scholarly article | Q13442814 |
P50 | author | Stefan Zeuzem | Q28360321 |
P2093 | author name string | Jörg Trojan | |
Angela Brieger | |||
Guido Plotz | |||
Jochen Raedle | |||
P2860 | cites work | Mutations of two PMS homologues in hereditary nonpolyposis colon cancer | Q24318484 |
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 | ||
Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei | Q27860728 | ||
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 | ||
hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA | Q28138775 | ||
Identification of mismatch repair protein complexes in HeLa nuclear extracts and their interaction with heteroduplex DNA | Q28140727 | ||
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 | ||
Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs | Q28287503 | ||
Mutations of GTBP in genetically unstable cells | Q28292802 | ||
Tumour susceptibility and spontaneous mutation in mice deficient in Mlh1, Pms1 and Pms2 DNA mismatch repair | Q28508905 | ||
ATP-dependent interaction of human mismatch repair proteins and dual role of PCNA in mismatch repair | Q28610858 | ||
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 | ||
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 | ||
DNA mismatch correction in a defined system | Q34674714 | ||
ATP hydrolysis-dependent formation of a dynamic ternary nucleoprotein complex with MutS and MutL. | Q34712687 | ||
The DNA binding properties of the MutL protein isolated from Escherichia coli | Q35919359 | ||
Physical interaction between components of DNA mismatch repair and nucleotide excision repair | Q36733353 | ||
Escherichia coli MutL loads DNA helicase II onto DNA. | Q38308417 | ||
ATP-hydrolysis-dependent conformational switch modulates the stability of MutS-mismatch complexes | Q38316177 | ||
DNA-dependent activation of the hMutSalpha ATPase | Q38331192 | ||
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 | ||
Identification of hMutLbeta, a heterodimer of hMLH1 and hPMS1. | Q40920177 | ||
Evidence for a connection between the mismatch repair system and the G2 cell cycle checkpoint | Q41303489 | ||
MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast | Q42427955 | ||
Heteroduplex DNA and ATP induced conformational changes of a MutS mismatch repair protein from Thermus aquaticus | Q42975008 | ||
DNA chain length dependence of formation and dynamics of hMutSalpha.hMutLalpha.heteroduplex complexes | Q43664681 | ||
Mismatch repair, molecular switches, and signal transduction | Q47787090 | ||
Isolation and characterization of the Escherichia coli mutL gene product. | Q54734906 | ||
Mutation in the magnesium binding site of hMSH6 disables the hMutSalpha sliding clamp from translocating along DNA | Q58117131 | ||
Initiation of methyl-directed mismatch repair | Q64389906 | ||
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 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | MutL homolog 1 | Q6716597 |
MutS homolog 2 | Q6717778 | ||
MutS homolog 6 | Q6717781 | ||
single-stranded DNA binding | Q14864720 | ||
MutS homolog 3 | Q21118766 | ||
PMS1 homolog 2, mismatch repair system component | Q21118767 | ||
P304 | page(s) | 711-718 | |
P577 | publication date | 2002-02-01 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | hMutSalpha forms an ATP-dependent complex with hMutLalpha and hMutLbeta on DNA. | |
P478 | volume | 30 |
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. |
Q24295128 | Cytoskeletal scaffolding proteins interact with Lynch-Syndrome associated mismatch repair protein MLH1 |
Q36527421 | DNA mismatch repair and Lynch syndrome |
Q34309933 | DNA mismatch repair and oxidative DNA damage: implications for cancer biology and treatment |
Q36215972 | DNA mismatch repair complex MutSβ promotes GAA·TTC repeat expansion in human cells |
Q24647002 | DNA mismatch repair: molecular mechanism, cancer, and ageing |
Q50287454 | MSH2:MSH6 recruits MLH1:PMS2 to mismatch and interacts with PCNA |
Q39656168 | Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair |
Q35537125 | Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair |
Q24679608 | N-terminus of hMLH1 confers interaction of hMutLalpha and hMutLbeta with hMutSalpha |
Q33643516 | Nuclear reorganization of DNA mismatch repair proteins in response to DNA damage |
Q47113405 | Proteome Stability as a Key Factor of Genome Integrity |
Q36277189 | Repeat instability: mechanisms of dynamic mutations |
Q34236531 | Selenium compounds activate ATM-dependent DNA damage response via the mismatch repair protein hMLH1 in colorectal cancer cells |
Q28285134 | Structural, molecular and cellular functions of MSH2 and MSH6 during DNA mismatch repair, damage signaling and other noncanonical activities |
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 |
Q36448284 | The multifaceted mismatch-repair system |
Q24298905 | Thymosin beta 4 expression and nuclear transport are regulated by hMLH1 |
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