Martin Picard

Adrien, V., Taulier, N., Verchère, A., Monlezun, L., Picard, M., Ducruix, A., Broutin, I., Pincet, F., Urbach, W., 2024. Kinetic study of membrane protein interactions: from three to two dimensions. Sci Rep 14, 882. https://doi.org/10.1038/s41598-023-50827-5

Picard, M., 2023. Membrane proteins. Biochimie, Membranes Proteins 205, 1–2. https://doi.org/10.1016/j.biochi.2023.01.018

Batista Dos Santos, W., Souabni, H., Picard, M., 2022. Corseting a tripartite ABC transporter to make it fit for transport. Biochimie S0300-9084(22)00308-X. https://doi.org/10.1016/j.biochi.2022.11.012

Adrien, V., Rayan, G., Astafyeva, K., Broutin, I., Picard, M., Fuchs, P., Urbach, W., Taulier, N., 2021. How to best estimate the viscosity of lipid bilayers. Biophys Chem 281, 106732. https://doi.org/10.1016/j.bpc.2021.106732

Alav, I., Kobylka, J., Kuth, M.S., Pos, K.M., Picard, M., Blair, J.M.A., Bavro, V.N., 2021. Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria. Chem Rev. https://doi.org/10.1021/acs.chemrev.1c00055

Souabni, H., Batista dos Santos, W., Cece, Q., Catoire, L.J., Puvanendran, D., Bavro, V.N., Picard, M., 2021. Quantitative real-time analysis of the efflux by the MacAB-TolC tripartite efflux pump clarifies the role of ATP hydrolysis within mechanotransmission mechanism. Communications Biology 4, 1–9. https://doi.org/10.1038/s42003-021-01997-3

Glavier, M., Puvanendran, D., Salvador, D., Decossas, M., Phan, G., Garnier, C., Frezza, E., Cece, Q., Schoehn, G., Picard, M., Taveau, J.-C., Daury, L., Broutin, I., Lambert, O., 2020. Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex. Nature Communications 11, 4948. https://doi.org/10.1038/s41467-020-18770-5

Souabni, H., Santos, W.B. dos, Cece, Q., Puvanendran, D., Picard, M., 2020. Quantum dot probes for the quantitative study of drug transport by the MacAB TolC efflux pump in lipid scaffolds. bioRxiv 2020.06.16.154831. https://doi.org/10.1101/2020.06.16.154831

Puvanendran, D., Souabni, H., Salvador, D., Lambert, O., Cece, Q., Picard, M., 2020. Rationale for the Quantitative Reconstitution of Membrane Proteins into Proteoliposomes. Methods Mol Biol 2168, 63–72. https://doi.org/10.1007/978-1-0716-0724-4_3

Gomez-Zepeda, D., Taghi, M., Smirnova, M., Sergent, P., Liu, W.-Q., Chhuon, C., Vidal, M., Picard, M., Thioulouse, E., Broutin, I., Guerrera, I.-C., Scherrmann, J.-M., Parmentier, Y., Decleves, X., Menet, M.-C., 2019. LC-MS/MS-based quantification of efflux transporter proteins at the BBB. J Pharm Biomed Anal 164, 496–508. https://doi.org/10.1016/j.jpba.2018.11.013

Champeil, P., de Foresta, B., Picard, M., Gauron, C., Georgin, D., le Maire, M., Møller, J.V., Lenoir, G., Montigny, C., 2019. Interaction of detergents with biological membranes: Comparison of fluorescence assays with filtration protocols and implications for the rates of detergent association, dissociation and flip-flop. PLoS ONE 14, e0222932. https://doi.org/10.1371/journal.pone.0222932

Puvanendran, D., Cece, Q., Picard, M., 2018. Reconstitution of the activity of RND efflux pumps: a “bottom-up” approach. Research in Microbiology, Special issue on Bacterial multidrug efflux pumps 169, 442–449. https://doi.org/10.1016/j.resmic.2017.11.004

Picard, M., Tikhonova, E.B., Broutin, I., Lu, S., Verchère, A., Zgurskaya, H.I., 2018. Biochemical Reconstitution and Characterization of Multicomponent Drug Efflux Transporters. Methods Mol. Biol. 1700, 113–145. https://doi.org/10.1007/978-1-4939-7454-2_8

Gomez-Zepeda, D., Chaves, C., Taghi, M., Sergent, P., Liu, W.-Q., Chhuon, C., Vidal, M., Picard, M., Thioulouse, E., Broutin, I., Guerrera, I.-C., Scherrmann, J.-M., Parmentier, Y., Decleves, X., Menet, M.-C., 2017. Targeted unlabeled MRM analysis of cell markers for the study of sample heterogeneity in isolated rat brain cortical microvessels. J. Neurochem. https://doi.org/10.1111/jnc.14095

