Bazzacco, P., Billon-Denis, E., Sharma, K.S., Catoire, L.J., Mary, S., Le Bon, C., Point, E., Banères, J.-L., Durand, G.,
Zito, F., Pucci, B., Popot, J.-L. (2012) Non-ionic homopolymeric amphipols: Application to membrane protein
folding, cell-free synthesis, and solution NMR. Biochemistry 51:1416–1430.
Bazzacco, P., Sharma, K.S., Durand, G., Giusti, F., Ebel, C., Popot, J.-L., Pucci, B. (2009) Trapping and stabilization of
integral membrane proteins by hydrophobically grafted glucose-based telomers. Biomacromolecules 10:3317–3326.
Bechara, C., Bolbach, G., Bazzacco, P., Sharma, S.K., Durand, G., Popot, J.-L., Zito, F., Sagan, S. (2012) MALDI mass
spectrometry analysis of membrane protein/amphipol complexes. Anal. Chem. 84:6128–6135.
Bersch, B., Dörr, J.M., Hessel, A., Killian, J.A., Schanda, P. (2017) Proton-detected solid-state NMR spectroscopy of a
zinc diffusion facilitator protein in native nanodiscs. Angew. Chem. Int. Ed. 56:2508–2512.
Booth, M., Peel, R., Partanen, R., Hondow, N., Vasilca, V., Jeuken, L.J.C., Critchley, K. (2013) Amphipol-encapsulated
CuInS 2 /ZnS quantum dots with excellent colloidal stability. RSC Adv. 3:20559–20566.
Botte, M., Zaccai, N.R., Lycklama A., Nijeholt, J., Martin, R., Knoops, K., Papai, G., Zou, J., Deniaud, A.,
Karuppasamy, M., Jiang, Q., Singha Roy, A., Schulten, K., Schultz, P., Rappsilber, J., Zaccai, G., Berger, I.,
Collinson, I., Schaffitzel, C. (2016) A central cavity within the holotranslocon suggests a mechanism for membrane
protein insertion. Sci. Rep. 6:38399.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Brotherus, J.R., Jost, P.C., Griffith, O.H., Hokin, L.E. (1979) Detergent inactivation of sodium- and potassium-activated
adenosinetriphosphatase of the electric eel. Biochemistry 18:5043–5050.
Calabrese, A.N., Watkinson, T.G., Henderson, P.J.F., Radford, S.E., Ashcroft, A.E. (2015) Amphipols outperform
dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase. Anal. Chem. 87:1118–1126.
Cao, E., Liao, M., Cheng, Y., Julius, D. (2013) TRPV1 structures in distinct conformations reveal activation
mechanisms. Nature 504:113–118.
Casiraghi, M. (2016) Functional Modulation of a G Protein-Coupled Receptor Conformational Landscape in a Lipid
Bilayer. Thèse de Doctorat, Paris-7 University, Paris, 249 p.
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., Baaden, M., Guittet, E., Banères, J.-L. (2011) Electrostatically-driven fast association and
perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium
dissociation constants in the high-to-low nanomolar range. J. Biomol. NMR 50:191–195.
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010a)
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., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E., Popot, J.-L. (2010b) Solution NMR mapping of
water-accessible residues in the transmembrane β-barrel of OmpX. Eur. Biophys. J. 39:623–630.
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. Res. 197:91–95.
Champeil, P., le Maire, M., Andersen, J.P., Guillain, F., Gingold, M., LundII, S., Møller, J.V. (1986) Kinetic
characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium
pump. Rate-limiting steps under different conditions. J. Biol. Chem. 261:16372–16384.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Changeux, J.-P., Giraudat, J., Heidmann, T., Popot, J.-L., Sobel, A. (1980) Functional properties of the acetylcholine
receptor protein. Neurochem. Int. 2:219–231.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Charvolin, D., Picard, M., Huang, L.-S., Berry, E.A., Popot, J.-L. (2014) Solution behavior and crystallization of
cytochrome bc 1 in the presence of amphipols. J. Membr. Biol. 247:981–996.
Chen, Y., Clarke, O.B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, C., Godoy-Ruiz, R., von Alpen, D.C.,
Manzini, C., Blaner, W.S., Frank, J., Quadro, L., Weber, D.J., Shapiro, L., Hendrickson, W.A., Mancia, F. (2016)
Structure of the STRA6 receptor for retinol uptake. Science 353:pii aad8266–8261.
Cherezov, V., J. C., Papiz, M.Z., Caffrey, M. (2006) Room to move: crystallizing membrane proteins in swollen lipidic
mesophases. J. Mol. Biol. 357:1605–1618.
