Vial, F., Oukhaled, A.G., Auvray, L., Tribet, C. (2007) Long-living channels of well-defined radius opened in lipid
bilayers by polydisperse, hydrophobically-modified polyacrylic acids. Soft Matter 3:75–78.
Vial, F., Rabhi, S., Tribet, C. (2005) Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids
and kinetics of vesicle disruption. Langmuir 21:853–862.
Wang, Z., Fan, G., Hryc, C.F., Blaza, J.N., Serysheva, I.I., Schmid, M.F., Chiu, W., Luisi, B.F., Du, D. (2017) An
allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife 6:e24905.
Watkinson, T.G., Calabrese, A.N., Ault, J.R., Radford, S.E., Ashcroft, A.E. (2017) FPOP-LC-MS/MS suggests
differences in interaction sites of amphipols and detergents with outer membrane proteins. J. Am. Soc. Mass
Spectrom. 28:50–55.
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. Int. J. Mass
Spectrom. 391:54–61.
Wei, R., Wang, X., Zhang, Y., Mukherjee, S., Zhang, L., Chen, Q., Huang, X., Jing, S., Liu, C., Li, S., Wang, G., Xu, Y.,
Zhu, S., Williams, A.J., Sun, F., Yin, C.C. (2016) Structural insights into Ca
2+ -activated long-range allosteric channel
gating of RyR1. Cell Res. 26:977–994.
Wheatley, M., Charlton, J., Jamshad, M., Routledge, S.J., Bailey, S., La-Borde, P.J., Azam, M.T., Logan, R.T., Bill, R.
M., Dafforn, T.R., Poyner, D.R. (2016) GPCR–styrene maleic acid lipid particles (GPCR–SMALPs): their nature and
potential. Biochem. Soc. Trans. 44:619–623.
Wickstrand, C., Dods, R., Royant, A., Neutze, R. (2015) Bacteriorhodopsin: Would the real structural intermediates
please stand up? Biochim. Biophys. Acta 1850:536–553.
Wilkens, S. (2000) F 1 F O -ATP synthase–stalking mind and imagination. J. Bioenerg. Biomembr. 32:333–339.
Wilkens, S., Capaldi, R.A. (1998a) Electron microscopic evidence of two stalks linking the F 1 and F O parts of the
Escherichia coli ATP synthase. Biochim. Biophys. Acta 1365:93–97.
Wilkens, S., Capaldi, R.A. (1998b) ATP synthase's second stalk comes into focus. Nature 393:29.
Wilkens, S., Zhou, J., Nakayama, R., Dunn, S.D., Capaldi, R.A. (2000) Localization of the δ subunit in the Escherichia
coli F 1 F O -ATPsynthase by immuno-electron microscopy: The δ subunit binds on top of the F 1 . J. Mol. Biol.
295:387–391.
Wilkes, M., Madej, M.G., Kreuter, L., Rhinow, D., Heinz, V., De Sanctis, S., Ruppel, S., Richter, R.M., Joos, F.,
Grieben, M., Pike, A.C., Huiskonen, J.T., Carpenter, E.P., Kühlbrandt, W., Witzgall, R., Ziegler, C. (2017) Molecular
insights into lipid-assisted Ca
2+ regulation of the TRP channel polycystin-2. Nat. Struct. Mol. Biol. 24:123–130.
Wojtowicz, H., Prochnicka-Chalufour, A., de Amorim, G.C., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G.,
Gubellini, F., Koutsioubas, A., Pérez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N. (2016)
Structural basis of the signalling through a bacterial membrane receptor, HasR, deciphered by an integrative
approach. Biochem. J. 473:2239–2248.
Wu, Z.S., Cui, Z.C., Cheng, H., Fan, C., Melcher, K., Jiang, Y., Zhang, C.H., Jiang, H.L., Cong, Y., Liu, Q., Xu,
H.E. (2015) High yield and efficient expression and purification of the human 5-HT 3A receptor. Acta Pharmacol. Sin.
36:1024–1032.
Zaccai, G. (2004) The effect of water on protein dynamics. Phil. Trans. R. Soc. Lond. B 359:1269–1275.
Zhang, N., Tsybovsky, Y., Kolesnikov, A.V., Rozanowska, M., Swider, M., Schwartz, S.B., Stone, E.M., Palczewska,
G., Maeda, A., Kefalov, V.J., Jacobson, S.G., Cideciyan, A.V., Palczewski, K. (2015a) Protein misfolding and the
pathogenesis of ABCA4-associated retinal degenerations. Hum. Mol. Genet. 24:3220–3237.
Zhang, R., Sahu, I.D., Liu, L., Osatuke, A., Comer, R.G., Dabney-Smith, C., Lorigan, G.A. (2015b) Characterizing the
structure of lipodisq nanoparticles for membrane protein spectroscopic studies. Biochim. Biophys. Acta
1848:329–333.
Zoonens, M. (2004) Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et
des polymères amphiphiles, les amphipols. Application à l'étude structurale des protéines membranaires par RMN à
haute résolution. Thèse de Doctorat, Université Paris-6, 233 p.
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. USA 102:8893–8898.
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.
Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759–796.
Zubcevic, L., Herzik, M.A., Jr., Chung, B.C., Liu, Z., Lander, G.C., Lee, S.-Y. (2016) Cryo-electron microscopy
structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23:180–186.
332
5 Formation and Properties of Membrane Protein/Amphipol Complexes
bilayers by polydisperse, hydrophobically-modified polyacrylic acids. Soft Matter 3:75–78.
