The mycobacterial mutasome: composition and recruitment in live cells
Gessner S, Martin Z, Reiche MA, Santos JA, Dhar N, Dinkele R, De Wet T, Ramudzuli A, Anoosheh S, Lang D, Aaron J, Chew TL, Herrmann J, Müller R, McKinney JD, Woodgate R, Mizrahi V, Lamers MH, Warner DF.
Accepted: eLife, Aug 2023
A four-point molecular handover during Okazaki maturation
Botto MM, Borsellini A, Lamers MH.
Accepted: Nat Struct Mol Biol, July 2023
A high-throughput exonuclease assay based on the fluorescent base analog 2-aminopurine
Botto MM, Murthy S, Lamers MH.
ACS Omega 2023 Feb 20;8(9):8285–8292
MutL binds to 3' resected ends and blocks polymerase access
Borsellini A, Lebbink J, Lamers MH.
Nucleic Acid Res. 2022 June 24; 50(11):6224-6234
DNA-dependent binding of nargenincin to DnaE1 inhibits replication in Mycobacterium tuberculosis
Chengalroyen MD, Mason MK, Borsellini A, Tassoni R, Abrahams GL, Lynch S, Ahn YM, Ambler J, Young K, Crowley BM, Olsen DB, Warner DF, Barry Iii CE, Boshoff HIM, Lamers MH, Mizrahi V.
ACS Infect Dis. 2022 Mar 11;8(3):612-625
Cryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair
Borsellini A, Kunetsky V, Friedhoff P, Lamers MH.
Nat Struct & Mol Biol. 2022 Jan;29(1):59-66
Zinc finger protein ZNF384 is an adaptor of Ku to DNA during classical non-homologous end-joining
Singh JK, Smith R, Rother MB, de Groot AJL, Wiegant WW, Vreeken K, D'Augustin O, Kim RQ, Qian H, Krawczyk PM, González-Prieto R, Vertegaal ACO, Lamers M, Huet S, van Attikum H.
Nat Commun. 2021 Nov 12;12(1):6560
The selection process of licensing a DNA mismatch for repair
Fernandez-Leiro R, Bhairosing-Kok D, Kunetsky V, Laffeber C, Winterwerp HH, Groothuizen F, Fish A, Lebbink JHG, Friedhoff P, Sixma TK, Lamers MH. (2021)
Nat. Struct. & Mol. Biol. 28(4):373-381
Novel antibiotics targeting bacterial replicative DNA polymerases
Santos JA, Lamers MH. (2020)
Antibiotics 9(11):776
Polymerization and editing modes of a high-fidelity DNA polymerase are linked by a well-defined path
Dodd T, Botto M, Paul F, Fernandez-Leiro R, Lamers MH, Ivanov I. (2020)
Nat. Commun. 11(1):5379
SMCHD1 mutation spectrum for facioscapulohumeral muscular dystrophy type 2 (FSHD2) and Bosma arhinia microphthalmia syndrome (BAMS) reveals disease-specific localisation of variants in the ATPase domain
Lemmers RJLF, van der Stoep N, Vliet PJV, Moore SA, San Leon Granado D, (...) Lamers M, van der Maarel SM. (2019)
J. Med. Genet. 56(10):693-700
Antigen Presentation: Visualizing the MHC Class I Peptide-Loading Bottleneck.
Lamers M, Berlin I, Neefjes J. (2018)
Curr. Biol. 28(2): R83-R86
Reduced structural flexibility for an exonuclease deficient DNA polymerase III mutant
Gahlon HL, Walker AR, Cisneros GA, Lamers MH, Rueda DS. (2018)
Phys Chem Chem Phys. 20(42):26892-26902.
Single-molecule studies contrast ordered DNA replication with stochastic translesion synthesis
Zhao G, Gleave ES, Lamers MH. (2017)
eLife 6 e32177.
High-fidelity DNA replication in Mycobacterium tuberculosis relies on a trinuclear zinc center
Baños-Mateos S, van Roon A-MM, Lang UF, Maslen SL, Skehel JM, Lamers MH. (2017)
Nat Commun. 8(1):855.
DNA Replication in Mycobacterium tuberculosis
Ditse Z, Lamers MH, Warner DF. (2017)
Microbiol. Spectr. 5(2).