References
323
Zito, F., Pucci, B., Popot, J.-L. (2012) Non-ionic homopolymeric amphipols: Application to membrane protein
folding, cell-free synthesis, and solution NMR. Biochemistry 51:1416–1430.
Bazzacco, P., Sharma, K.S., Durand, G., Giusti, F., Ebel, C., Popot, J.-L., Pucci, B. (2009) Trapping and stabilization of
integral membrane proteins by hydrophobically grafted glucose-based telomers. Biomacromolecules 10:3317–3326.
Bechara, C., Bolbach, G., Bazzacco, P., Sharma, S.K., Durand, G., Popot, J.-L., Zito, F., Sagan, S. (2012) MALDI mass
spectrometry analysis of membrane protein/amphipol complexes. Anal. Chem. 84:6128–6135.
Bersch, B., Dörr, J.M., Hessel, A., Killian, J.A., Schanda, P. (2017) Proton-detected solid-state NMR spectroscopy of a
zinc diffusion facilitator protein in native nanodiscs. Angew. Chem. Int. Ed. 56:2508–2512.
Booth, M., Peel, R., Partanen, R., Hondow, N., Vasilca, V., Jeuken, L.J.C., Critchley, K. (2013) Amphipol-encapsulated
CuInS 2 /ZnS quantum dots with excellent colloidal stability. RSC Adv. 3:20559–20566.
Botte, M., Zaccai, N.R., Lycklama A., Nijeholt, J., Martin, R., Knoops, K., Papai, G., Zou, J., Deniaud, A.,
Karuppasamy, M., Jiang, Q., Singha Roy, A., Schulten, K., Schultz, P., Rappsilber, J., Zaccai, G., Berger, I.,
Collinson, I., Schaffitzel, C. (2016) A central cavity within the holotranslocon suggests a mechanism for membrane
protein insertion. Sci. Rep. 6:38399.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Brotherus, J.R., Jost, P.C., Griffith, O.H., Hokin, L.E. (1979) Detergent inactivation of sodium- and potassium-activated
adenosinetriphosphatase of the electric eel. Biochemistry 18:5043–5050.
Calabrese, A.N., Watkinson, T.G., Henderson, P.J.F., Radford, S.E., Ashcroft, A.E. (2015) Amphipols outperform
dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase. Anal. Chem. 87:1118–1126.
Cao, E., Liao, M., Cheng, Y., Julius, D. (2013) TRPV1 structures in distinct conformations reveal activation
mechanisms. Nature 504:113–118.
Casiraghi, M. (2016) Functional Modulation of a G Protein-Coupled Receptor Conformational Landscape in a Lipid
Bilayer. Thèse de Doctorat, Paris-7 University, Paris, 249 p.
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., Baaden, M., Guittet, E., Banères, J.-L. (2011) Electrostatically-driven fast association and
perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium
dissociation constants in the high-to-low nanomolar range. J. Biomol. NMR 50:191–195.
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010a)
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., Zoonens, M., van Heijenoort, C., Giusti, F., Guittet, E., Popot, J.-L. (2010b) Solution NMR mapping of
water-accessible residues in the transmembrane β-barrel of OmpX. Eur. Biophys. J. 39:623–630.
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. Res. 197:91–95.
Champeil, P., le Maire, M., Andersen, J.P., Guillain, F., Gingold, M., LundII, S., Møller, J.V. (1986) Kinetic
characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium
pump. Rate-limiting steps under different conditions. J. Biol. Chem. 261:16372–16384.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Changeux, J.-P., Giraudat, J., Heidmann, T., Popot, J.-L., Sobel, A. (1980) Functional properties of the acetylcholine
receptor protein. Neurochem. Int. 2:219–231.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Charvolin, D., Picard, M., Huang, L.-S., Berry, E.A., Popot, J.-L. (2014) Solution behavior and crystallization of
cytochrome bc 1 in the presence of amphipols. J. Membr. Biol. 247:981–996.
Chen, Y., Clarke, O.B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, C., Godoy-Ruiz, R., von Alpen, D.C.,
Manzini, C., Blaner, W.S., Frank, J., Quadro, L., Weber, D.J., Shapiro, L., Hendrickson, W.A., Mancia, F. (2016)
Structure of the STRA6 receptor for retinol uptake. Science 353:pii aad8266–8261.
Cherezov, V., J. C., Papiz, M.Z., Caffrey, M. (2006) Room to move: crystallizing membrane proteins in swollen lipidic
mesophases. J. Mol. Biol. 357:1605–1618.
References
323