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2024

Zuniga, D., Zoumpoulakis, A., Veloso, R.F., Peverini, L., Shi, S., Pozza, A., Kugler, V., Bonneté, F., Bouceba, T., Wagner, R., Corringer, P.-J., Fernandes, C.A.H., Vénien-Bryan, C., 2024. Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndrome. The FASEB Journal 38, e70146. https://doi.org/10.1096/fj.202401567R
Zuniga, D., Zoumpoulakis, A., Veloso, R.F., Peverini, L., Shi, S., Pozza, A., Kugler, V., Bonneté, F., Bouceba, T., Wagner, R., Corringer, P.-J., Fernandes, C.A.H., Vénien-Bryan, C., 2024. Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndrome. https://doi.org/10.1101/2024.02.09.579451
Zinke, M., Lejeune, M., Mechaly, A., Bardiaux, B., Boneca, I.G., Delepelaire, P., Izadi-Pruneyre, N., 2024. Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake. Nat Commun 15, 331. https://doi.org/10.1038/s41467-023-44606-z
Saade, C., Pozza, A., Bonnete, F., Finet, S., Lutz-Bueno, V., Tully, M.D., Varela, P.F., Lacapere, J.-J., Combet, S., 2024. Enhanced structure/function of mTSPO translocator in lipid:surfactant mixed micelles. Biochimie S0300-9084(24)00083-X. https://doi.org/10.1016/j.biochi.2024.04.008
Riché, A., Dumas, L., Malesinski, S., Bossan, G., Madigou, C., Zito, F., Alric, J., 2024. The stromal side of the cytochrome b6f complex regulates state transitions. Plant Cell koae190. https://doi.org/10.1093/plcell/koae190
Mégret-Cavalier, M., Pozza, A., Cece, Q., Bonneté, F., Broutin, I., Phan, G., 2024. Starting with an Integral Membrane Protein Project for Structural Biology: Production, Purification, Detergent Quantification, and Buffer Optimization—Case Study of the Exporter CntI from Pseudomonas aeruginosa, in: Journet, L., Cascales, E. (Eds.), Bacterial Secretion Systems : Methods and Protocols, Methods in Molecular Biology. Springer US, New York, NY, pp. 415–430. https://doi.org/10.1007/978-1-0716-3445-5_26
Desgranges, S., Lacanau, V., Bonneté, F., Soulié, M., Bihel, F., Bourgeois, D., Contino-Pépin, C., 2024. Synthesis, Characterization, and Self-Assembling Properties of New Amphiphilic Dendrons Bearing Branched TRIS-Derived Oligomers as Polar Head Groups. Macromolecules. https://doi.org/10.1021/acs.macromol.3c02388
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

2023

Pozza, A., Bonneté, F., 2023. Analysis and modeling of SDS and DPC micelle SAXS data for membrane protein solution structure characterization. Data in Brief 47, 108915. https://doi.org/10.1016/j.dib.2023.108915
Picard, M., 2023. Membrane proteins. Biochimie, Membranes Proteins 205, 1–2. https://doi.org/10.1016/j.biochi.2023.01.018
Michon, B., López-Sánchez, U., Degrouard, J., Nury, H., Leforestier, A., Rio, E., Salonen, A., Zoonens, M., 2023. Role of surfactants in electron cryo-microscopy film preparation. Biophysical Journal 122, 1846–1857. https://doi.org/10.1016/j.bpj.2023.04.016
Gagelin, A., Largeau, C., Masscheleyn, S., Piel, M.S., Calderón-Mora, D., Bouillaud, F., Hénin, J., Miroux, B., 2023. Molecular determinants of inhibition of UCP1-mediated respiratory uncoupling. Nat Commun 14, 2594. https://doi.org/10.1038/s41467-023-38219-9
Combet, S., Bonneté, F., Finet, S., Pozza, A., Saade, C., Martel, A., Koutsioubas, A., Lacapère, J.-J., 2023. Effect of amphiphilic environment on the solution structure of mouse TSPO translocator protein. Biochimie, Membranes Proteins 205, 61–72. https://doi.org/10.1016/j.biochi.2022.11.014
Biou, V., 2023. Lipid-membrane protein interaction visualised by cryo-EM: A review. Biochimica et Biophysica Acta (BBA) - Biomembranes 1865, 184068. https://doi.org/10.1016/j.bbamem.2022.184068
Banères, J.-L., Botzanowski, T., Boutin, J.A., Calamini, B., Castel, J., Catoire, L.J., Cianférani, S., Demesmay, C., Ferguson, G., Ferry, G., Kniazeff, J., Krimm, I., Langer, T., Lebon, G., Ley, M., Nyerges, M., Schwob, M., Venien-Bryan, C., Wagner, R., Zeder-Lutz, G., Zilian-Stohrer, C., 2023. Biophysical Dissection of Isolated GPCRs: The Adenosine A2A Receptor under the Bistouries. Receptors 2, 47–92. https://doi.org/10.3390/receptors2010004

