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Bibliography

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
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
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
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
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
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
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
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
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
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
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
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
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
Zoonens, M., Popot, J.-L., 2014. Amphipols for Each Season. J. Membr. Biol. 247, 759–796. https://doi.org/10.1007/s00232-014-9666-8
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
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
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
Popot, J.-L., Berry, E.A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon, Y., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F., Zoonens, M., Pucci, B., Tribet, C., 2003. Amphipols: polymeric surfactants for membrane biology research. Cell. Mol. Life Sci. 60, 1559–1574.
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