Cappuccio, J.A., Blanchette, C.D., Sulchek, T.A., Arroyo, E.S., Kralj, J.M., Hinz, A.K., Kuhn, E.A., Chromy, B.A.,
Segelke, B.W., Rothschild, K.J., Fletcher, J.E., Katzen, F., Peterson, T.C., Kudlicki, W.A., Bench, G., Hoeprich, P.
D., Coleman, M.A. (2008) Cell-free co-expression of functional membrane proteins and apolipoprotein, forming
soluble nanolipoprotein particles. Mol. Cell. Proteom. 7:2246–2253.
Carey, M.C., Small, D.M. (1972) Micelle formation by bile salts. Physical-chemical and thermodynamic considerations.
Arch. Intern. Med. 130:506–527.
Carlson, J.W., Jonas, A., Sligar, S.G. (1997) Imaging and manipulation of high-density lipoproteins. Biophys. J.
73:1184–1189.
Casiraghi, M., Damian, M., Lescop, E., Point, E., Moncoq, K., Morellet, N., Levy, D., Marie, J., Guittet, E., Banères,
J.-L., Catoire, L.J. (2016) Functional modulation of a GPCR conformational landscape in a lipid bilayer. J. Am.
Chem. Soc. 138:11170–11175
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010)
Structure of a GPCR ligand in its receptor-bound state: leukotriene B 4 adopts a highly constrained conformation when
associated to human BLT2. J. Am. Chem. Soc. 132:9049–9057.
Catoire, L.J., Warnet, X.L., Warschawski, D.E. (2014) Micelles, bicelles, amphipols, nanodiscs, liposomes or intact
cells: The hitch-hiker guide to the study of membrane proteins by NMR, in: Mus-Veteau, I., ed., Membrane protein
production for structural analysis. Springer, pp. 315–346.
Catte, A., Patterson, J.C., Jones, M.K., Jerome, W.G., Bashtovyy, D., Su, Z., Gu, F., Chen, J., Aliste, M.P., Harvey, S.C.,
Li, L., Weinstein, G., Segrest, J.P. (2006) Novel changes in discoidal high density lipoprotein morphology:
a molecular dynamics study. Biophys. J. 90:4345–4360.
Chabaud, E. (1997) Application des tensioactifs fluorés à la manipulation in vitro des protéines membranaires. Rapport
de D.E.A., Université Paris-VI.
Chabaud, E., Barthélémy, P., Mora, N., Popot, J.-L., Pucci, B. (1998) Stabilization of integral membrane proteins in
aqueous solution using fluorinated surfactants. Biochimie 80:515–530.
Chaudier, Y., Barthélémy, P., Pucci, B. (2001) Synthesis and preliminary assessment of hybrid hydrocarbonfluorocarbon anionic and non-ionic surfactants. Tetrahedron Lett. 42:3583–3585.
Chaudier, Y., Zito, F., Barthélémy, P., Stroebel, D., Améduri, B., Popot, J.-L., Pucci, B. (2002) Synthesis and
preliminary biochemical assessment of ethyl-terminated perfluoroalkylamine oxide surfactants. Bioorg. Med.
Chem. Lett. 12:1587–1590.
Cho, K.H., Byrne, B., Chae, P.S. (2013) Hemifluorinated maltose-neopentyl glycol (HF-MNG) amphiphiles for
membrane protein stabilisation. ChemBioChem 14:452–455.
Chung, B.H., Anantharamaiah, G.M., Brouillette, C.G., Nishida, T., Segrest, J.P. (1985) Studies of synthetic peptide
analogs of the amphipathic helix. Correlation of structure with function. J. Biol. Chem. 260:10256–10262.
Chung, J., Prestegard, J.H. (1993) Characterization of field-ordered aqueous liquid crystals by NMR diffusion
measurements. J. Phys. Chem. 97:9837–9843.
Civjan, N.R., Bayburt, T.H., Schuler, M.A., Sligar, S.G. (2003) Direct solubilization of heterologously expressed
membrane proteins by incorporation into nanoscale lipid bilayers. BioTechniques 35:556–560, 562–563.