2022

Royes, J., Talbot, P., Le Bon, C., Moncoq, K., Uzan, M., Zito, F., Miroux, B., 2022. Membrane Protein Production in Escherichia coli: Protocols and Rules. Methods Mol Biol 2507, 19–39. https://doi.org/10.1007/978-1-0716-2368-8_2
Pozza, A., Giraud, F., Cece, Q., Casiraghi, M., Point, E., Damian, M., Le Bon, C., Moncoq, K., Banères, J.-L., Lescop, E., Catoire, L.J., 2022. Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure. Nat Commun 13, 1780. https://doi.org/10.1038/s41467-022-29410-5
Marconnet, A., Michon, B., Prost, B., Solgadi, A., Le Bon, C., Giusti, F., Tribet, C., Zoonens, M., 2022. Influence of Hydrophobic Groups Attached to Amphipathic Polymers on the Solubilization of Membrane Proteins along with Their Lipids. Anal Chem 94, 14151–14158. https://doi.org/10.1021/acs.analchem.2c01746
Makamte, S., Thureau, A., Jabrani, A., Paquelin, A., Plessis, A., Sanial, M., Rudenko, O., Oteri, F., Baaden, M., Biou, V., 2022. A large disordered region confers a wide spanning volume to vertebrate Suppressor of Fused as shown in a trans-species solution study. J Struct Biol 214, 107853. https://doi.org/10.1016/j.jsb.2022.107853
Gagelin, A., Largeau, C., Masscheleyn, S., Piel, M.S., Calderon-Mora, D., Bouillaud, F., Hénin, J., Miroux, B., 2022. Molecular determinants of inhibition of UCP1-mediated respiratory uncoupling. https://doi.org/10.1101/2022.12.09.516457
Combet, S., Bonneté, F., Finet, S., Pozza, A., Saade, C., Martel, A., Koutsioubas, A., Lacapère, J.-J., 2022. Effect of amphiphilic environment on the solution structure of mouse TSPO translocator protein. Biochimie. https://doi.org/10.1016/j.biochi.2022.11.014
Bouillaud, F., Miroux, B., 2022. Les protéines découplantes UCP1-3, entre bioénergétique et métabolisme. Médecine des Maladies Métaboliques, Le tissu adipeux brun 16, 677–688. https://doi.org/10.1016/j.mmm.2022.10.003
Biou, V., Adaixo, R.J.D., Chami, M., Coureux, P.-D., Laurent, B., Enguéné, V.Y.N., de Amorim, G.C., Izadi-Pruneyre, N., Malosse, C., Chamot-Rooke, J., Stahlberg, H., Delepelaire, P., 2022. Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog. Commun Biol 5, 355. https://doi.org/10.1038/s42003-022-03306-y
Biou, V., 2022. Lipid-membrane protein interaction visualised by cryo-EM: A review. Biochimica et biophysica acta. Biomembranes 1865, 184068. https://doi.org/10.1016/j.bbamem.2022.184068
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

