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Anfinsen, C.B., Harber, E., Sela, M. (1961) The kinetics of formation of native ribonuclease during oxidation of the
reduced polypeptide chain. Proc. Natl. Acad. Sci. USA 47:1309–1314.
Anfinsen, C.B., Scheraga, H.A. (1975) Experimental and theoretical aspects of protein folding. Adv. Prot. Chem.
29:205–300.
Aponte-Santamaríaa, C., Brionesa, R., Schenk, A.D., Walz, T., de Groot, B.L. (2012) Molecular driving forces defining
lipid positions around aquaporin-0. Proc. Natl. Acad. Sci. USA 109:9887–9892.
Arunmanee, W., Harris, J.R., Lakey, J.H. (2014) Outer membrane protein F stabilised with minimal amphipol forms
linear arrays and LPS-dependent 2D crystals. J. Membr. Biol. 247:949–956.
Banères, J.-L., Mesnier, D., Martin, A., Joubert, L., Dumuis, A., Bockaert, J. (2005) Molecular characterization of a
purified 5-HT 4 receptor. A structural basis for drug efficacy. J. Biol. Chem. 280:20253–20260.
Banères, J.-L., Popot, J.-L., Mouillac, B. (2011) New advances in production and functional folding of G protein-coupled
receptors. Trends Biotechnol. 29:314–322.
Bannwarth, M., Schulz, G.E. (2003) The expression of outer membrane proteins for crystallization. Biochim. Biophys.
Acta 1610:37–45.
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.
Bogdanov, M., Dowhan, W., Vitrac, H. (2014) Lipids and topological rules governing membrane protein assembly.
Biochim. Biophys. Acta 1843:1475–1488.
Booth, P.J. (2003) The trials and tribulations of membrane protein folding in vitro. Biochim. Biophys. Acta 1610:51–56.
Bowie, J.U. (2005) Solving the membrane protein folding problem. Nature 438:581–589.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Buchanan, S.K. (1999) β-barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin.
Struct. Biol. 9:455–461.
Buchanan, S.K., Yamashita, S., Fleming, K.G. (2012) Structure and folding of outer membrane proteins, in: Tamm,
L.K. (Ed.), Membranes. Elsevier, Oxford:Academic Press, pp. 139–163.
Caffrey, M. (2011) Crystallizing membrane proteins for structure-function studies using lipidic mesophases. Biochem.
Soc. Trans. 39:725–732.
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.
Cherezov, V. (2011) Lipidic cubic phase technologies for membrane protein structural studies. Curr. Opin. Struct. Biol.
21:559–566.
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.
Cherezov, V., Rosenbaum, D.M., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Kuhn, P.,
Weis, W.I., Kobilka, B.K., Stevens, R.C. (2007) High-resolution crystal structure of an engineered human β 2 -
adrenergic G protein-coupled receptor. Science 318:1258–1265.
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.
Damian, M., Martin, A., Mesnier, D., Pin, J.-P., Banères, J.-L. (2006) Asymmetric conformational changes in a GPCR
dimer controlled by G-proteins. EMBO J. 13:5693–5702.
Elter, S., Raschle, T., Arens, S., Viegas, A., Gelev, V., Etzkorn, M., Wagner, G. (2014) The use of amphipols for NMR
structural characterization of 7-TM proteins. J. Membr. Biol. 247:957–964.
Engelman, D.M., Chen, Y., Chin, C.-N., Curran, R., Dixon, A.M., Dupuy, A., Lee, A., Lehnert, U., Mathews, E.,
Reshetnyak, Y., Senes, A., Popot, J.-L. (2003) Membrane protein folding: beyond the two-stage model. FEBS Lett.
555:122–125.
Goehring, A., Lee, C.-H., Wang, K.H., Michel, J.C., Claxton, D.P., Baconguis, I., Althoff, T., Fischer, S., Garcia, C.,
Gouaux, E. (2014) Screening and large-scale expression of membrane proteins in mammalian cells for structural
studies. Nat. Protoc. 9:2574–2585.
