Publications

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

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