Associated Papers
Disruption of protein-protein interaction hotspots in the C-terminal domain of MLH1 confers mismatch repair deficiency.
Fishwick KM et al.
Nar Cancer, 2025
WRN helicase and mismatch repair complexes independently and synergistically disrupt cruciform DNA structures.
Mengoli V et al.
The Embo Journal, 2023
36541070 (PubMed )
Supplement: EMBJ-42-e111998-s002.pdf
Evaluation of literature searching tools for curation of mismatch repair gene variants in hereditary colon cancer.
Kaushik V et al.
Advanced Genetics (hoboken, N.j.), 2021
36618447 (PubMed )
Supplement: GGN2-2-e10039-s001.zip › Google_Scholar_and_Mastermind_Search_Data_-_for_Submission.xlsx › Google_Scholar___Mastermind
The mutagen and carcinogen cadmium is a high-affinity inhibitor of the zinc-dependent MutLα endonuclease.
Sherrer SM et al.
Proceedings of the National Academy of Sciences of the United States of America, 2018
Dual daughter strand incision is processive and increases the efficiency of DNA mismatch repair.
Hermans N et al.
Nucleic Acids Research, 2016
Endonuclease activities of MutLα and its homologs in DNA mismatch repair.
Kadyrova LY et al.
Dna Repair, 2016
Structure of the MutLα C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site.
Gueneau E et al.
Nature Structural & Molecular Biology, 2013
The C-terminal domain is sufficient for endonuclease activity of Neisseria gonorrhoeae MutL.
Duppatla V et al.
The Biochemical Journal, 2009
The PMS2 subunit of human MutLalpha contains a metal ion binding domain of the iron-dependent repressor protein family.
Kosinski J et al.
Journal of Molecular Biology, 2008
Endonucleolytic function of MutLalpha in human mismatch repair.
Kadyrov FA et al.
Cell, 2006
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