Li, Y.* , Boes, A.* , Cui, Y., Zhao, S., Liao, Q., Gong, H., Breukink, E., Lutkenhaus, J., Terrak, M.* , & Du, S.*. (2022). Identification of the potential active site of the septal peptidoglycan polymerase FtsW. PLoS Genetics, 18 (1), 1009993. doi:10.1371/journal.pgen.1009993 * These authors have contributed equally to this work. |
Boes, A., Brunel, J. M., Derouaux, A., Kerff, F., Bouhss, A., Touze, T., Breukink, E., & Terrak, M. (2020). Squalamine and Aminosterol Mimics Inhibit the Peptidoglycan Glycosyltransferase Activity of PBP1b. Antibiotics. doi:10.3390/antibiotics9070373 |
Boes, A., Olatunji, S., Mohammadi, T., Breukink, E., & Terrak, M. (2020). Fluorescence anisotropy assays for high throughput screening of compounds binding to lipid II, PBP1b, FtsW and MurJ. Scientific Reports, 10 (1), 6280. doi:10.1038/s41598-020-63380-2 |
Pazos, M., Peters, K., Boes, A., Safaei, Y., Kenward, C., Caveney, N. A., Laguri, C., Breukink, E., Strynadka, N. C. J., Simorre, J.-P., Terrak, M., & Vollmer, W. (2020). SPOR Proteins Are Required for Functionality of Class A Penicillin-Binding Proteins in Escherichia coli. MBio, 11 (6). doi:10.1128/mBio.02796-20 |
Boes, A., olatunji, S., Breukink, E., & Terrak, M. (08 January 2019). Regulation of the Peptidoglycan Polymerase Activity of PBP1b by Antagonist Actions of the Core Divisome Proteins FtsBLQ and FtsN. MBio, 10. doi:10.1128/mBio.01912-18 |
Leclercq, S., Derouaux, A., Olatunji, S., Fraipont, C., Egan, A. J. F., Vollmer, W., Breukink, E., & Terrak, M. (24 February 2017). Interplay between Penicillin-binding proteins and SEDS proteins promotes bacterial cell wall synthesis. Scientific Reports, 7, 43306. doi:10.1038/srep43306 |
Sauvage, E., & Terrak, M. (17 February 2016). Glycosyltransferases and Transpeptidases/Penicillin-Binding Proteins: Valuable Targets for New Antibacterials. Antibiotics, 5 (1). doi:10.3390/antibiotics5010012 |
Bury, D., Dahmane, I., Derouaux, A., Dumbre, S., Herdewijn, P., Matagne, A., Breukink, E., Mueller-Seitz, E., Petz, M., & Terrak, M. (2015). Positive cooperativity between acceptor and donor sites of the peptidoglycan glycosyltransferase. Biochemical Pharmacology, 93 (2), 141-50. doi:10.1016/j.bcp.2014.11.003 |
Arguelles Arias, A., Ongena, M., Devreese, B., Terrak, M., Joris, B., & Fickers, P. (2013). Characterization of amylolysin, a novel lantibiotic from Bacillus amyloliquefaciens GA1. PLoS ONE, 8 (12). doi:10.1371/journal.pone.0083037 |
Derouaux, A., Sauvage, E., & Terrak, M. (2013). Peptidoglycan glycosyltransferase substrate mimics as templates for the design of new antibacterial drugs. Frontiers in Immunology, 4, 78. doi:10.3389/fimmu.2013.00078 |
Rocaboy, M., Herman, R., Sauvage, E., Remaut, H., Moonens, K., Terrak, M., Charlier, P., & Kerff, F. (2013). The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain. Molecular Microbiology. doi:10.1111/mmi.12361 |
Dumbre, S., Derouaux, A., Lescrinier, E., Piette, A., Joris, B., Terrak, M., & Herdewijn, P. (2012). Synthesis of Modified Peptidoglycan Precursor Analogues for the Inhibition of Glycosyltransferase. Journal of the American Chemical Society. doi:10.1021/ja302099u |
Terrak, M., Sauvage, E., Derouaux, A., Dehareng, D., Bouhss, A., Breukink, E., Jeanjean, S., & Nguyen-Distèche, M. (2008). Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli. Journal of Biological Chemistry, 283 (42), 28464-70. doi:10.1074/jbc.M803223200 |
Terrak, M., Ghosh, T. K., van Heijenoort, J., Van Beeumen, J., Lampilas, M., Aszodi, J., Ayala, J. A., Ghuysen, J.-M., & Nguyen-Distèche, M. (October 1999). The Catalytic, Glycosyl Transferase and Acyl Transferase Modules of the Cell Wall Peptidoglycan-Polymerizing Penicillin-Binding Protein 1b of Escherichia Coli. Molecular Microbiology, 34 (2), 350-364. doi:10.1046/j.1365-2958.1999.01612.x |
Goffin, C., Fraipont, C., Ayala, J., Terrak, M., Nguyen-Distèche, M., & Ghuysen, J.-M. (September 1996). The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia Coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure. Journal of Bacteriology, 178 (18), 5402-5409. doi:10.1128/jb.178.18.5402-5409.1996 |