2021

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
Somboon, K., Melling, O., Lejeune, M., Pinheiro, G.M.S., Paquelin, A., Bardiaux, B., Nilges, M., Delepelaire, P., Khalid, S., Izadi-Pruneyre, N., 2021. Interaction of the TonB dependent transporter HasR with its cognate TonB-like protein HasB in a membrane environment. bioRxiv 2021.04.21.440789. https://doi.org/10.1101/2021.04.21.440789v1
Piel, M.S., Masscheleyn, S., Bouillaud, F., Moncoq, K., Miroux, B., 2021. Structural models of mitochondrial uncoupling proteins obtained in DPC micelles are not functionally relevant. FEBS J 288, 3024–3033. https://doi.org/10.1111/febs.15629
Ouldali, M., Moncoq, K., de la Valette, A. de la C., Arteni, A.A., Betton, J.-M., Lepault, J., 2021. Study of membrane deformations induced by Hepatitis C protein NS4B and its terminal amphipathic peptides. Biochim Biophys Acta Biomembr 1863, 183537. https://doi.org/10.1016/j.bbamem.2020.183537
Makamte, S., Jabrani, A., Paquelin, A., Plessis, A., Sanial, M., Thureau, A., Rudenko, O., Oteri, F., Baaden, M., Biou, V., 2021. A large disordered region confers a wide spanning volume to vertebrate Suppressor of Fused as shown in a trans-species solution study. bioRxiv 2021.06.14.447554. https://doi.org/10.1101/2021.06.14.447554v1
Louet, M., Casiraghi, M., Damian, M., Costa, M.G., Renault, P., Gomes, A.A., Batista, P.R., M’Kadmi, C., Mary, S., Cantel, S., Denoyelle, S., Ben Haj Salah, K., Perahia, D., Bisch, P.M., Fehrentz, J.-A., Catoire, L.J., Floquet, N., Banères, J.-L., 2021. Concerted conformational dynamics and water movements in the ghrelin G protein-coupled receptor. eLife 10, e63201. https://doi.org/10.7554/eLife.63201
Le Bon, C., Michon, B., Popot, J.-L., Zoonens, M., 2021. Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy. Q Rev Biophys 54, e6. https://doi.org/10.1017/S0033583521000044
Labarre, C., Dautin, N., Grzegorzewicz, A., Jackson, M., McNeil, M., Mohiman, N., Sago, L., Bayan, N., 2021. S16 and T18 mannosylation sites of LppX are not essential for its activity in phthiocerol dimycocerosates localization at the surface of Mycobacterium tuberculosis. Res Microbiol 103874. https://doi.org/10.1016/j.resmic.2021.103874
Higgins, A.J., Flynn, A.J., Marconnet, A., Musgrove, L.J., Postis, V.L.G., Lippiat, J.D., Chung, C.-W., Ceska, T., Zoonens, M., Sobott, F., Muench, S.P., 2021. Cycloalkane-modified amphiphilic polymers provide direct extraction of membrane proteins for CryoEM analysis. Commun Biol 4, 1337. https://doi.org/10.1038/s42003-021-02834-3
Dautin, N., 2021. Folding Control in the Path of Type 5 Secretion. Toxins 13, 341. https://doi.org/10.3390/toxins13050341
Damian, M., Louet, M., Gomes, A.A.S., M’Kadmi, C., Denoyelle, S., Cantel, S., Mary, S., Bisch, P.M., Fehrentz, J.-A., Catoire, L.J., Floquet, N., Banères, J.-L., 2021. Allosteric modulation of ghrelin receptor signaling by lipids. Nat Commun 12, 3938. https://doi.org/10.1038/s41467-021-23756-y
Clénet, D., Clavier, L., Strobbe, B., Bon, C.L., Zoonens, M., Saulnier, A., 2021. Full-length G glycoprotein directly extracted from rabies virus with detergent and then stabilized by amphipols in liquid and freeze-dried forms. Biotechnology and Bioengineering n/a. https://doi.org/10.1002/bit.27900
Biou, V., Adaixo, R.J.D., Chami, M., Coureux, P.-D., Laurent, B., Ntsogo, Y., Amorim, G.C. de, Izadi-Pruneyre, N., Malosse, C., Chamot-Rooke, J., Stahlberg, H., Delepelaire, P., 2021. Functional and structural characterization of Serratia marcescens ExbB: determinants of the interaction with HasB/TonB. bioRxiv 2021.04.21.440815. https://doi.org/10.1101/2021.04.21.440815v1
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
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
Abel, S., Marchi, M., Solier, J., Finet, S., Brillet, K., Bonneté, F., 2021. Structural insights into the membrane receptor ShuA in DDM micelles and in a model of gram-negative bacteria outer membrane as seen by SAXS and MD simulations. Biochim Biophys Acta Biomembr 1863, 183504. https://doi.org/10.1016/j.bbamem.2020.183504