Corin, K., Baaske, P., Ravel, D.B., Song, J., Brown, E., Wang, X., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Luo,
Y., Braun, D., Zhang, S. (2011) Designer lipid-like peptides: a class of detergents for studying functional olfactory
receptors using commercial cell-free systems. PLoS ONE 6:e25067.
Cui, T.X., Canlas, C.G., Xu, Y., Tang, P. (2010) Anesthetic effects on the structure and dynamics of the second
transmembrane domains of nAChR α4β2. Biochim. Biophys. Acta 1798:161–166.
Czerski, L., Sanders, C.R. (2000) Functionality of a membrane protein in bicelles. Anal. Biochem. 284:327–333.
Daury, L., Orange, F., Taveau, J.-C., Verchère, A., Monlezun, L., Gounou, C., Marreddy, R.K.R., Picard, M., Broutin, I.,
Pos, K.M., Lambert, O. (2016) Tripartite assembly of RND multidrug efflux pumps. Nat. Commun. 7:10731.
Dauvergne, J., Polidori, A., Vénien-Bryan, C., Pucci, B. (2008) Synthesis of a hemifluorinated amphiphile designed for
self-assembly and two-dimensional crystallization of membrane proteins. Tet. Lett. 49:2247–2250.
De Angelis, A., Nevzorov, A., Park, S.H., Howell, S.C., Mrse, A.A., Opella, S.J. (2004) High-resolution NMR
spectroscopy of membrane proteins in “aligned” bicelles. J. Am. Chem. Soc. 126:15340–15341.
De Angelis, A.A., Opella, S.J. (2007) Bicelle samples for solid-state NMR of membrane proteins. Nat. Protoc.
2:2332–2338.
Debnath, A., Schäfer, L.V. (2015) Structure and dynamics of phospholipid nanodiscs from all-atom and coarse-grained
simulations. J. Phys. Chem. B 119:6991–7002.
Dempsey, C.E., Sternberg, B. (1991) Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced
by melittin and [Ala-14]melittin. Biochim. Biophys. Acta 1061:175–184.
Denisov, I.G., Baas, B.J., Grinkova, Y.V., Sligar, S.G. (2007) Cooperativity in cytochrome P450 3A4: linkages in
substrate binding, spin state, uncoupling, and product formation. J. Biol. Chem. 282:7066–7076.
References
137
Segelke, B.W., Rothschild, K.J., Fletcher, J.E., Katzen, F., Peterson, T.C., Kudlicki, W.A., Bench, G., Hoeprich, P.
D., Coleman, M.A. (2008) Cell-free co-expression of functional membrane proteins and apolipoprotein, forming
soluble nanolipoprotein particles. Mol. Cell. Proteom. 7:2246–2253.
Carey, M.C., Small, D.M. (1972) Micelle formation by bile salts. Physical-chemical and thermodynamic considerations.
Arch. Intern. Med. 130:506–527.
Carlson, J.W., Jonas, A., Sligar, S.G. (1997) Imaging and manipulation of high-density lipoproteins. Biophys. J.
73:1184–1189.
Casiraghi, M., Damian, M., Lescop, E., Point, E., Moncoq, K., Morellet, N., Levy, D., Marie, J., Guittet, E., Banères,
J.-L., Catoire, L.J. (2016) Functional modulation of a GPCR conformational landscape in a lipid bilayer. J. Am.
Chem. Soc. 138:11170–11175
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010)
Structure of a GPCR ligand in its receptor-bound state: leukotriene B 4 adopts a highly constrained conformation when
associated to human BLT2. J. Am. Chem. Soc. 132:9049–9057.
Catoire, L.J., Warnet, X.L., Warschawski, D.E. (2014) Micelles, bicelles, amphipols, nanodiscs, liposomes or intact
cells: The hitch-hiker guide to the study of membrane proteins by NMR, in: Mus-Veteau, I., ed., Membrane protein
production for structural analysis. Springer, pp. 315–346.
Catte, A., Patterson, J.C., Jones, M.K., Jerome, W.G., Bashtovyy, D., Su, Z., Gu, F., Chen, J., Aliste, M.P., Harvey, S.C.,
Li, L., Weinstein, G., Segrest, J.P. (2006) Novel changes in discoidal high density lipoprotein morphology:
a molecular dynamics study. Biophys. J. 90:4345–4360.
