutation in DNA mismatch repair-deficient cells enhances 5-fluorouracil sensitivity that is independent of hMLH1 status |
Q35132521 | Signaling mismatch repair: the mechanics of an adenosine-nucleotide molecular switch |
Q26999680 | Single-molecule views of MutS on mismatched DNA. |
Q44530427 | The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair |
Q27627644 | The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch |
Q41860625 | The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair |
Q34533276 | The mechanism of mismatch repair and the functional analysis of mismatch repair defects in Lynch syndrome |
Q36448284 | The multifaceted mismatch-repair system |
Q35563361 | The predicted truncation from a cancer-associated variant of the MSH2 initiation codon alters activity of the MSH2-MSH6 mismatch repair complex |
Q28610649 | The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch |
Q24622206 | hMSH4-hMSH5 adenosine nucleotide processing and interactions with homologous recombination machinery |
Q24292227 | hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA. |
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