Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K., Sanders, C.R. (2001) Use of amphipathic
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Otzen, D.E. (2015) Proteins in a brave new surfactant world. Curr. Opin. Colloid Interface Sci. 20:161–169.
Otzen, D.E., Andersen, K.K. (2013) Folding of outer membrane proteins. Arch. Biochem. Biophys. 531:34–43.
Park, K.-H., Billon-Denis, E., Dahmane, T., Lebaupain, F., Pucci, B., Breyton, C., Zito, F. (2011) In the cauldron of cellfree synthesis of membrane proteins: Playing with new surfactants. New Biotech. 28:255–261.
Pocanschi, C., Popot, J.-L., Kleinschmidt, J.H. (2013) Folding and stability of outer membrane protein A (OmpA) from
Escherichia coli in an amphipathic polymer, amphipol A8-35. Eur. Biophys. J. 42:103–118.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L.J., Champeil, P.,
Charvolin, D., Cocco, M.J., Crémel, G., Dahmane, T., de la Maza, L.M., Ebel, C., Gabel, F., Giusti, F., Gohon,
Y., Goormaghtigh, E., Guittet, E., Kleinschmidt, J.H., Kühlbrandt, W., Le Bon, C., Martinez, K.L., Picard, M., Pucci,
B., Rappaport, F., Sachs, J.N., Tribet, C., van Heijenoort, C., Wien, F., Zito, F., Zoonens, M. (2011) Amphipols from
A to Z. Annu. Rev. Biophys. 40:379–408.
Popot, J.-L., Engelman, D.M. (2000) Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem.
69:881–923.
Popot, J.-L., Engelman, D.M. (2016) Membranes do not tell proteins how to fold. Biochemistry 55:5–18.
Popot, J.-L., Gerchman, S.-E., Engelman, D.M. (1987) Refolding of bacteriorhodopsin in lipid bilayers: a thermodynamically controlled two-stage process. J. Mol. Biol. 198:655–676.
Rasmussen, S.G.F., Choi, H.-J., Fung, J.J., Pardon, E., Casarosa, P., Chae, P.S., DeVree, B.T., Rosenbaum, D.M., Thian,
F.S., Kobilka, T.S., Schnapp, A., Konetzki, I., Sunahara, R.K., Gellman, S.H., Pautsch, A., Steyaert, J., Weis, W.I.,
Kobilka, B.K. (2011) Structure of a nanobody-stabilized active state of the β 2 adrenoceptor. Nature 469:175–180.
Schweizer, M., Hindennach, I., Garten, W., Henning, U. (1978) Major proteins of the Escherichia coli outer cell
envelope membrane. Interaction of protein II with lipopolysaccharide. Eur. J. Biochem. 82:211–217.
Sharma, K.S., Durand, G., Gabel, F., Bazzacco, P., Le Bon, C., Billon-Denis, E., Catoire, L.J., Popot, J.-L., Ebel, C.,
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Stangl, M., Unger, S., Keller, S., Schneider, D. (2014) Sequence-specific dimerization of a transmembrane helix in
amphipol A8-35. PLOS One 9:e110970.
Stanley, A.M., Fleming, K.G. (2008) The process of folding proteins into membranes: Challenges and progress. Arch.
Biochem. Biophys. 469:46–66.
Stansfeld, P.J., Jeffreys, E.E., Sansom, M.S.P. (2013) Multiscale simulations reveal conserved patterns of lipid
interactions with aquaporins. Structure 21:810–819.
Tamm, L.K., Hong, H., Liang, B. (2004) Folding and assembly of β-barrel membrane proteins. Biochim. Biophys. Acta
1666:250–263.
Tastan, O., Dutta, A., Booth, P., Klein-Seetharaman, J. (2014) Retinal proteins as model systems for membrane protein
folding. Biochim. Biophys. Acta 1837:656–663.
Vitrac, H., MacLean, D.M., Karlstaedt, A., Taegtmeyer, H., Jayaraman, V., Bogdanov, M., Dowhan, W. (2017) Dynamic
lipid-dependent modulation of protein topology by post-translational phosphorylation. J. Biol. Chem.
292:1613–1624.
White, S.H. (2003) Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett. 555:116–121.
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.
Zoonens, M., Zito, F., Martinez, K.L., Popot, J.-L. (2014) Amphipols: a general introduction and some protocols, in:
Mus-Veteau, I. (Ed.), Membrane Proteins Production for Structural Analysis. Springer, New York, Heidelberg,
Dordrecht, London, pp. 173–203.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
References
359
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Otzen, D.E. (2015) Proteins in a brave new surfactant world. Curr. Opin. Colloid Interface Sci. 20:161–169.