2020

Yan, X., Noël, F., Marcotte, I., DeWolf, C.E., Warschawski, D.E., Boisselier, E., 2020. AHNAK C-Terminal Peptide Membrane Binding-Interactions between the Residues 5654-5673 of AHNAK and Phospholipid Monolayers and Bilayers. Langmuir 36, 362–369. https://doi.org/10.1021/acs.langmuir.9b02973
Tifrea, D.F., Pal, S., le Bon, C., Cocco, M.J., Zoonens, M., de la Maza, L.M., 2020. Improved protection against Chlamydia muridarum using the native major outer membrane protein trapped in Resiquimod-carrying amphipols and effects in protection with addition of a Th1 (CpG-1826) and a Th2 (Montanide ISA 720) adjuvant. Vaccine. https://doi.org/10.1016/j.vaccine.2020.04.065
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
Signetti, L., Elizarov, N., Simsir, M., Paquet, A., Douguet, D., Labbal, F., Debayle, D., Di Giorgio, A., Biou, V., Girard, C., Duca, M., Bretillon, L., Bertolotto, C., Verrier, B., Azoulay, S., Mus-Veteau, I., 2020. Inhibition of Patched Drug Efflux Increases Vemurafenib Effectiveness against Resistant BrafV600E Melanoma. Cancers (Basel) 12. https://doi.org/10.3390/cancers12061500
Royes, J., Biou, V., Dautin, N., Tribet, C., Miroux, B., 2020. Inducible intracellular membranes: molecular aspects and emerging applications. Microb. Cell Fact. 19, 176. https://doi.org/10.1186/s12934-020-01433-x
Robescu, M.S., Rubini, R., Beneventi, E., Tavanti, M., Lonigro, C., Zito, F., Filippini, F., Cendron, L., Bergantino, E., 2020. From the Amelioration of a NADP+-dependent Formate Dehydrogenase to the Discovery of a New Enzyme: Round Trip from Theory to Practice. ChemCatChem 12, 2478–2487. https://doi.org/10.1002/cctc.201902089
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
Piel, M.S., Masscheleyn, S., Bouillaud, F., Moncoq, K., Miroux, B., 2020. Structural models of mitochondrial uncoupling proteins obtained in DPC micelles are not physiologically relevant for their uncoupling activity. bioRxiv 2020.07.20.195602. https://doi.org/10.1101/2020.07.20.195602
Marconnet, A., Michon, B., Le Bon, C., Giusti, F., Tribet, C., Zoonens, M., 2020. Solubilization and stabilization of membrane proteins by cycloalkane-modified amphiphilic polymers. Biomacromolecules. https://doi.org/10.1021/acs.biomac.0c00929
Lacanau, V., Bonneté, F., Wagner, P., Schmitt, M., Meyer, D., Bihel, F., Contino-Pépin, C., Bourgeois, D., 2020. From Electronic Waste to Suzuki-Miyaura Cross-Coupling Reaction in Water: Direct Valuation of Recycled Palladium in Catalysis. ChemSusChem. https://doi.org/10.1002/cssc.202001155
Gravel, A.E., Arnold, A.A., Fillion, M., Auger, M., Warschawski, D.E., Marcotte, I., 2020. Magnetically-orientable Tween-based model membranes for NMR studies of proteins. Biochim Biophys Acta Biomembr 183379. https://doi.org/10.1016/j.bbamem.2020.183379
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
Giusti, F., Casiraghi, M., Point, E., Damian, M., Rieger, J., Bon, C.L., Pozza, A., Moncoq, K., Banères, J.-L., Catoire, L.J., 2020. Structure of the agonist 12-HHT in its BLT2 receptor-bound state. Sci Rep 10, 2630. https://doi.org/10.1038/s41598-020-59571-6
Exner, T.E., Becker, Stefanie, Becker, Simon, Boniface-Guiraud, A., Delepelaire, P., Diederichs, K., Welte, W., 2020. Binding of HasA by its transmembrane receptor HasR follows a conformational funnel mechanism. Eur. Biophys. J. 49, 39–57. https://doi.org/10.1007/s00249-019-01411-1
Dietrich, C., Li de la Sierra-Gallay, I., Masi, M., Girard, E., Dautin, N., Constantinesco-Becker, F., Tropis, M., Daffé, M., van Tilbeurgh, H., Bayan, N., 2020. The C-terminal domain of Corynebacterium glutamicum mycoloyltransferase A is composed of five repeated motifs involved in cell wall binding and stability. Mol. Microbiol. https://doi.org/10.1111/mmi.14492
Dautin, N., Argentini, M., Mohiman, N., Labarre, C., Cornu, D., Sago, L., Chami, M., Dietrich, C., de Sousa d’Auria, C., Houssin, C., Masi, M., Salmeron, C., Bayan, N., 2020. Role of the unique, non-essential phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) in Corynebacterium glutamicum. Microbiology (Reading) 166, 759–776. https://doi.org/10.1099/mic.0.000937
Bosco, M., Damian, M., Chauhan, V., Roche, M., Guillet, P., Fehrentz, J.-A., Bonneté, F., Polidori, A., Banères, J.-L., Durand, G., 2020. Biotinylated non-ionic amphipols for GPCR ligands screening. Methods 180, 69–78. https://doi.org/10.1016/j.ymeth.2020.06.001
Bosco, M., Damian, M., Chauhan, V., Roche, M., Guillet, P., Fehrentz, J.-A., Bonneté, F., Polidori, A., Banères, J.-L., Durand, G., 2020. Biotinylated non-ionic amphipols for GPCR Ligands Screening. Methods. https://doi.org/10.1016/j.ymeth.2020.06.001

