Dubus Alice

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Main Referenced Co-authors

Frère, Jean-Marie (7)

Raquet, X. (4)

Christiaens, Léon (2)

Damblon, Christian (2)

Jamin, M. (2)

Main Referenced Keywords

Amino Acid Sequence (2); Kinetics (2); Molecular Sequence Data (2); Acylation (1); Anti-Bacterial Agents/metabolism (1);

Main Referenced Disciplines

Biochemistry, biophysics & molecular biology (6)

Microbiology (2)

Pharmacy, pharmacology & toxicology (1)

Publications (total 7)

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The most downloaded

315 downloads

Fonze, E., Charlier, P., To'th, Y., Vermeire, M., Raquet, X., Dubus, A., & Frère, J.-M. (1995). TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Crystallographica. Section D, Biological Crystallography, 51 (Pt 5), 682-94. doi:10.1107/S0907444994014496 https://hdl.handle.net/2268/80431

The most cited

84 citations (Scopus®)

Fonze, E., Charlier, P., To'th, Y., Vermeire, M., Raquet, X., Dubus, A., & Frère, J.-M. (1995). TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Crystallographica. Section D, Biological Crystallography, 51 (Pt 5), 682-94. doi:10.1107/S0907444994014496 https://hdl.handle.net/2268/80431

Lakaye, B., Dubus, A., Joris, B., & Frère, J.-M. (September 2002). Method for estimation of low outer membrane permeability to beta-lactam antibiotics. Antimicrobial Agents and Chemotherapy, 46 (9), 2901-2907. doi:10.1128/AAC.46.9.2901-2907.2002

https://hdl.handle.net/2268/22702

Peer Reviewed verified by ORBi

Lakaye, B., Dubus, A., Lepage, S., Groslambert, S., & Frère, J.-M. (January 1999). When Drug Inactivation Renders the Target Irrelevant to Antibiotic Resistance: A Case Story with Beta-Lactams. Molecular Microbiology, 31 (1), 89-101. doi:10.1046/j.1365-2958.1999.01150.x

https://hdl.handle.net/2268/27629

Peer Reviewed verified by ORBi

Galleni, M., Lamotte-Brasseur, J., Raquet, X., Dubus, A., Monnaie, D., Knox, J. R., & Frère, J.-M. (11 May 1995). The Enigmatic Catalytic Mechanism of Active-Site Serine Beta-Lactamases. Biochemical Pharmacology, 49 (9), 1171-8. doi:10.1016/0006-2952(94)00502-D

https://hdl.handle.net/2268/188778

Peer Reviewed verified by ORBi

Damblon, C., Ledent, P., Zhao, G. H., Jamin, M., Dubus, A., Vanhove, M.-L., Raquet, X., Christiaens, L., & Frère, J.-M. (1995). Thiolester substrates of DD-peptidases and beta-lactamases. Letters in Peptide Science, 2 (3-4), 212-216. doi:10.1007/BF00119156

https://hdl.handle.net/2268/77939

Peer Reviewed verified by ORBi

Damblon, C., Zhao, G. H., Jamin, M., Ledent, P., Dubus, A., Vanhove, M.-L., Raquet, X., Christiaens, L., & Frère, J.-M. (1995). Breakdown of the stereospecificity of DD-peptidases and beta-lactamases with thiolester substrates. Biochemical Journal, 309 ( Pt 2), 431-6. doi:10.1042/bj3090431

https://hdl.handle.net/2268/77931

Peer Reviewed verified by ORBi

Fonze, E., Charlier, P., To'th, Y., Vermeire, M., Raquet, X., Dubus, A., & Frère, J.-M. (1995). TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant. Acta Crystallographica. Section D, Biological Crystallography, 51 (Pt 5), 682-94. doi:10.1107/S0907444994014496

https://hdl.handle.net/2268/80431

Peer Reviewed verified by ORBi

Wilkin, J. M., Dubus, A., Joris, B., & Frère, J.-M. (1994). The mechanism of action of DD-peptidases: the role of Threonine-299 and -301 in the Streptomyces R61 DD-peptidase. Biochemical Journal, 301 ( Pt 2), 477-83. doi:10.1042/bj3010477

https://hdl.handle.net/2268/125364

Peer Reviewed verified by ORBi