Chaptal, V., Delolme, F., Kilburg, A., Magnard, S., Montigny, C., Picard, M., Prier, C., Monticelli, L., Bornert, O., Agez, M., Ravaud, S., Orelle, C., Wagner, R., Jawhari, A., Broutin, I., Pebay-Peyroula, E., Jault, J.-M., Kaback, H.R., le Maire, M., Falson, P., 2017. Quantification of Detergents Complexed with Membrane Proteins. Sci Rep 7, 41751. https://doi.org/10.1038/srep41751

Verchère, A., Broutin, I., Picard, M., 2017. Reconstitution of Membrane Proteins in Liposomes. Methods Mol. Biol. 1635, 259–282. https://doi.org/10.1007/978-1-4939-7151-0_14

Daury, L., Orange, F., Taveau, J.-C., Verchère, A., Monlezun, L., Gounou, C., Marreddy, R.K.R., Picard, M., Broutin, I., Pos, K.M., Lambert, O., 2016. Tripartite assembly of RND multidrug efflux pumps. Nature Communications 7, 10731. https://doi.org/10.1038/ncomms10731

Phan, G., Picard, M., Broutin, I., 2015. Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies. Antibiotics 4, 544–566. https://doi.org/10.3390/antibiotics4040544

Ntsogo Enguéné, V.Y., Verchère, A., Phan, G., Broutin, I., Picard, M., 2015. Catch me if you can: a biotinylated proteoliposome affinity assay for the investigation of assembly of the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa. Frontiers in Microbiology 6. https://doi.org/10.3389/fmicb.2015.00541

Monlezun, L., Phan, G., Benabdelhak, H., Lascombe, M.-B., Enguéné, V.Y.N., Picard, M., Broutin, I., 2015. New OprM structure highlighting the nature of the N-terminal anchor. Frontiers in Microbiology 6. https://doi.org/10.3389/fmicb.2015.00667

Verchère, A., Dezi, M., Adrien, V., Broutin, I., Picard, M., 2015. In vitro transport activity of the fully assembled MexAB-OprM efflux pump from Pseudomonas aeruginosa. Nature Communications 6, 6890. https://doi.org/10.1038/ncomms7890

Rayan, G., Adrien, V., Reffay, M., Picard, M., Ducruix, A., Schmutz, M., Urbach, W., Taulier, N., 2014. Surfactant Bilayers Maintain Transmembrane Protein Activity. Biophysical Journal 107, 1129–1135. https://doi.org/10.1016/j.bpj.2014.07.016

Ferrandez, Y., Dezi, M., Bosco, M., Urvoas, A., Valerio-Lepiniec, M., Le Bon, C., Giusti, F., Broutin, I., Durand, G., Polidori, A., Popot, J.-L., Picard, M., Minard, P., 2014. Amphipol-Mediated Screening of Molecular Orthoses Specific for Membrane Protein Targets. J. Membr. Biol. 247, 925–940. https://doi.org/10.1007/s00232-014-9707-3

Charvolin, D., Picard, M., Huang, L.-S., Berry, E.A., Popot, J.-L., 2014. Solution Behavior and Crystallization of Cytochrome bc 1 in the Presence of Amphipols. J. Membr. Biol. 247, 981–996. https://doi.org/10.1007/s00232-014-9694-4

Verchère, A., Dezi, M., Broutin, I., Picard, M., 2014. In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa. Journal of Visualized Experiments. https://doi.org/10.3791/50894

Verchère, A., Broutin, I., Picard, M., 2013. Hoechst likes to play hide and seek … use it with caution! Analytical Biochemistry 440, 117–119. https://doi.org/10.1016/j.ab.2013.05.019

Verchère, A., Dezi, M., Broutin, I., Picard, M., 2013. Investigation of an Efflux Pump Membrane Protein: A Roadmap. iConcept.

Verchère, A., Broutin, I., Picard, M., 2012. Photo-induced proton gradients for the in vitro investigation of bacterial efflux pumps. Scientific Reports 2. https://doi.org/10.1038/srep00306

Picard, M., Verchère, A., Broutin, I., 2012. Monitoring the active transport of efflux pumps after their reconstitution into proteoliposomes: Caveats and keys. Analytical Biochemistry 420, 194–196. https://doi.org/10.1016/j.ab.2011.09.025

Ferrandez, Y., Monlezun, L., Phan, G., Benabdelhak, H., Benas, P., Ulryck, N., Falson, P., Ducruix, A., Picard, M., Broutin, I., 2012. Stoichiometry of the MexA-OprM binding, as investigated by blue native gel electrophoresis: General. ELECTROPHORESIS 33, 1282–1287. https://doi.org/10.1002/elps.201100541

Wang, W., Monlezun, L., Picard, M., Benas, P., Français, O., Broutin, I., Le Pioufle, B., 2012. Activity monitoring of functional OprM using a biomimetic microfluidic device. The Analyst 137, 847. https://doi.org/10.1039/c2an16007b

Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L.J., Champeil, P., Charvolin, D., Cocco, M.J., Crémel, G., Dahmane, T., de la Maza, L.M., Ebel, C., Gabel, F., Giusti, F., Gohon, Y., Goormaghtigh, E., Guittet, E., Kleinschmidt, J.H., Kühlbrandt, W., Le Bon, C., Martinez, K.L., Picard, M., Pucci, B., Sachs, J.N., Tribet, C., van Heijenoort, C., Wien, F., Zito, F., Zoonens, M., 2011. Amphipols from A to Z. Annu Rev Biophys 40, 379–408. https://doi.org/10.1146/annurev-biophys-042910-155219

Phan, G., Benabdelhak, H., Lascombe, M.-B., Benas, P., Rety, S., Picard, M., Ducruix, A., Etchebest, C., Broutin, I., 2010. Structural and Dynamical Insights into the Opening Mechanism of P. aeruginosa OprM Channel. Structure 18, 507–517. https://doi.org/10.1016/j.str.2010.01.018

Picard, M., Duval-Terrié, C., Dé, E., Champeil, P., 2008. Stabilization of membranes upon interaction of amphipathic polymers with membrane proteins. Protein Science 13, 3056–3058. https://doi.org/10.1110/ps.04962104

Montigny, C., Picard, M., Lenoir, G., Gauron, C., Toyoshima, C., Champeil, P., 2007. Inhibitors Bound to Ca ²⁺$ -Free Sarcoplasmic Reticulum Ca ²⁺$ −ATPase Lock Its Transmembrane Region but Not Necessarily Its Cytosolic Region, Revealing the Flexibility of the Loops Connecting Transmembrane and Cytosolic Domains ^†$. Biochemistry 46, 15162–15174. https://doi.org/10.1021/bi701855r

Olesen, C., Picard, M., Winther, A.-M.L., Gyrup, C., Morth, J.P., Oxvig, C., Møller, J.V., Nissen, P., 2007. The structural basis of calcium transport by the calcium pump. Nature 450, 1036–1042. https://doi.org/10.1038/nature06418

Picard, M., Jensen, A.-M.L., Sørensen, T.L.-M., Champeil, P., Møller, J.V., Nissen, P., 2007. Ca2+ versus Mg2+ Coordination at the Nucleotide-binding site of the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Molecular Biology 368, 1–7. https://doi.org/10.1016/j.jmb.2007.01.082

Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L., Champeil, P., 2006. Protective and inhibitory effects of various types of amphipols on the Ca2+-ATPase from sarcoplasmic reticulum: a comparative study. Biochemistry 45, 1861–1869. https://doi.org/10.1021/bi051954a

Picard, M., Toyoshima, C., Champeil, P., 2006. Effects of Inhibitors on Luminal Opening of Ca2+ Binding Sites in an E2P-like Complex of Sarcoplasmic Reticulum Ca22+-ATPase with Be22+-fluoride. Journal of Biological Chemistry 281, 3360–3369. https://doi.org/10.1074/jbc.M511385200

Lenoir, G., Jaxel, C., Picard, M., le Maire, M., Champeil, P., Falson, P., 2006. Conformational Changes in Sarcoplasmic Reticulum Ca ²⁺$ -ATPase Mutants: Effect of Mutations either at Ca ²⁺$ -Binding Site II or at Tryptophan 552 in the Cytosolic Domain ^†$. Biochemistry 45, 5261–5270. https://doi.org/10.1021/bi0522091

Picard, M., Toyoshima, C., Champeil, P., 2005. The Average Conformation at Micromolar [Ca2+] of Ca2+-ATPase with Bound Nucleotide Differs from That Adopted with the Transition State Analog ADP{middle dot}AlFx or with AMPPCP under Crystallization Conditions at Millimolar [Ca2+]. Journal of Biological Chemistry 280, 18745–18754. https://doi.org/10.1074/jbc.M501596200

Lenoir, G., Picard, M., Gauron, C., Montigny, C., Le Marechal, P., Falson, P., le Maire, M., Moller, J.V., Champeil, P., 2004. Functional Properties of Sarcoplasmic Reticulum Ca2+-ATPase after Proteolytic Cleavage at Leu119-Lys120, Close to the A-domain. Journal of Biological Chemistry 279, 9156–9166. https://doi.org/10.1074/jbc.M311411200

Lenoir, G., Picard, M., Moller, J.V., le Maire, M., Champeil, P., Falson, P., 2004. Involvement of the L6-7 Loop in SERCA1a Ca2+-ATPase Activation by Ca2+ (or Sr2+) and ATP. Journal of Biological Chemistry 279, 32125–32133. https://doi.org/10.1074/jbc.M402934200