2019

Royes, J., Ilioaia, O., Lubart, Q., Angius, F., Dubacheva, G.V., Bally, M., Miroux, B., Tribet, C., 2019. Bacteria-Based Production of Thiol-Clickable, Genetically Encoded Lipid Nanovesicles. Angew. Chem. Int. Ed. Engl. 58, 7395–7399. https://doi.org/10.1002/anie.201902929
Romoli, O., Mukherjee, S., Mohid, S.A., Dutta, A., Montali, A., Franzolin, E., Brady, D., Zito, F., Bergantino, E., Rampazzo, C., Tettamanti, G., Bhunia, A., Sandrelli, F., 2019. Enhanced Silkworm Cecropin B Antimicrobial Activity against Pseudomonas aeruginosa from Single Amino Acid Variation. ACS Infect Dis 5, 1200–1213. https://doi.org/10.1021/acsinfecdis.9b00042
Petrella, S., Capton, E., Raynal, B., Giffard, C., Thureau, A., Bonneté, F., Alzari, P.M., Aubry, A., Mayer, C., 2019. Overall Structures of Mycobacterium tuberculosis DNA Gyrase Reveal the Role of a Corynebacteriales GyrB-Specific Insert in ATPase Activity. Structure 27, 579-589.e5. https://doi.org/10.1016/j.str.2019.01.004
Perry, T.N., Souabni, H., Rapisarda, C., Fronzes, R., Giusti, F., Popot, J.-L., Zoonens, M., Gubellini, F., 2019. BAmSA: Visualising transmembrane regions in protein complexes using biotinylated amphipols and electron microscopy. Biochim Biophys Acta Biomembr 1861, 466–477. https://doi.org/10.1016/j.bbamem.2018.11.004
Nawrocki, W.J., Bailleul, B., Picot, D., Cardol, P., Rappaport, F., Wollman, F.-A., Joliot, P., 2019. The mechanism of cyclic electron flow. Biochim Biophys Acta Bioenerg 1860, 433–438. https://doi.org/10.1016/j.bbabio.2018.12.005
Kanonenberg, K., Royes, J., Kedrov, A., Poschmann, G., Angius, F., Solgadi, A., Spitz, O., Kleinschrodt, D., Stühler, K., Miroux, B., Schmitt, L., 2019. Shaping the lipid composition of bacterial membranes for membrane protein production. Microb. Cell Fact. 18, 131. https://doi.org/10.1186/s12934-019-1182-1
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
Delepelaire, P., 2019. Bacterial ABC transporters of iron containing compounds. Res. Microbiol. 170, 345–357. https://doi.org/10.1016/j.resmic.2019.10.008
de la Fuente-Herreruela, D., Monnappa, A.K., Muñoz-Úbeda, M., Morallón-Piña, A., Enciso, E., Sánchez, L., Giusti, F., Natale, P., López-Montero, I., 2019. Lipid–peptide bioconjugation through pyridyl disulfide reaction chemistry and its application in cell targeting and drug delivery. Journal of Nanobiotechnology 17, 77. https://doi.org/10.1186/s12951-019-0509-8
Dauvergne, J., Desuzinges, E.M., Faugier, C., Igonet, S., Soulié, M., Grousson, E., Cornut, D., Bonneté, F., Durand, G., Dejean, E., Jawhari, A., 2019. Glycosylated Amphiphilic Calixarene-Based Detergent for Functional Stabilization of Native Membrane Proteins. ChemistrySelect 4, 5535–5539. https://doi.org/10.1002/slct.201901220
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
Casiraghi, M., Point, E., Pozza, A., Moncoq, K., Banères, J.-L., Catoire, L.J., 2019. NMR analysis of GPCR conformational landscapes and dynamics. Mol. Cell. Endocrinol. 484, 69–77. https://doi.org/10.1016/j.mce.2018.12.019
Bouhlel, Z., Arnold, A.A., Warschawski, D.E., Lemarchand, K., Tremblay, R., Marcotte, I., 2019. Labelling strategy and membrane characterization of marine bacteria Vibrio splendidus by in vivo2H NMR. Biochim Biophys Acta Biomembr 1861, 871–878. https://doi.org/10.1016/j.bbamem.2019.01.018