Vial, F., Rabhi, S., Tribet, C. (2005) Association of octyl-modified poly(acrylic acid) onto unilamellar vesicles of lipids
and kinetics of vesicle disruption. Langmuir 21:853–862.
Wang, Z., Fan, G., Hryc, C.F., Blaza, J.N., Serysheva, I.I., Schmid, M.F., Chiu, W., Luisi, B.F., Du, D. (2017) An
allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife 6:e24905.
Watkinson, T.G., Calabrese, A.N., Ault, J.R., Radford, S.E., Ashcroft, A.E. (2017) FPOP-LC-MS/MS suggests
differences in interaction sites of amphipols and detergents with outer membrane proteins. J. Am. Soc. Mass
Spectrom. 28:50–55.
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. Int. J. Mass
Spectrom. 391:54–61.
Wei, R., Wang, X., Zhang, Y., Mukherjee, S., Zhang, L., Chen, Q., Huang, X., Jing, S., Liu, C., Li, S., Wang, G., Xu, Y.,
Zhu, S., Williams, A.J., Sun, F., Yin, C.C. (2016) Structural insights into Ca
2+ -activated long-range allosteric channel
gating of RyR1. Cell Res. 26:977–994.
Wheatley, M., Charlton, J., Jamshad, M., Routledge, S.J., Bailey, S., La-Borde, P.J., Azam, M.T., Logan, R.T., Bill, R.
M., Dafforn, T.R., Poyner, D.R. (2016) GPCR–styrene maleic acid lipid particles (GPCR–SMALPs): their nature and
potential. Biochem. Soc. Trans. 44:619–623.
Wickstrand, C., Dods, R., Royant, A., Neutze, R. (2015) Bacteriorhodopsin: Would the real structural intermediates
please stand up? Biochim. Biophys. Acta 1850:536–553.
Wilkens, S. (2000) F 1 F O -ATP synthase–stalking mind and imagination. J. Bioenerg. Biomembr. 32:333–339.
Wilkens, S., Capaldi, R.A. (1998a) Electron microscopic evidence of two stalks linking the F 1 and F O parts of the
Escherichia coli ATP synthase. Biochim. Biophys. Acta 1365:93–97.
Wilkens, S., Capaldi, R.A. (1998b) ATP synthase's second stalk comes into focus. Nature 393:29.
Wilkens, S., Zhou, J., Nakayama, R., Dunn, S.D., Capaldi, R.A. (2000) Localization of the δ subunit in the Escherichia
coli F 1 F O -ATPsynthase by immuno-electron microscopy: The δ subunit binds on top of the F 1 . J. Mol. Biol.
295:387–391.
Wilkes, M., Madej, M.G., Kreuter, L., Rhinow, D., Heinz, V., De Sanctis, S., Ruppel, S., Richter, R.M., Joos, F.,
Grieben, M., Pike, A.C., Huiskonen, J.T., Carpenter, E.P., Kühlbrandt, W., Witzgall, R., Ziegler, C. (2017) Molecular
insights into lipid-assisted Ca
2+ regulation of the TRP channel polycystin-2. Nat. Struct. Mol. Biol. 24:123–130.
Wojtowicz, H., Prochnicka-Chalufour, A., de Amorim, G.C., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G.,
Gubellini, F., Koutsioubas, A., Pérez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N. (2016)
Structural basis of the signalling through a bacterial membrane receptor, HasR, deciphered by an integrative
approach. Biochem. J. 473:2239–2248.
Wu, Z.S., Cui, Z.C., Cheng, H., Fan, C., Melcher, K., Jiang, Y., Zhang, C.H., Jiang, H.L., Cong, Y., Liu, Q., Xu,
H.E. (2015) High yield and efficient expression and purification of the human 5-HT 3A receptor. Acta Pharmacol. Sin.
36:1024–1032.
Zaccai, G. (2004) The effect of water on protein dynamics. Phil. Trans. R. Soc. Lond. B 359:1269–1275.
Zhang, N., Tsybovsky, Y., Kolesnikov, A.V., Rozanowska, M., Swider, M., Schwartz, S.B., Stone, E.M., Palczewska,
G., Maeda, A., Kefalov, V.J., Jacobson, S.G., Cideciyan, A.V., Palczewski, K. (2015a) Protein misfolding and the
pathogenesis of ABCA4-associated retinal degenerations. Hum. Mol. Genet. 24:3220–3237.
Zhang, R., Sahu, I.D., Liu, L., Osatuke, A., Comer, R.G., Dabney-Smith, C., Lorigan, G.A. (2015b) Characterizing the
structure of lipodisq nanoparticles for membrane protein spectroscopic studies. Biochim. Biophys. Acta
1848:329–333.
Zoonens, M. (2004) Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et
des polymères amphiphiles, les amphipols. Application à l'étude structurale des protéines membranaires par RMN à
haute résolution. Thèse de Doctorat, Université Paris-6, 233 p.
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. USA 102:8893–8898.
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.
Zoonens, M., Popot, J.-L. (2014) Amphipols for each season. J. Membr. Biol. 247:759–796.
Zubcevic, L., Herzik, M.A., Jr., Chung, B.C., Liu, Z., Lander, G.C., Lee, S.-Y. (2016) Cryo-electron microscopy
structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23:180–186.
332
5 Formation and Properties of Membrane Protein/Amphipol Complexes