 Labar, G.; Brandt, N.; Flaba, A.; Wouters, J.; Leherte, L. (2021). Structure and dynamics of an archeal monoglyceride lipase from Palaeococcus ferrophilus as revealed by crystallography and in silico analysis. Biomolecules 11(4): 533. https://dx.doi.org/10.3390/biom11040533, more- 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
- Rigane, E.; Dutoit, R.; Matthijs, S.; Brandt, N.; Flahaut, S.; Belghith, K.S. (2020). Characterization of putative virulence factors of Pseudomonas aeruginosa strain RBS isolated from a saltern, Tunisia: effect of metal ion cofactors on the structure and the activity of LasB. Biomed. Res. Int. 2020: 6047528. https://hdl.handle.net/10.1155/2020/6047528, 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
- Dutoit, R.; Brandt, N.; Legrain, C.; Bauvois, C. (2012). Functional characterization of two M42 aminopeptidases erroneously annotated as cellulases. PLoS One 7(11): e50639. https://dx.doi.org/10.1371/journal.pone.0050639, more
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