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Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton, J.W., 2014. Amphipol-Trapped ExbB-ExbD Membrane Protein Complex from Escherichia coli: A Biochemical and Structural Case Study. J. Membr. Biol. 247, 1005–1018. https://doi.org/10.1007/s00232-014-9678-4
Della Pia, E.A., Hansen, R.W., Zoonens, M., Martinez, K.L., 2014. Functionalized Amphipols: A Versatile Toolbox Suitable for Applications of Membrane Proteins in Synthetic Biology. J. Membr. Biol. 247, 815–826. https://doi.org/10.1007/s00232-014-9663-y
Planchard, N., Point, E., Dahmane, T., Giusti, F., Renault, M., Le Bon, C., Durand, G., Milon, A., Guittet, E., Zoonens, M., Popot, J.-L., Catoire, L.J., 2014. The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media. J. Membr. Biol. 247, 827–842. https://doi.org/10.1007/s00232-014-9654-z
Etzkorn, M., Zoonens, M., Catoire, L.J., Popot, J.-L., Hiller, S., 2014. How Amphipols Embed Membrane Proteins: Global Solvent Accessibility and Interaction with a Flexible Protein Terminus. J. Membr. Biol. 247, 965–970. https://doi.org/10.1007/s00232-014-9657-9
Della Pia, E.A., Holm, J.V., Lloret, N., Le Bon, C., Popot, J.-L., Zoonens, M., Nygård, J., Martinez, K.L., 2014. A step closer to membrane protein multiplexed nanoarrays using biotin-doped polypyrrole. ACS Nano 8, 1844–1853. https://doi.org/10.1021/nn406252h
Zoonens, M., Zito, F., Martinez, K.L., Popot, J.-L., 2014. Amphipols: A General Introduction and Some Protocols, in: Mus-Veteau, I. (Ed.), Membrane Proteins Production for Structural Analysis. Springer New York, pp. 173–203.
Hattab, G., Suisse, A.Y.T., Ilioaia, O., Casiraghi, M., Dezi, M., Warnet, X.L., Warschawski, D.E., Moncoq, K., Zoonens, M., Miroux, B., 2014. Membrane Protein Production in Escherichia coli: Overview and Protocols, in: Mus-Veteau, I. (Ed.), Membrane Proteins Production for Structural Analysis. Springer New York, pp. 87–106.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L., 2014. Synthesis of an oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res. 42, e83. https://doi.org/10.1093/nar/gku250
Zoonens, M., Comer, J., Masscheleyn, S., Pebay-Peyroula, E., Chipot, C., Miroux, B., Dehez, F., 2013. Dangerous liaisons between detergents and membrane proteins. The case of mitochondrial uncoupling protein 2. J. Am. Chem. Soc. 135, 15174–15182. https://doi.org/10.1021/ja407424v
Blesneac, I., Ravaud, S., Machillot, P., Zoonens, M., Masscheylen, S., Miroux, B., Vivaudou, M., Pebay-Peyroula, E., 2012. Assaying the proton transport and regulation of UCP1 using solid supported membranes. Eur. Biophys. J. 41, 675–679. https://doi.org/10.1007/s00249-012-0844-2
Blesneac, I., Ravaud, S., Juillan-Binard, C., Barret, L.-A., Zoonens, M., Polidori, A., Miroux, B., Pucci, B., Pebay-Peyroula, E., 2012. Production of UCP1 a membrane protein from the inner mitochondrial membrane using the cell free expression system in the presence of a fluorinated surfactant. Biochim. Biophys. Acta 1818, 798–805. https://doi.org/10.1016/j.bbamem.2011.12.016
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Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E., Popot, J.-L., 2010. Solution NMR mapping of water-accessible residues in the transmembrane beta-barrel of OmpX. Eur. Biophys. J. 39, 623–630. https://doi.org/10.1007/s00249-009-0513-2
Zoonens, M., Miroux, B., 2010. Expression of membrane proteins at the Escherichia coli membrane for structural studies. Methods Mol. Biol. 601, 49–66. https://doi.org/10.1007/978-1-60761-344-2_4
Tribet, C., Diab, C., Dahmane, T., Zoonens, M., Popot, J.-L., Winnik, F.M., 2009. Thermodynamic characterization of the exchange of detergents and amphipols at the surfaces of integral membrane proteins. Langmuir 25, 12623–12634. https://doi.org/10.1021/la9018772
Catoire, L.J., Zoonens, M., van Heijenoort, C., Giusti, F., Popot, J.-L., Guittet, E., 2009. Inter- and intramolecular contacts in a membrane protein/surfactant complex observed by heteronuclear dipole-to-dipole cross-relaxation. J. Magn. Reson. 197, 91–95. https://doi.org/10.1016/j.jmr.2008.11.017
Zoonens, M., Reshetnyak, Y.K., Engelman, D.M., 2008. Bilayer interactions of pHLIP, a peptide that can deliver drugs and target tumors. Biophys. J. 95, 225–235. https://doi.org/10.1529/biophysj.107.124156
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L., 2007. Dynamics of membrane protein/amphipol association studied by Förster resonance energy transfer: implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46, 10392–10404. https://doi.org/10.1021/bi7007596
Petkova, V., Benattar, J.-J., Zoonens, M., Zito, F., Popot, J.-L., Polidori, A., Jasseron, S., Pucci, B., 2007. Free-Standing Films of Fluorinated Surfactants as 2D Matrices for Organizing Detergent-Solubilized Membrane Proteins. Langmuir 23, 4303–4309. https://doi.org/10.1021/la063249o
Triba, M.N., Zoonens, M., Popot, J.-L., Devaux, P.F., Warschawski, D.E., 2006. Reconstitution and alignment by a magnetic field of a beta-barrel membrane protein in bicelles. Eur. Biophys. J. 35, 268–275. https://doi.org/10.1007/s00249-005-0014-x
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L., 2005. NMR study of a membrane protein in detergent-free aqueous solution. Proc. Natl. Acad. Sci. U.S.A. 102, 8893–8898. https://doi.org/10.1073/pnas.0503750102
Nowaczyk, M., Oworah-Nkruma, R., Zoonens, M., Rögner, M., Popot, J.-L., 2004. - Amphipols: Strategies for an Improved PS2 Environment in Detergent-Free Aqueous Solution, in: Miyake, J., Igarashi, Y., Rögner, Matthias (Eds.), Biohydrogen III. Elsevier Science, Amsterdam, pp. 151–159. https://doi.org/10.1016/B978-008044356-0/50013-0
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Ferrage, F., Zoonens, M., Warschawski, D.E., Popot, J.-L., Bodenhausen, G., 2003. Slow diffusion of macromolecular assemblies by a new pulsed field gradient NMR method. J. Am. Chem. Soc. 125, 2541–2545. https://doi.org/10.1021/ja0211407