Preprints or postprints of articles can also be found on HAL.


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.
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.
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.
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.
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.
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.
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.
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.
Dautin, N., 2021. Folding Control in the Path of Type 5 Secretion. Toxins 13, 341.
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.
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.
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.
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.
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.


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.
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.
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.
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.
Royes, J., Biou, V., Dautin, N., Tribet, C., Miroux, B., 2020. Inducible intracellular membranes: molecular aspects and emerging applications. Microb. Cell Fact. 19, 176.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.


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.
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.
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.
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.
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.
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.
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.
Delepelaire, P., 2019. Bacterial ABC transporters of iron containing compounds. Res. Microbiol. 170, 345–357.
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.
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.
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.
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.
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.


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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.


Verchère, A., Broutin, I., Picard, M., 2017. Reconstitution of Membrane Proteins in Liposomes. Methods Mol. Biol. 1635, 259–282.
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.
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.
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.
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.
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.
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.
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.
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.
Bouillaud, F., Casteilla, L., Klaus, S., Miroux, B., 2017. Editorial. Biochimie 134, 1–2.
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.


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.
Zito, F., 2016. Silent or Not Silent? Consequences of the Human mt-cyb Polymorphism. Hum. Mutat. 37, 833.
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.
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.
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.
Popot, J.-L., Engelman, D.M., 2016. Membranes Do Not Tell Proteins How To Fold. Biochemistry 55, 5–18.
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.
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.
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.
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.
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.
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.


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.
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.
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.
Miroux, B., Pebay-Peyroula, E., 2015. Editorial overview: Membranes. Current Opinion in Structural Biology 33, vii–ix.
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.
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.
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.
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.