2018

Warschawski, D.E., Arnold, A.A., Marcotte, I., 2018. A New Method of Assessing Lipid Mixtures by 31P Magic-Angle Spinning NMR. Biophysical Journal 114, 1368–1376. https://doi.org/10.1016/j.bpj.2018.01.025
Tifrea, D.F., Pal, S., Le Bon, C., Giusti, F., Popot, J.-L., Cocco, M.J., Zoonens, M., de la Maza, L.M., 2018. Co-delivery of amphipol-conjugated adjuvant with antigen, and adjuvant combinations, enhance immune protection elicited by a membrane protein-based vaccine against a mucosal challenge with Chlamydia. Vaccine 36, 6640–6649. https://doi.org/10.1016/j.vaccine.2018.09.055
Serra-Batiste, M., Tolchard, J., Giusti, F., Zoonens, M., Carulla, N., 2018. Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer’s Disease. Front Mol Biosci 5, 38. https://doi.org/10.3389/fmolb.2018.00038
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
Poulhazan, A., Arnold, A.A., Warschawski, D.E., Marcotte, I., 2018. Unambiguous Ex Situ and in Cell 2D 13C Solid-State NMR Characterization of Starch and Its Constituents. Int J Mol Sci 19. https://doi.org/10.3390/ijms19123817
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
Le Bon, C., Marconnet, A., Masscheleyn, S., Popot, J.-L., Zoonens, M., 2018. Folding and stabilizing membrane proteins in amphipol A8-35. Methods 147, 95–105. https://doi.org/10.1016/j.ymeth.2018.04.012
Dumas, L., Zito, F., Auroy, P., Johnson, X., Peltier, G., Alric, J., 2018. Structure-function analysis of chloroplast proteins via random mutagenesis using error-prone PCR. Plant Physiology 177, 465–475. https://doi.org/10.1104/pp.17.01618
Dilworth, M.V., Piel, M.S., Bettaney, K.E., Ma, P., Luo, J., Sharples, D., Poyner, D.R., Gross, S.R., Moncoq, K., J F Henderson, P., Miroux, B., Bill, R.M., 2018. Microbial expression systems for membrane proteins. Methods 147, 3–39. https://doi.org/10.1016/j.ymeth.2018.04.009
Corey, R.A., Pyle, E., Allen, W.J., Watkins, D.W., Casiraghi, M., Miroux, B., Arechaga, I., Politis, A., Collinson, I., 2018. Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion. Proc. Natl. Acad. Sci. U.S.A. 115, 7967–7972. https://doi.org/10.1073/pnas.1721536115
Chipot, C., Dehez, F., Schnell, J.R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L.J., Miroux, B., Kunji, E.R.S., Veglia, G., Cross, T.A., Schanda, P., 2018. Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies. Chem. Rev. 118, 3559–3607. https://doi.org/10.1021/acs.chemrev.7b00570
Casiraghi, M., Damian, M., Lescop, E., Baneres, J.-L., Catoire, L.J., 2018. Illuminating the energy landscape of GPCRs: the key contribution of solution-state NMR associated with Escherichia coli as an expression host. Biochemistry 57, 2297–2307. https://doi.org/10.1021/acs.biochem.8b00035
Azar, E., Constantin, D., Warschawski, D.E., 2018. The effect of gramicidin inclusions on the local order of membrane components. Eur Phys J E Soft Matter 41, 44. https://doi.org/10.1140/epje/i2018-11644-5
Arnold, A.A., Bourgouin, J.-P., Genard, B., Warschawski, D.E., Tremblay, R., Marcotte, I., 2018. Whole cell solid-state NMR study of Chlamydomonas reinhardtii microalgae. J. Biomol. NMR 70, 123–131. https://doi.org/10.1007/s10858-018-0164-7
Angius, F., Ilioaia, O., Amrani, A., Suisse, A., Rosset, L., Legrand, A., Abou-Hamdan, A., Uzan, M., Zito, F., Miroux, B., 2018. A novel regulation mechanism of the T7 RNA polymerase based expression system improves overproduction and folding of membrane proteins. Sci Rep 8, 8572. https://doi.org/10.1038/s41598-018-26668-y

