Mary, S., Damian, M., Rahmeh, R., Marie, J., Mouillac, B., Banères, J.-L. (2014) Amphipols in G protein-coupled
receptor pharmacology: What are they good for? J. Membr. Biol. 247:853–860.
Nabiev, I.R., Efremóv, R.G., Chumanov, G.D. (1985) The chromophore-binding site of bacteriorhodopsin. Resonance
Raman and surface-enhanced resonance Raman spectroscopy and quantum chemical study. J. Biosci. 8:363–374.
Nabiev, I.R., Chumanov, G.D., Efremóv, R.G. (1990) Surface-enhanced Raman spectroscopy of biomolecules. Part
II. Application of short- and long-range components of SERS to the study of the structure and function of membrane
proteins. J. Raman Spectrosc. 21:49–53
Oluwole, A.O., Danielczak, B., Meister, A., Babalola, J.O., Vargas, C., Keller, S. (2017) Solubilization of membrane
proteins into functional lipid-bilayer nanodiscs using a diisobutylene/maleic acid copolymer. Angew. Chem. Int.
Ed. Engl. 56:1919–1924.
Opačić, M., Durand, G., Bosco, M., Polidori, A., Popot, J.-L. (2014a) Amphipols and photosynthetic light-harvesting
pigment-protein complexes. J. Membr. Biol. 247:1031–1041.
Opačić, M., Giusti, F., Broos, J., Popot, J.-L. (2014b) Isolation of Escherichia coli mannitol permease, EII
mtl , trapped in
amphipol A8-35 and fluorescein-labeled A8-35. J. Membr. Biol. 247:1019–1030.
Orwick-Rydmark, M., Lovett, J.E., Graziadei, A., Lindholm, L., Hicks, M.R., Watts, A. (2012) Detergent-free
incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional
and biophysical studies. Nano Lett. 12:4687–4692.
Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L., Champeil, P. (2006) Protective
and inhibitory effects of various types of amphipols on the Ca
2+ -ATPase from sarcoplasmic reticulum: a comparative
study. Biochemistry 45:1861–1869.
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.
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.
Polovinkin, V., Balandin, T., Volkov, O., Round, E., Borshchevskiy, V., Utrobin, P., von Stetten, D., Royant, A.,
Willbold, D., Arzumanyan, A., Popot, J.-L., Gordeliy, V. (2014) Nanoparticle surface-enhanced Raman scattering of
bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
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.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslow, R.A., Dafforn, T.R., Baldwin, S.A., Muench, S.P. (2015) The
use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.
Biochim. Biophys. Acta 1848:496–501.
Rahmeh, R., Damian, M., Cottet, M., Orcel, H., Mendre, C., Durroux, T., Sharma, K.S., Durand, G., Pucci, B., Trinquet,
E., Zwier, J.M., Deupi, X., Bron, P., Banères JL., Mouillac, B., Granier, S. (2012) Structural insights into biased G
protein-coupled receptor signaling revealed by fluorescence spectroscopy. Proc. Natl. Acad. Sci. USA
109:6733–6738.
Richter, K., Haslbeck, M., Buchner, J. (2010) The heat shock response: Life on the verge of death. Molec. Cell
40:253–266.
Scheidelaar, S., Koorengevel, M.C., Pardo, J.D., Meeldijk, J.D., Breukink, E., Killian, J.A. (2015) Molecular model for
the solubilization of membranes into nanodisks by styrene-maleic acid copolymers. Biophys. J. 108:279–290.
Sebai, S., Cribier, S., Karimi, A., Massotte, D., Tribet, T. (2010) Permeabilisation of lipid membranes and cells by a lightresponsive copolymer. Langmuir 26:14135–14141.
Sebai, S., Milioni, D., Walrant, A., Alves, I., Sagan, S., Huin, C., Auvray, L., Massotte, D., Cribier, S., Tribet, C. (2012)
Photocontrol of the translocation of molecules, peptides, and quantum dots through cell and lipid membranes doped
with azobenzene copolymers. Angew. Chem. Int. Ed. 51:2132–2136.
Shinzawa-Itoh, K., Shimomura, H., Yanagisawa, S., Shimada, S., Takahashi, R., Oosaki, M., Ogura, T., Tsukihara,
T. (2016) Purification of active respiratory supercomplex from bovine heart mitochondria enables functional studies.
J. Biol. Chem. 291:4178–4184.
Smirnova, I.A., Sjöstrand, D., Li, F., Björck, M., Schäfer, J., Östbye, H., Högbom, M., von Ballmoos, C., Lander, G.,
Ädelroth, P., Brzezinski, P. (2016) Isolation of yeast Complex IV in native lipid nanodiscs. Biochim. Biophys. Acta
1858:2984–2992.
Smith, S.O., Lugtenburg, J., Mathies, R.A. (1985) Determination of retinal chromophore structure in bacteriorhodopsin
with resonance Raman spectroscopy. J. Membr. Biol. 85:95–109.
Stangl, M., Hemmelmann, M., Allmeroth, M., Zentel, R., Schneider, D. (2014a) A minimal hydrophobicity is needed to
employ amphiphilic p(HPMA)-co-p(LMA) random copolymers in membrane research. Biochemistry 53:1410–1419.