Otzen, D.E., Andersen, K.K. (2013) Folding of outer membrane proteins. Arch. Biochem. Biophys. 531:34–43.
Park, K.-H., Billon-Denis, E., Dahmane, T., Lebaupain, F., Pucci, B., Breyton, C., Zito, F. (2011) In the cauldron of cellfree synthesis of membrane proteins: Playing with new surfactants. New Biotech. 28:255–261.
Pocanschi, C., Popot, J.-L., Kleinschmidt, J.H. (2013) Folding and stability of outer membrane protein A (OmpA) from
Escherichia coli in an amphipathic polymer, amphipol A8-35. Eur. Biophys. J. 42:103–118.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L.J., Champeil, P.,
Charvolin, D., Cocco, M.J., Crémel, G., Dahmane, T., de la Maza, L.M., Ebel, C., Gabel, F., Giusti, F., Gohon,
Y., Goormaghtigh, E., Guittet, E., Kleinschmidt, J.H., Kühlbrandt, W., Le Bon, C., Martinez, K.L., Picard, M., Pucci,
B., Rappaport, F., Sachs, J.N., Tribet, C., van Heijenoort, C., Wien, F., Zito, F., Zoonens, M. (2011) Amphipols from
A to Z. Annu. Rev. Biophys. 40:379–408.
Popot, J.-L., Engelman, D.M. (2000) Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem.
69:881–923.
Popot, J.-L., Engelman, D.M. (2016) Membranes do not tell proteins how to fold. Biochemistry 55:5–18.
Popot, J.-L., Gerchman, S.-E., Engelman, D.M. (1987) Refolding of bacteriorhodopsin in lipid bilayers: a thermodynamically controlled two-stage process. J. Mol. Biol. 198:655–676.
Rasmussen, S.G.F., Choi, H.-J., Fung, J.J., Pardon, E., Casarosa, P., Chae, P.S., DeVree, B.T., Rosenbaum, D.M., Thian,
F.S., Kobilka, T.S., Schnapp, A., Konetzki, I., Sunahara, R.K., Gellman, S.H., Pautsch, A., Steyaert, J., Weis, W.I.,
Kobilka, B.K. (2011) Structure of a nanobody-stabilized active state of the β 2 adrenoceptor. Nature 469:175–180.
Schweizer, M., Hindennach, I., Garten, W., Henning, U. (1978) Major proteins of the Escherichia coli outer cell
envelope membrane. Interaction of protein II with lipopolysaccharide. Eur. J. Biochem. 82:211–217.
Sharma, K.S., Durand, G., Gabel, F., Bazzacco, P., Le Bon, C., Billon-Denis, E., Catoire, L.J., Popot, J.-L., Ebel, C.,
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Stangl, M., Unger, S., Keller, S., Schneider, D. (2014) Sequence-specific dimerization of a transmembrane helix in
amphipol A8-35. PLOS One 9:e110970.
Stanley, A.M., Fleming, K.G. (2008) The process of folding proteins into membranes: Challenges and progress. Arch.
Biochem. Biophys. 469:46–66.
Stansfeld, P.J., Jeffreys, E.E., Sansom, M.S.P. (2013) Multiscale simulations reveal conserved patterns of lipid
interactions with aquaporins. Structure 21:810–819.
Tamm, L.K., Hong, H., Liang, B. (2004) Folding and assembly of β-barrel membrane proteins. Biochim. Biophys. Acta
1666:250–263.
Tastan, O., Dutta, A., Booth, P., Klein-Seetharaman, J. (2014) Retinal proteins as model systems for membrane protein
folding. Biochim. Biophys. Acta 1837:656–663.
Vitrac, H., MacLean, D.M., Karlstaedt, A., Taegtmeyer, H., Jayaraman, V., Bogdanov, M., Dowhan, W. (2017) Dynamic
lipid-dependent modulation of protein topology by post-translational phosphorylation. J. Biol. Chem.
292:1613–1624.
White, S.H. (2003) Translocons, thermodynamics, and the folding of membrane proteins. FEBS Lett. 555:116–121.
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.
Zoonens, M., Zito, F., Martinez, K.L., Popot, J.-L. (2014) Amphipols: a general introduction and some protocols, in:
Mus-Veteau, I. (Ed.), Membrane Proteins Production for Structural Analysis. Springer, New York, Heidelberg,
Dordrecht, London, pp. 173–203.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
References
359