Chabaud, E. (1997) Application des tensioactifs fluorés à la manipulation in vitro des protéines membranaires. Rapport
de D.E.A., Université Paris-VI.
Chabaud, E., Barthélémy, P., Mora, N., Popot, J.-L., Pucci, B. (1998) Stabilization of integral membrane proteins in
aqueous solution using fluorinated surfactants. Biochimie 80:515–530.
Chaudier, Y., Barthélémy, P., Pucci, B. (2001) Synthesis and preliminary assessment of hybrid hydrocarbonfluorocarbon anionic and non-ionic surfactants. Tetrahedron Lett. 42:3583–3585.
Chaudier, Y., Zito, F., Barthélémy, P., Stroebel, D., Améduri, B., Popot, J.-L., Pucci, B. (2002) Synthesis and
preliminary biochemical assessment of ethyl-terminated perfluoroalkylamine oxide surfactants. Bioorg. Med.
Chem. Lett. 12:1587–1590.
Cho, K.H., Byrne, B., Chae, P.S. (2013) Hemifluorinated maltose-neopentyl glycol (HF-MNG) amphiphiles for
membrane protein stabilisation. ChemBioChem 14:452–455.
Chung, B.H., Anantharamaiah, G.M., Brouillette, C.G., Nishida, T., Segrest, J.P. (1985) Studies of synthetic peptide
analogs of the amphipathic helix. Correlation of structure with function. J. Biol. Chem. 260:10256–10262.
Chung, J., Prestegard, J.H. (1993) Characterization of field-ordered aqueous liquid crystals by NMR diffusion
measurements. J. Phys. Chem. 97:9837–9843.
Civjan, N.R., Bayburt, T.H., Schuler, M.A., Sligar, S.G. (2003) Direct solubilization of heterologously expressed
membrane proteins by incorporation into nanoscale lipid bilayers. BioTechniques 35:556–560, 562–563.
Corin, K., Baaske, P., Ravel, D.B., Song, J., Brown, E., Wang, X., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Luo,
Y., Braun, D., Zhang, S. (2011) Designer lipid-like peptides: a class of detergents for studying functional olfactory
receptors using commercial cell-free systems. PLoS ONE 6:e25067.
Cui, T.X., Canlas, C.G., Xu, Y., Tang, P. (2010) Anesthetic effects on the structure and dynamics of the second
transmembrane domains of nAChR α4β2. Biochim. Biophys. Acta 1798:161–166.
Czerski, L., Sanders, C.R. (2000) Functionality of a membrane protein in bicelles. Anal. Biochem. 284:327–333.
Daury, L., Orange, F., Taveau, J.-C., Verchère, A., Monlezun, L., Gounou, C., Marreddy, R.K.R., Picard, M., Broutin, I.,
Pos, K.M., Lambert, O. (2016) Tripartite assembly of RND multidrug efflux pumps. Nat. Commun. 7:10731.
Dauvergne, J., Polidori, A., Vénien-Bryan, C., Pucci, B. (2008) Synthesis of a hemifluorinated amphiphile designed for
self-assembly and two-dimensional crystallization of membrane proteins. Tet. Lett. 49:2247–2250.
De Angelis, A., Nevzorov, A., Park, S.H., Howell, S.C., Mrse, A.A., Opella, S.J. (2004) High-resolution NMR
spectroscopy of membrane proteins in “aligned” bicelles. J. Am. Chem. Soc. 126:15340–15341.
De Angelis, A.A., Opella, S.J. (2007) Bicelle samples for solid-state NMR of membrane proteins. Nat. Protoc.
2:2332–2338.
Debnath, A., Schäfer, L.V. (2015) Structure and dynamics of phospholipid nanodiscs from all-atom and coarse-grained
simulations. J. Phys. Chem. B 119:6991–7002.
Dempsey, C.E., Sternberg, B. (1991) Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced
by melittin and [Ala-14]melittin. Biochim. Biophys. Acta 1061:175–184.
Denisov, I.G., Baas, B.J., Grinkova, Y.V., Sligar, S.G. (2007) Cooperativity in cytochrome P450 3A4: linkages in
substrate binding, spin state, uncoupling, and product formation. J. Biol. Chem. 282:7066–7076.
References
137