Bayburt, T.H., Grinkova, Y.V., Sligar, S.G. (2002) Self-assembly of discoidal phospholipid bilayer nanoparticles with
membrane scaffold proteins. Nano Lett. 2:853–856.
Bazzacco, P. (2009) Non-ionic amphipols: new tools for in vitro studies of membrane proteins. Validation and
development of biochemical and biophysical applications. Thèse de Doctorat, Université Paris-7, 176 p.
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.
Beaugrand, M., Arnold, A.A., Juneau, A., Balieiro Gambaro, A., Warschawski, D.E., Williamson, P.T.F., Marcotte,
I. (2016) Magnetically oriented bicelles with monoalkylphosphocholines: versatile membrane mimetics for nuclear
magnetic resonance applications. Langmuir 32:13244–13251.
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.
Böckmann, R.A., Caflisch, A. (2005) Spontaneous formation of detergent micelles around the outer membrane protein
OmpX. Biophys. J. 88:3191–3204.
Caravan, P., Ellison, J.J., McMurry, T.J., Lauffer, R.B. (1999) Gadolinium(III) chelates as MRI contrast agents:
Structure, dynamics, and applications. Chem. Rev. 99:2293–2352.
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., 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.
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., 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.
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.
Chill, J.H., Louis, J.M., Baber, J.L., Bax, A. (2006a) Measurement of
15
N relaxation in the detergent-solubilized
tetrameric KcsA potassium channel. J. Biomol. NMR 36:123–136.
Chill, J.H., Louis, J.M., Miller, M., Bax, A. (2006b) NMR study of the tetrameric KcsA potassium channel in detergent
micelles. Protein Sci. 15:684–698.
Chou, J.J., Kaufman, J.D., Stahl, S.J., Wingfield, P.T., Bax, A. (2002) Micelle-induced curvature in a water-insoluble
HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J. Am. Chem.
Soc. 124:2450–2451.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Doctorat, Université Paris-7, 229 p.
Dahmane, T., Damian, M., Mary, S., Popot, J.-L., Banères, J.-L. (2009) Amphipol-assisted in vitro folding of G proteincoupled receptors. Biochemistry 48:6516–6521.
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.
Denisov, I.G., Grinkova, Y.V., Lazarides, A.A., Sligar, S.G. (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126:3477–3487.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
References
491
membrane scaffold proteins. Nano Lett. 2:853–856.
Bazzacco, P. (2009) Non-ionic amphipols: new tools for in vitro studies of membrane proteins. Validation and
development of biochemical and biophysical applications. Thèse de Doctorat, Université Paris-7, 176 p.
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.
Beaugrand, M., Arnold, A.A., Juneau, A., Balieiro Gambaro, A., Warschawski, D.E., Williamson, P.T.F., Marcotte,
I. (2016) Magnetically oriented bicelles with monoalkylphosphocholines: versatile membrane mimetics for nuclear
magnetic resonance applications. Langmuir 32:13244–13251.
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.
Böckmann, R.A., Caflisch, A. (2005) Spontaneous formation of detergent micelles around the outer membrane protein
OmpX. Biophys. J. 88:3191–3204.
Caravan, P., Ellison, J.J., McMurry, T.J., Lauffer, R.B. (1999) Gadolinium(III) chelates as MRI contrast agents:
Structure, dynamics, and applications. Chem. Rev. 99:2293–2352.
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., 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.
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., 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.
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.
Chill, J.H., Louis, J.M., Baber, J.L., Bax, A. (2006a) Measurement of
15
N relaxation in the detergent-solubilized
tetrameric KcsA potassium channel. J. Biomol. NMR 36:123–136.
Chill, J.H., Louis, J.M., Miller, M., Bax, A. (2006b) NMR study of the tetrameric KcsA potassium channel in detergent
micelles. Protein Sci. 15:684–698.
Chou, J.J., Kaufman, J.D., Stahl, S.J., Wingfield, P.T., Bax, A. (2002) Micelle-induced curvature in a water-insoluble
HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J. Am. Chem.
Soc. 124:2450–2451.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Doctorat, Université Paris-7, 229 p.
Dahmane, T., Damian, M., Mary, S., Popot, J.-L., Banères, J.-L. (2009) Amphipol-assisted in vitro folding of G proteincoupled receptors. Biochemistry 48:6516–6521.
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.
Denisov, I.G., Grinkova, Y.V., Lazarides, A.A., Sligar, S.G. (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126:3477–3487.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007a) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
References
491