2017

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
Jabrani, A., Makamte, S., Moreau, E., Gharbi, Y., Plessis, A., Bruzzone, L., Sanial, M., Biou, V., 2017. Biophysical characterisation of the novel zinc binding property in Suppressor of Fused. Scientific Reports 7, 11139. https://doi.org/10.1038/s41598-017-11203-2
Hirose, M., Schilf, P., Rohde, S., Gupta, Y., Sancerni, T., Alves-Guerra, M.-C., Sina, C., Jaster, R., Miroux, B., Ibrahim, S.M., 2017. The mitochondrial uncoupling protein 2 gene is causal for the spontaneous polycystic liver diseases in mice. Mitochondrion. https://doi.org/10.1016/j.mito.2017.10.011
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
Fu, H.-Y., Picot, D., Choquet, Y., Longatte, G., Sayegh, A., Delacotte, J., Guille-Collignon, M., Lemaître, F., Rappaport, F., Wollman, F.-A., 2017. Redesigning the QA binding site of Photosystem II allows reduction of exogenous quinones. Nat Commun 8, 15274. https://doi.org/10.1038/ncomms15274
Dumas, L., Zito, F., Blangy, S., Auroy, P., Johnson, X., Peltier, G., Alric, J., 2017. A stromal region of cytochrome b6f subunit IV is involved in the activation of the Stt7 kinase in Chlamydomonas. PNAS 201713343. https://doi.org/10.1073/pnas.1713343114
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
Casiraghi, M., Banères, J.-L., Catoire, L.J., 2017. NMR Spectroscopy for the Characterization of GPCR Energy Landscapes, in: SpringerLink, Topics in Medicinal Chemistry. Springer, Berlin, Heidelberg, pp. 1–26. https://doi.org/10.1007/7355_2017_31
Carranza, G., Angius, F., Ilioaia, O., Solgadi, A., Miroux, B., Arechaga, I., 2017. Cardiolipin plays an essential role in the formation of intracellular membranes in Escherichia coli. Biochim. Biophys. Acta 1859, 1124–1132. https://doi.org/10.1016/j.bbamem.2017.03.006
Bouillaud, F., Casteilla, L., Klaus, S., Miroux, B., 2017. Editorial. Biochimie 134, 1–2. https://doi.org/10.1016/j.biochi.2017.01.012
Booth, V., Warschawski, D.E., Santisteban, N.P., Laadhari, M., Marcotte, I., 2017. Recent progress on the application of (2)H solid-state NMR to probe the interaction of antimicrobial peptides with intact bacteria. Biochim. Biophys. Acta. https://doi.org/10.1016/j.bbapap.2017.07.018

2016

Zito, F., Alric, J., 2016. Heme ci or cn of the Cytochrome b6f Complex, A Short Retrospective, in: Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling, Advances in Photosynthesis and Respiration. Springer, Dordrecht, pp. 295–306. https://doi.org/10.1007/978-94-017-7481-9_15
Zito, F., 2016. Silent or Not Silent? Consequences of the Human mt-cyb Polymorphism. Hum. Mutat. 37, 833. https://doi.org/10.1002/humu.22885
Zambolin, S., Clantin, B., Chami, M., Hoos, S., Haouz, A., Villeret, V., Delepelaire, P., 2016. Structural basis for haem piracy from host haemopexin by Haemophilus influenzae. Nat Commun 7, 11590. https://doi.org/10.1038/ncomms11590
Wojtowicz, H., Prochnicka-Chalufour, A., Cardoso de Amorim, G., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G., Gubellini, F., Koutsioubas, A., Perez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N., 2016. Structural basis of the signaling through a bacterial membrane receptor HasR deciphered by an integrative approach. Biochem. J. https://doi.org/10.1042/BCJ20160131
Warnet, X.L., Laadhari, M., Arnold, A.A., Marcotte, I., Warschawski, D.E., 2016. A (2)H magic-angle spinning solid-state NMR characterisation of lipid membranes in intact bacteria. Biochim. Biophys. Acta 1858, 146–152. https://doi.org/10.1016/j.bbamem.2015.10.020
Popot, J.-L., Engelman, D.M., 2016. Membranes Do Not Tell Proteins How To Fold. Biochemistry 55, 5–18. https://doi.org/10.1021/acs.biochem.5b01134
Plamont, M.-A., Billon-Denis, E., Maurin, S., Gauron, C., Pimenta, F.M., Specht, C.G., Shi, J., Quérard, J., Pan, B., Rossignol, J., Moncoq, K., Morellet, N., Volovitch, M., Lescop, E., Chen, Y., Triller, A., Vriz, S., Le Saux, T., Jullien, L., Gautier, A., 2016. Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo. Proc. Natl. Acad. Sci. U.S.A. 113, 497–502. https://doi.org/10.1073/pnas.1513094113
Hirose, M., Schilf, P., Lange, F., Mayer, J., Reichart, G., Maity, P., Jöhren, O., Schwaninger, M., Scharffetter-Kochanek, K., Sina, C., Sadik, C.D., Köhling, R., Miroux, B., Ibrahim, S.M., 2016. Uncoupling protein 2 protects mice from aging. Mitochondrion 30, 42–50. https://doi.org/10.1016/j.mito.2016.06.004
Casiraghi, M., Damian, M., Lescop, E., Point, E., Moncoq, K., Morellet, N., Levy, D., Marie, J., Guittet, E., Banères, J.-L., Catoire, L.J., 2016. Functional Modulation of a G Protein-Coupled Receptor Conformational Landscape in a Lipid Bilayer. J. Am. Chem. Soc. 138, 11170–11175. https://doi.org/10.1021/jacs.6b04432
Bergdoll, L., Ten Brink, F., Nitschke, W., Picot, D., Baymann, F., 2016. From low- to high-potential bioenergetic chains: Thermodynamic constraints of Q-cycle function. Biochim. Biophys. Acta 1857, 1569–1579. https://doi.org/10.1016/j.bbabio.2016.06.006
Beaugrand, M., Arnold, A.A., Juneau, A., Gambaro, A.B., Warschawski, D.E., Williamson, P.T.F., Marcotte, I., 2016. Magnetically Oriented Bicelles with Monoalkylphosphocholines: Versatile Membrane Mimetics for Nuclear Magnetic Resonance Applications. Langmuir 32, 13244–13251. https://doi.org/10.1021/acs.langmuir.6b03099
Angius, F., Ilioaia, O., Uzan, M., Miroux, B., 2016. Membrane Protein Production in Escherichia coli: Protocols and Rules, in: Mus-Veteau, I. (Ed.), Heterologous Expression of Membrane Proteins. Springer New York, New York, NY, pp. 37–52.