References
403
receptor pharmacology: What are they good for? J. Membr. Biol. 247:853–860.
Nabiev, I.R., Efremóv, R.G., Chumanov, G.D. (1985) The chromophore-binding site of bacteriorhodopsin. Resonance
Raman and surface-enhanced resonance Raman spectroscopy and quantum chemical study. J. Biosci. 8:363–374.
Nabiev, I.R., Chumanov, G.D., Efremóv, R.G. (1990) Surface-enhanced Raman spectroscopy of biomolecules. Part
II. Application of short- and long-range components of SERS to the study of the structure and function of membrane
proteins. J. Raman Spectrosc. 21:49–53
Oluwole, A.O., Danielczak, B., Meister, A., Babalola, J.O., Vargas, C., Keller, S. (2017) Solubilization of membrane
proteins into functional lipid-bilayer nanodiscs using a diisobutylene/maleic acid copolymer. Angew. Chem. Int.
Ed. Engl. 56:1919–1924.
Opačić, M., Durand, G., Bosco, M., Polidori, A., Popot, J.-L. (2014a) Amphipols and photosynthetic light-harvesting
pigment-protein complexes. J. Membr. Biol. 247:1031–1041.
Opačić, M., Giusti, F., Broos, J., Popot, J.-L. (2014b) Isolation of Escherichia coli mannitol permease, EII
mtl , trapped in
amphipol A8-35 and fluorescein-labeled A8-35. J. Membr. Biol. 247:1019–1030.
Orwick-Rydmark, M., Lovett, J.E., Graziadei, A., Lindholm, L., Hicks, M.R., Watts, A. (2012) Detergent-free
incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional
and biophysical studies. Nano Lett. 12:4687–4692.
Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L., Champeil, P. (2006) Protective
and inhibitory effects of various types of amphipols on the Ca
2+ -ATPase from sarcoplasmic reticulum: a comparative
study. Biochemistry 45:1861–1869.
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.
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.
Polovinkin, V., Balandin, T., Volkov, O., Round, E., Borshchevskiy, V., Utrobin, P., von Stetten, D., Royant, A.,
Willbold, D., Arzumanyan, A., Popot, J.-L., Gordeliy, V. (2014) Nanoparticle surface-enhanced Raman scattering of
bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
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.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslow, R.A., Dafforn, T.R., Baldwin, S.A., Muench, S.P. (2015) The
use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.
Biochim. Biophys. Acta 1848:496–501.
Rahmeh, R., Damian, M., Cottet, M., Orcel, H., Mendre, C., Durroux, T., Sharma, K.S., Durand, G., Pucci, B., Trinquet,
E., Zwier, J.M., Deupi, X., Bron, P., Banères JL., Mouillac, B., Granier, S. (2012) Structural insights into biased G
protein-coupled receptor signaling revealed by fluorescence spectroscopy. Proc. Natl. Acad. Sci. USA
109:6733–6738.
Richter, K., Haslbeck, M., Buchner, J. (2010) The heat shock response: Life on the verge of death. Molec. Cell
40:253–266.
Scheidelaar, S., Koorengevel, M.C., Pardo, J.D., Meeldijk, J.D., Breukink, E., Killian, J.A. (2015) Molecular model for
the solubilization of membranes into nanodisks by styrene-maleic acid copolymers. Biophys. J. 108:279–290.
Sebai, S., Cribier, S., Karimi, A., Massotte, D., Tribet, T. (2010) Permeabilisation of lipid membranes and cells by a lightresponsive copolymer. Langmuir 26:14135–14141.
Sebai, S., Milioni, D., Walrant, A., Alves, I., Sagan, S., Huin, C., Auvray, L., Massotte, D., Cribier, S., Tribet, C. (2012)
Photocontrol of the translocation of molecules, peptides, and quantum dots through cell and lipid membranes doped
with azobenzene copolymers. Angew. Chem. Int. Ed. 51:2132–2136.
Shinzawa-Itoh, K., Shimomura, H., Yanagisawa, S., Shimada, S., Takahashi, R., Oosaki, M., Ogura, T., Tsukihara,
T. (2016) Purification of active respiratory supercomplex from bovine heart mitochondria enables functional studies.
J. Biol. Chem. 291:4178–4184.
Smirnova, I.A., Sjöstrand, D., Li, F., Björck, M., Schäfer, J., Östbye, H., Högbom, M., von Ballmoos, C., Lander, G.,
Ädelroth, P., Brzezinski, P. (2016) Isolation of yeast Complex IV in native lipid nanodiscs. Biochim. Biophys. Acta
1858:2984–2992.
Smith, S.O., Lugtenburg, J., Mathies, R.A. (1985) Determination of retinal chromophore structure in bacteriorhodopsin
with resonance Raman spectroscopy. J. Membr. Biol. 85:95–109.
Stangl, M., Hemmelmann, M., Allmeroth, M., Zentel, R., Schneider, D. (2014a) A minimal hydrophobicity is needed to
employ amphiphilic p(HPMA)-co-p(LMA) random copolymers in membrane research. Biochemistry 53:1410–1419.
References
403