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Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
De Zorzi, R., Liao, M., Walz, T. (2016) Single-particle electron microscopy in the study of membrane protein structure.
Microscopy (Oxf) 65:81–96.
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Efremov, R.G., Leitner, A., Aebersold, R., Raunser, S. (2015) Architecture and conformational switch mechanism of the
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Chávez-Gutiérrez, L. (2015) The dynamic conformational landscape of γ-secretase. J. Cell Sci. 128:589–598.
Etzkorn, M., Raschle, T., Hagn, F., Gelev, V., Rice, A.J., Walz, T., Wagner, G. (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure
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closed and desensitized states. J. Membr. Biol. 223:161–172.
Ferrandez, Y., Dezi, M., Bosco, M., Urvoas, A., Valério, 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.
Fitzpatrick, A.W.P., Llabrés, S., Neuberger, A., Blaza, J.N., Bai, X.-C., Okada, U., Murakami, S., van Veen, H.W.,
Zachariae, U., Scheres, S.H.W., Luisi, B.F., Du, D. (2017) Structure of the MacAB–TolC ABC-type tripartite
multidrug efflux pump. Nat. Microbiol. 2:17070.
Flötenmeyer, M., Weiss, H., Tribet, C., Popot, J.-L., Leonard, K. (2007) The use of amphipathic polymers for cryoelectron microscopy of NADH:ubiquinone oxidoreductase (Complex I). J. Microsc. 227:229–235.
Frank, J. (2006) Three-dimensional Electron Microscopy of Macromolecular Assemblies: Visualization of Biological
Molecules in their Native State. Oxford Univerity Press, New York, 342 p.
Fujiyoshi, Y. (2011) Electron crystallography for structural and functional studies of membrane proteins. J Electron
Microsc (Tokyo) 60 Suppl 1:S149-S159.
Gao, Y., Cao, E., Julius, D., Cheng, Y. (2016) TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid
action. Nature 534:347–351.
Ge, J., Li, W., Zhao, Q., Li, N., Chen, M., Zhi, P., Li, R., Gao, N., Xiao, B., Yang, M. (2015) Architecture of the
mammalian mechanosensitive Piezo1 channel. Nature 527:64–69.
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 16:3751–3761.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
References
585
161:438–449.
Chiu, Y.H., Jin, X., Medina, C., Leonhardt, S.A., Kiessling, V., Bennett, B.C., Shu, S., Tamm, L.K., Yeager, M.,
Ravichandran, K.S., Bayliss, D.A. (2017) A quantized mechanism for activation of pannexin channels. Nat.
Commun. 8:14324.
Chowdhury, S., Ketcham, S.A., Schroer, T.A., Lander, G.C. (2015) Structural organization of the dynein-dynactin
complex bound to microtubules. Nat. Struct. Mol. Biol. 22:345–347.
Constantine, M., Liew, C.K., Lo, V., Macmillan, A., Cranfield, C.G., Sunde, M., Whan, R., Graham, R.M., Martinac,
B. (2016) Heterologously-expressed and liposome-reconstituted human transient receptor potential melastatin 4 channel (TRPM4) is a functional tetramer. Sci. Rep. 6:19352.
Cvetkov, T.L., Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J. Biol. Chem. 286:38168–38176.
Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
De Zorzi, R., Liao, M., Walz, T. (2016) Single-particle electron microscopy in the study of membrane protein structure.
Microscopy (Oxf) 65:81–96.
Dobro, M.J., Melanson, L.A., Jensen, G.J., McDowall, A.W. (2010) Plunge freezing for electron cryomicroscopy. Meth.
Enzymol. 481:63–82.
Dubochet, J., Adrian, M., Chang, J.J., Homo, J.C., Lepault, J., McDowall, A.W., Schultz, P. (1988) Cryo-electron
microscopy of vitrified specimens. Q. Rev. Biophys. 21:129–228.
Dubochet, J. (2015) A reminiscence about early times of vitreous water in electron cryomicroscopy. Biophys. J.
109:812–817.
Efremov, R.G., Leitner, A., Aebersold, R., Raunser, S. (2015) Architecture and conformational switch mechanism of the
ryanodine receptor. Nature 517:39–43.
Ekiert, D.C., Bhabha, G., Isom, G.L., Greenan, G., Ovchinnikov, S., Henderson, I.R., Cox, J.S., Vale, R.D. (2017)
Architectures of lipid transport systems for the bacterial outer membrane. Cell 169:273–285.
Elad, N., De Strooper, B., Lismont, S., Hagen, W., Veugelen, S., Arimon, M., Horré, K., Berezovska, O., Sachse, C.,
Chávez-Gutiérrez, L. (2015) The dynamic conformational landscape of γ-secretase. J. Cell Sci. 128:589–598.
Etzkorn, M., Raschle, T., Hagn, F., Gelev, V., Rice, A.J., Walz, T., Wagner, G. (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure
21:394–401.
Fan, G., Gonzalez, J., Popova, O.B., Wensel, T.G., Serysheva, I.I. (2014) A first look into the 3D structure of the TRPV2
channel by single-particle cryo-EM. Biophys. J. 106:600a–601a.
Fernández-Ballester, G., Ferrer-Montiel, A. (2008) Molecular modeling of the full-length human TRPV1 channel in
closed and desensitized states. J. Membr. Biol. 223:161–172.
Ferrandez, Y., Dezi, M., Bosco, M., Urvoas, A., Valério, 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.
Fitzpatrick, A.W.P., Llabrés, S., Neuberger, A., Blaza, J.N., Bai, X.-C., Okada, U., Murakami, S., van Veen, H.W.,
Zachariae, U., Scheres, S.H.W., Luisi, B.F., Du, D. (2017) Structure of the MacAB–TolC ABC-type tripartite
multidrug efflux pump. Nat. Microbiol. 2:17070.
Flötenmeyer, M., Weiss, H., Tribet, C., Popot, J.-L., Leonard, K. (2007) The use of amphipathic polymers for cryoelectron microscopy of NADH:ubiquinone oxidoreductase (Complex I). J. Microsc. 227:229–235.
Frank, J. (2006) Three-dimensional Electron Microscopy of Macromolecular Assemblies: Visualization of Biological
Molecules in their Native State. Oxford Univerity Press, New York, 342 p.
Fujiyoshi, Y. (2011) Electron crystallography for structural and functional studies of membrane proteins. J Electron
Microsc (Tokyo) 60 Suppl 1:S149-S159.
Gao, Y., Cao, E., Julius, D., Cheng, Y. (2016) TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid
action. Nature 534:347–351.
Ge, J., Li, W., Zhao, Q., Li, N., Chen, M., Zhi, P., Li, R., Gao, N., Xiao, B., Yang, M. (2015) Architecture of the
mammalian mechanosensitive Piezo1 channel. Nature 527:64–69.
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 16:3751–3761.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
References
585