Self-correcting mismatches during high-fidelity DNA replication
Fernandez-Leiro R, Conrad J, Yang JC, Freund SMV, Scheres HWS and Lamers MH. (2017)
Nature Structure & Molecular Biology 24(2):140-143
Cryo-EM structures of the E. coli replicative DNA polymerase reveal dynamic interactions with clamp, exonuclease and t
Fernandez-Leiro R, Conrad J, Scheres HWS and Lamers MH. (2015)
eLife 4:e11134
Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum
Aibara S, Valkov E, Lamers MH, Dimitrova L, Hurt E, Stewart M. (2015)
Acta Crystallogr F Struct Biol Commun. 2015 71(7):876-88
Replication fidelity in M. tuberculosis is mediated by an ancestral prokaryotic proofreader
Rock JM, Lang UF, Chase MR, Ford CB, Gerrick ER, Gawande R, Coscolla M, Gagneux S, Fortune SM and Lamers MH. (2015)
Nature Genetics. 47(6):677-681
Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface
Aibara S, Valkov E, Lamers M, Stewart M. (2015)
Nucleic Acids Res. 43(3):1927-36.
Hekate: software for the mass spectrometric analysis and three-dimensional visualization of cross-linked protein samples
Holding AN, Lamers MH, Stephens E and Skehel JM (2013)
J. Proteome Res. 12(12):5923-33
A structural role for the PHP domain in E. coli DNA polymerase III
Barros T, Guenther J, Kelch B, Anaya J, Prabhaker A, O’Donnell M, Kuriyan J and Lamers MH. (2013)
BMC Struc. Biol. 13(1):8
Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair
Toste Rêgo A, Holding A, Kent H and Lamers MH. (2013)
EMBO J. 32(9): 1334-43
The ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD-fold that binds membranes
Hadders MA, Agromayor M, Obita T, Perisic O, Caballe A, Kloc M, Lamers MH, Williams RL and Martin‐Serrano J. (2012)
Proc. Natl. Acad. Sci. 109(43)17424-9
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
Jura N, Endres N, Engel K, Deindl S, Das R, Lamers MH, Wemmer D, Zhang X, and Kuriyan J. (2009)
Cell 137(7):1293-307
Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation
Batchelor JD, Doucleff M, Lee CJ, Matsubara K, De Carlo S, Heideker J, Lamers MH, Pelton JG and Wemmer DE. (2008)
J. Mol. Biol. 384(5)1058-75
A consensus view of DNA binding by the C family replicative DNA polymerases
Lamers MH and O'Donnell M. (2008)
Proc. Natl. Acad. Sci. 105(52):20565-6
The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase
Winger JA, Derbyshire ER, Lamers MH, Marletta MA, and Kuriyan J. (2008)
BMC Struct. Biol. 8:42
Crystal Structure of the Catalytic α Subunit of E. coli Replicative DNA Polymerase III
Lamers MH, Georgescu RE, Lee SG, O'Donnell M and Kuriyan J. (2006)
Cell 126(5):881-92
ATP increases the affinity between MutS ATPase domains: implication for ATP hydrolysis and conformational changes
Lamers MH, Georgijevic D, Lebbink J, Winterwerp HHK, Agianian B, de Wind N, and Sixma TK. (2004)
J. Biol. Chem. 279(42):43879-85
Dissimilar mispair recognition spectra of Arabidopsis DNA-mismatch repair proteins MSH2·MSH6 (MutSα) and MSH2·MSH7 (MutSγ)
Wu SY, Culligan K, Lamers M, and Hays J. (2003)
Nucleic Acid Res. 31(20):6027-34
Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates
Natrajan G, Lamers MH, Enzlin JH, Winterwerp HHK, Perrakis A and Sixma TK. (2003)
Nucleic Acid Res. 31(16)4814-21
The alternating ATPase domains of MutS control DNA mismatch repair
Lamers MH, Winterwerp HHK and Sixma TK. (2003)
EMBO J. 22(3)746-56
The crystal structure of DNA mismatch repair protein MutS binding to a G:T mismatch
Lamers MH, Perrakis A, Enzlin JH. Winterwerp HHK, de Wind N and Sixma TK. (2000)
Nature 407(6805):711-17
