Nos activités de recherche sont orientées vers la caractérisation biochimique, biophysique et structurale de protéines impliquées dans la physiologie et la pathogénèse bactériennes, plus particulièrement dans les processus de signalisation.
Type II topoisomerases challenges
Biologie structurale d’enzymes et complexes métaboliques
Biologie de Cibles du Paludisme et Antipaludiques
PknA/PknB in mycobacterial cell division
The genes pknA and pknB are located near the origin of replication in M. tuberculosis and are part of a conserved operon that also includes pstP (coding the only known Ser/Thr protein phosphatase […]
Control of glutamate metabolism in mycobacteria
We recently demonstrated the existence of a phosphorylation-dependent control of glutamate metabolism in mycobacteria, in collaboration with H. O’Hare’s group in Leicester (O’Hare et al., 2008). Our results were supported by similar observations […]
Envelope stress response
Our group, which has a long-term interest in protein folding, studies protein quality control systems in the periplasm of Escherichia coli. Our main objective is to understand the mechanism of misfolded protein sensing by […]
Structural studies of type II topoisomerases
Our main research projects focus on structural and functional studies of M. tuberculosis DNA gyrase and aim to understand the structural dynamics of DNA recognition by DNA gyrase and the quinolone resistance mechanisms […]
ATPase inhibitors, the cases of human heat shock protein 90 and bacterial type IIA topoisomerases
Organic synthesis, still the limiting factor of Medicinal Chemistry? This ongoing project is based on our reviews (1-3) on the inhibitors of the ATPase functions of human heat shock protein 90 (HSP90) or bacterial […]
Acyl-CoAs are the major metabolic carriers of carbon in living organisms. The most conserved ways to their synthesis include the oxidative decarboxylation of α-ketoacids carried out by three distinct enzymatic machineries: the pyruvate dehydrogenase […]
Tuberculosis still remains a major threat for public health, with one-third of the world population latently infected, and more than one million deaths per year according to the WHO. Among the factors that have […]
Despite the conservation of central metabolism, an increasing amount of evidence indicates that there are unique features in Actinobacteria, one of the largest bacterial phyla that includes important human pathogens like Mycobacterium tuberculosis and […]
2019Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling, Sci Signal 2019 May;12(580).
2019Novel mechanistic insights into physiological signaling pathways mediated by mycobacterial Ser/Thr protein kinases, Genes Immun. 2019 Apr;.
2019Double autoinhibition mechanism of signal transduction ATPases with numerous domains (STAND) with a tetratricopeptide repeat sensor, Nucleic Acids Res. 2019 Apr;47(7):3795-3810.
2019The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F binding protein with unknown function, J. Struct. Biol. 2019 May;206(2):216-224.
2019Overall Structures of Mycobacterium tuberculosis DNA Gyrase Reveal the Role of a Corynebacteriales GyrB-Specific Insert in ATPase Activity, Structure 2019 Apr;27(4):579-589.e5.
2018The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop, Antimicrob. Agents Chemother. 2019 Jan;63(1).
2018New substrates and interactors of the mycobacterial Serine/Threonine protein kinase PknG identified by a tailored interactomic approach, J Proteomics 2019 Feb;192:321-333.
2018The synthesis and kinetic evaluation of aryl α-aminophosphonates as novel inhibitors of T. cruzi trans-sialidase, Eur J Med Chem 2018 Oct;158:25-33.
2018Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance, J. Struct. Biol. 2018 Nov;204(2):165-171.
2018ArfGAP1 restrictsentry by controlling the actin cytoskeleton, EMBO Rep. 2018 Jan;19(1):29-42.
+Voir la liste complète de publications
25-28 Rue du Docteur Roux