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.
Feinstein, H.E., Tifrea, D., Sun, G., Popot, J.-L., de la Maza, L.M., Cocco, M.J. (2014) Long-term stability of a vaccine
formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J. Membr. Biol.
247:1053–1065.
Fernández, C., Adeishvili, K., Wüthrich, K. (2001) Transverse relaxation-optimized NMR spectroscopy with the outer
membrane protein OmpX in dihexanoylphosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA 98:2358–2363.
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.
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.
Forman, S.A., Chiara, D.C., Miller, K.W. (2015) Anesthetics target interfacial transmembrane sites in nicotinic
acetylcholine receptors. Neuropharmacology 96:169–177.
Frindi, M., Michels, B., Zana, R. (1992a) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 2. C 6 E 3 , C 8 E 4 and C 8 E 8 . J. Phys.
Chem. 96:6095–6102.
Frindi, M., Michels, B., Zana, R. (1992b) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 3. Surfactants with a sugar head
group. J. Phys. Chem. 96:8137–8141.
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.
Giusti, F., Rieger, J., Catoire, L., Qian, S., Calabrese, A.N., Watkinson, T.G., Casiraghi, M., Radford, S.E., Ashcroft, A.
E., Popot, J.-L. (2014) Synthesis, characterization and applications of a perdeuterated amphipol. J. Membr. Biol.
247:909–924.
Goddard, A.D., Dijkman, P.M., Adamson, R.J., Inácio dos Reis, R., Watts, A. (2015) Reconstitution of membrane
proteins: A GPCR as an example. Meth. Enzymol. 556:405–424.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Thèse de DEA, Université Paris VI, Paris, 28 p.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Thèse de Doctorat, Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L., Ebel, C. (2004) Partial specific volume and solvent
interactions of amphipol A8-35. Anal. Biochem. 334:318–334.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Goyal, P., Krasteva, P.V., Van Gerven, N., Gubellini, F., Van den Broeck, I., Troupiotis-Tsaïlaki, A., Jonckheere, W.,
Péhau-Arnaudet, G., Pinkner, J.S., Chapman, M.R., Hultgren, S.J., Howorka, S., Fronzes, R., Remaut, H. (2014)
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516:250–253.
Grethen, A., Glueck, D., Keller, S. (2018) Role of coulombic repulsion in collisional lipid transfer among SMA(2:1)bounded nanodiscs. J. Membr. Biol., in the press.
Grethen, A., Oluwole, A.O., Danielczak, B., Vargas, C., Keller, S. (2017) Thermodynamics of nanodisc formation
mediated by styrene/maleic acid (2:1) copolymer. Sci. Rep. 7:11517.
Grigorieff, N., Ceska, T.A., Downing, K.H., Baldwin, J.M., Henderson, R. (1996) Electron-crystallographic refinement
of the structure of bacteriorhodopsin. J. Mol. Biol. 259:393–421.
References
325
channel by single-particle cryo-EM. Biophys. J. 106:600a-601a.
Feinstein, H.E., Tifrea, D., Sun, G., Popot, J.-L., de la Maza, L.M., Cocco, M.J. (2014) Long-term stability of a vaccine
formulated with the amphipol-trapped major outer membrane protein from Chlamydia trachomatis. J. Membr. Biol.
247:1053–1065.
Fernández, C., Adeishvili, K., Wüthrich, K. (2001) Transverse relaxation-optimized NMR spectroscopy with the outer
membrane protein OmpX in dihexanoylphosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA 98:2358–2363.
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.
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.
Forman, S.A., Chiara, D.C., Miller, K.W. (2015) Anesthetics target interfacial transmembrane sites in nicotinic
acetylcholine receptors. Neuropharmacology 96:169–177.
Frindi, M., Michels, B., Zana, R. (1992a) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 2. C 6 E 3 , C 8 E 4 and C 8 E 8 . J. Phys.
Chem. 96:6095–6102.
Frindi, M., Michels, B., Zana, R. (1992b) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 3. Surfactants with a sugar head
group. J. Phys. Chem. 96:8137–8141.
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.
Giusti, F., Rieger, J., Catoire, L., Qian, S., Calabrese, A.N., Watkinson, T.G., Casiraghi, M., Radford, S.E., Ashcroft, A.
E., Popot, J.-L. (2014) Synthesis, characterization and applications of a perdeuterated amphipol. J. Membr. Biol.
247:909–924.
Goddard, A.D., Dijkman, P.M., Adamson, R.J., Inácio dos Reis, R., Watts, A. (2015) Reconstitution of membrane
proteins: A GPCR as an example. Meth. Enzymol. 556:405–424.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Thèse de DEA, Université Paris VI, Paris, 28 p.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Thèse de Doctorat, Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L., Ebel, C. (2004) Partial specific volume and solvent
interactions of amphipol A8-35. Anal. Biochem. 334:318–334.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Goyal, P., Krasteva, P.V., Van Gerven, N., Gubellini, F., Van den Broeck, I., Troupiotis-Tsaïlaki, A., Jonckheere, W.,
Péhau-Arnaudet, G., Pinkner, J.S., Chapman, M.R., Hultgren, S.J., Howorka, S., Fronzes, R., Remaut, H. (2014)
Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516:250–253.
Grethen, A., Glueck, D., Keller, S. (2018) Role of coulombic repulsion in collisional lipid transfer among SMA(2:1)bounded nanodiscs. J. Membr. Biol., in the press.
Grethen, A., Oluwole, A.O., Danielczak, B., Vargas, C., Keller, S. (2017) Thermodynamics of nanodisc formation
mediated by styrene/maleic acid (2:1) copolymer. Sci. Rep. 7:11517.
Grigorieff, N., Ceska, T.A., Downing, K.H., Baldwin, J.M., Henderson, R. (1996) Electron-crystallographic refinement
of the structure of bacteriorhodopsin. J. Mol. Biol. 259:393–421.
References
325