References
357
Anfinsen, C.B., Harber, E., Sela, M. (1961) The kinetics of formation of native ribonuclease during oxidation of the
reduced polypeptide chain. Proc. Natl. Acad. Sci. USA 47:1309–1314.
Anfinsen, C.B., Scheraga, H.A. (1975) Experimental and theoretical aspects of protein folding. Adv. Prot. Chem.
29:205–300.
Aponte-Santamaríaa, C., Brionesa, R., Schenk, A.D., Walz, T., de Groot, B.L. (2012) Molecular driving forces defining
lipid positions around aquaporin-0. Proc. Natl. Acad. Sci. USA 109:9887–9892.
Arunmanee, W., Harris, J.R., Lakey, J.H. (2014) Outer membrane protein F stabilised with minimal amphipol forms
linear arrays and LPS-dependent 2D crystals. J. Membr. Biol. 247:949–956.
Banères, J.-L., Mesnier, D., Martin, A., Joubert, L., Dumuis, A., Bockaert, J. (2005) Molecular characterization of a
purified 5-HT 4 receptor. A structural basis for drug efficacy. J. Biol. Chem. 280:20253–20260.
Banères, J.-L., Popot, J.-L., Mouillac, B. (2011) New advances in production and functional folding of G protein-coupled
receptors. Trends Biotechnol. 29:314–322.
Bannwarth, M., Schulz, G.E. (2003) The expression of outer membrane proteins for crystallization. Biochim. Biophys.
Acta 1610:37–45.
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.
Bogdanov, M., Dowhan, W., Vitrac, H. (2014) Lipids and topological rules governing membrane protein assembly.
Biochim. Biophys. Acta 1843:1475–1488.
Booth, P.J. (2003) The trials and tribulations of membrane protein folding in vitro. Biochim. Biophys. Acta 1610:51–56.
Bowie, J.U. (2005) Solving the membrane protein folding problem. Nature 438:581–589.
Broecker, J., Eger, B.T., Ernst, O.P. (2017) Crystallogenesis of membrane proteins mediated by polymer-bounded lipid
nanodiscs. Structure 25:384–392.
Buchanan, S.K. (1999) β-barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin.
Struct. Biol. 9:455–461.
Buchanan, S.K., Yamashita, S., Fleming, K.G. (2012) Structure and folding of outer membrane proteins, in: Tamm,
L.K. (Ed.), Membranes. Elsevier, Oxford:Academic Press, pp. 139–163.
Caffrey, M. (2011) Crystallizing membrane proteins for structure-function studies using lipidic mesophases. Biochem.
Soc. Trans. 39:725–732.
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.
Cherezov, V. (2011) Lipidic cubic phase technologies for membrane protein structural studies. Curr. Opin. Struct. Biol.
21:559–566.
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.
Cherezov, V., Rosenbaum, D.M., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Kuhn, P.,
Weis, W.I., Kobilka, B.K., Stevens, R.C. (2007) High-resolution crystal structure of an engineered human β 2 -
adrenergic G protein-coupled receptor. Science 318:1258–1265.
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.
Damian, M., Martin, A., Mesnier, D., Pin, J.-P., Banères, J.-L. (2006) Asymmetric conformational changes in a GPCR
dimer controlled by G-proteins. EMBO J. 13:5693–5702.
Elter, S., Raschle, T., Arens, S., Viegas, A., Gelev, V., Etzkorn, M., Wagner, G. (2014) The use of amphipols for NMR
structural characterization of 7-TM proteins. J. Membr. Biol. 247:957–964.
Engelman, D.M., Chen, Y., Chin, C.-N., Curran, R., Dixon, A.M., Dupuy, A., Lee, A., Lehnert, U., Mathews, E.,
Reshetnyak, Y., Senes, A., Popot, J.-L. (2003) Membrane protein folding: beyond the two-stage model. FEBS Lett.
555:122–125.
Goehring, A., Lee, C.-H., Wang, K.H., Michel, J.C., Claxton, D.P., Baconguis, I., Althoff, T., Fischer, S., Garcia, C.,
Gouaux, E. (2014) Screening and large-scale expression of membrane proteins in mammalian cells for structural
studies. Nat. Protoc. 9:2574–2585.
References
357