2015

Watkinson, T.G., Calabrese, A.N., Giusti, F., Zoonens, M., Radford, S.E., Ashcroft, A.E., 2015. Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry. International Journal of Mass Spectrometry 391, 54–61. https://doi.org/10.1016/j.ijms.2015.06.017
Warnet, X.L., Arnold, A.A., Marcotte, I., Warschawski, D.E., 2015. In-Cell Solid-State NMR: An Emerging Technique for the Study of Biological Membranes. Biophysical Journal 109, 2461–2466. https://doi.org/10.1016/j.bpj.2015.10.041
Mora, L., Moncoq, K., England, P., Oberto, J., de Zamaroczy, M., 2015. The Stable Interaction Between Signal Peptidase LepB of Escherichia coli and Nuclease Bacteriocins Promotes Toxin Entry into the Cytoplasm. J. Biol. Chem. 290, 30783–30796. https://doi.org/10.1074/jbc.M115.691907
Miroux, B., Pebay-Peyroula, E., 2015. Editorial overview: Membranes. Current Opinion in Structural Biology 33, vii–ix. https://doi.org/10.1016/j.sbi.2015.09.006
Hattab, G., Warschawski, D.E., Moncoq, K., Miroux, B., 2015. Escherichia coli as host for membrane protein structure determination: a global analysis. Sci Rep 5, 12097. https://doi.org/10.1038/srep12097
Giusti, F., Kessler, P., Westh Hansen, R., Della Pia, E.A., Le Bon, C., Mourier, G., Popot, J.-L., Martinez, K.L., Zoonens, M., 2015. Synthesis of a Polyhistidine-bearing Amphipol and its Use for Immobilizing Membrane Proteins. Biomacromolecules. https://doi.org/10.1021/acs.biomac.5b01010
Giraud, P., Créchet, J.-B., Uzan, M., Bontems, F., Sizun, C., 2015. Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1. Biomol NMR Assign 9, 107–111. https://doi.org/10.1007/s12104-014-9554-2
Delepelaire, P., Izadi-Pruneyre, N., Delepierre, M., Ghigo, J.-M., Schwartz, M., 2015. A tribute to Cécile Wandersman. Res. Microbiol. 166, 393–398.
Arnold, A.A., Genard, B., Zito, F., Tremblay, R., Warschawski, D.E., Marcotte, I., 2015. Identification of lipid and saccharide constituents of whole microalgal cells by 13C solid-state NMR. Biochim. Biophys. Acta 1848, 369–377. https://doi.org/10.1016/j.bbamem.2014.07.017