| Droogmans, Louis |
Information last updated: 2020-08-28 |
Université Libre de Bruxelles; Faculté des Sciences; Department of Molecular Biology; Laboratory of microbiology, more
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| A1 Publications (5) [show] |
- Dutoit, R.; Brandt, N.; Van Elder, D.; Droogmans, L. (2020). X-ray crystallography to study the oligomeric state transition of the Thermotoga maritima M42 aminopeptidase TmPep1050. Jove-Journal of Visualized Experiments 159: e61288. https://dx.doi.org/10.3791/61288, more
- Dutoit, R.; Brandt, N.; Van Gompel, T.; Van Elder, D.; Van Dyck, J.; Sobott, F.; Droogmans, L. (2020). M42 aminopeptidase catalytic site: the structural and functional role of a strictly conserved aspartate residue. Proteins-Structure Function and Bioinformatics 88(12): 1639-1647. https://dx.doi.org/10.1002/prot.25982, more
 Wolff, P.; Villette, C.; Zumsteg, J.; Heintz, D.; Antoine, L.; Chane-Woon-Ming, B.; Droogmans, L.; Grosjean, H.; Westhof, E. (2020). Comparative patterns of modified nucleotides in individual tRNA species from a mesophilic and two thermophilic archaea. Rna 26(12): 1957-1975. https://hdl.handle.net/10.1261/rna.077537.120, more- Dutoit, R.; Van Gompel, T.; Brandt, N.; Van Elder, D.; Van Dyck, J.; Sobott, F.; Droogmans, L. (2019). How metal cofactors drive dimer–dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima. J. Biol. Chem. 294(47): 17777-17789. https://dx.doi.org/10.1074/jbc.RA119.009281, more
- Roovers, M.; Hale, C.; Tricot, C.; Terns, M.P.; Terns, R.M.; Grosjean, H.; Droogmans, L. (2006). Formation of the conserved pseudouridine at position 55 in archaeal tRNA. Nucleic Acids Res. 34(15): 4293-4301. https://dx.doi.org/10.1093/nar/gkl530, more
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