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
Cecchini, M., Changeux, J.-P. (2015) The nicotinic acetylcholine receptor and its prokaryotic homologues: Structure,
conformational transitions & allosteric modulation. Neuropharmacology 96:137–149.
Cevc, G., Marsh, D. (1987) Phospholipid Bilayers: Physical Principles and Models. Wiley, New York, 442 p.
Chang, G., Spencer, R.H., Lee, A.T., Barclay, M.T., Rees, D.C. (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220–2226.
Changeux, J.-P. (2012) The nicotinic acetylcholine receptor: The founding father of the pentameric ligand-gated ion
channel superfamily. J. Biol. Chem. 287:40207–40215.
Changeux, J.-P., Corringer, P.-J., Maskos, U. (2015) The nicotinic acetylcholine receptor: From molecular biology to
cognition. Neuropharmacology 96:135–136.
Changeux, J.-P., Edelstein, S.J. (2005) Nicotinic Acetylcholine Receptors: From Molecular Biology to Cognition. Odile
Jacob Publishing Corporation, New York, 284 p.
Clark, K.M., Jenkins, J.L., Fedoriw, N., Dumont, M.E. (2017) Human CaaX protease ZMPSTE24 expressed in yeast:
Structure and inhibition by HIV protease inhibitors. Protein Sci. 26:242–257.
Clegg, J.S. (1983) What is the cytosol? Trends Biochem. Sci. 8:436–437.
Collinson, I., Corey, R.A., Allen, W.J. (2015) Channel crossing: how are proteins shipped across the bacterial plasma
membrane? Philos. Trans. R. Soc. B 370:20150025.
Corringer, P.-J., Poitevin, F., Prévost, M.S., Sauguet, L., Delarue, M., Changeux, J.-P. (2012) Structure and pharmacology of pentameric receptor channels: from bacteria to brain. Structure 20:941–956.
Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., Rosenbusch, J.P. (1992)
Crystal structures explain functional properties of two E. coli porins. Nature 358:727–733.
Cymer, F., von Heijne, G., White, S.H. (2015) Mechanisms of integral membrane protein insertion and folding. J. Mol.
Biol. 427:999–1022.
daCosta, C.J.B., Baenziger, F.E. (2013) Gating of pentameric ligand-gated ion channels: Structural insights and
ambiguities. Structure 21:1271–1283.
daCosta, C.J.B., Baenziger, J.E. (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol.
Chem. 284:17819–17825.
Debnath, D., Nielsen, K.L., Otzen, D.E. (2010) In vitro association of fragments of a β-sheet membrane protein. Biophys.
Chem. 148:112–120.
Deisenhofer, J., Epp, O., Miki, K., Huber, R., Michel, H. (1985) Structure of the protein subunits in the photosynthetic
reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature 318:618–624.
Dilger, J.P., Fisher, L.R., Haydon, D.A. (1982) A critical comparison of electrical and optical methods for bilayer
thickness determination. Chem. Phys. Lipids 30:159–176.
Doyle, D.A., Cabral, J.M., Pfuetzner, R.A., Kuo, A., Gulbis, J.M., Cohen, S.L., Chait, B.T., MacKinnon, R. (1998) The
structure of the potassium channel: Molecular basis of K
+ conduction and selectivity. Science 280:69–77.
Dracheva, S., Bose, S., Hendler, R.W. (1996) Chemical and functional studies on the importance of purple membrane
lipids in bacteriorhodopsin photocycle behavior. FEBS Lett. 382:209–212.
Drachmann, N.D., Olesen, C., Møller, J.V., Guo, Z., Nissen, P., Bublitz, M. (2014) Comparing crystal structures of Ca
2+ -
ATPase in the presence of different lipids. FEBS J. 281:4249–4262.
Du, J., Lü, W., Wu, S., Cheng, Y., Gouaux, E. (2015) Glycine receptor mechanism elucidated by electron cryomicroscopy. Nature 526:224–229.
Efremov, R.G., Baradaran, R., Sazanov, L.A. (2010) The architecture of respiratory complex I. Nature 465:441–445.
Engelman, D.M. (2005) Membranes are more mosaic than fluid. Nature 438:578–580.
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.
Engelman, D.M., Steitz, T.A. (1981) The spontaneous insertion of proteins into and across membranes: the helical
hairpin hypothesis. Cell 23:411–422.
Fernández, C., Hilty, C., Wider, G., Wüthrich, K. (2002) Lipid-protein interactions in DHPC micelles containing the
integral membrane protein OmpX investigated by NMR spectroscopy. Proc. Natl. Acad. Sci. USA 99:13533–13537.
Ferrand, M., Dianoux, A.J., Petry, W., Zaccai, G. (1993) Thermal motions and function of bacteriorhodopsin in purple
membranes: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA
90:9668–9672.
Fyfe, P.K., McAuley, K.E., Roszak, A.W., Isaacs, N.W., Cogdell, R.J., Jones, M.R. (2001) Probing the interface between
membrane proteins and membrane lipids by X-ray crystallography. Trends Biochem. Sci. 26:106–112.
Gonen, T., Cheng, Y., Sliz, P., Hiroaki, Y., Fujiyoshi, Y., Harrison, S.C., Walz, T. (2005) Lipid-protein interactions in
double-layered two-dimensional AQP0 crystals. Nature 438:633–638.
52
1 Membrane Proteins and Their Natural Environment
J.-L., Catoire, L.J. (2016) Functional modulation of a GPCR conformational landscape in a lipid bilayer. J. Am.
Chem. Soc. 138:11170–11175
Cecchini, M., Changeux, J.-P. (2015) The nicotinic acetylcholine receptor and its prokaryotic homologues: Structure,
conformational transitions & allosteric modulation. Neuropharmacology 96:137–149.
Cevc, G., Marsh, D. (1987) Phospholipid Bilayers: Physical Principles and Models. Wiley, New York, 442 p.
Chang, G., Spencer, R.H., Lee, A.T., Barclay, M.T., Rees, D.C. (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220–2226.
Changeux, J.-P. (2012) The nicotinic acetylcholine receptor: The founding father of the pentameric ligand-gated ion
channel superfamily. J. Biol. Chem. 287:40207–40215.
Changeux, J.-P., Corringer, P.-J., Maskos, U. (2015) The nicotinic acetylcholine receptor: From molecular biology to
cognition. Neuropharmacology 96:135–136.
Changeux, J.-P., Edelstein, S.J. (2005) Nicotinic Acetylcholine Receptors: From Molecular Biology to Cognition. Odile
Jacob Publishing Corporation, New York, 284 p.
Clark, K.M., Jenkins, J.L., Fedoriw, N., Dumont, M.E. (2017) Human CaaX protease ZMPSTE24 expressed in yeast:
Structure and inhibition by HIV protease inhibitors. Protein Sci. 26:242–257.
Clegg, J.S. (1983) What is the cytosol? Trends Biochem. Sci. 8:436–437.
Collinson, I., Corey, R.A., Allen, W.J. (2015) Channel crossing: how are proteins shipped across the bacterial plasma
membrane? Philos. Trans. R. Soc. B 370:20150025.
Corringer, P.-J., Poitevin, F., Prévost, M.S., Sauguet, L., Delarue, M., Changeux, J.-P. (2012) Structure and pharmacology of pentameric receptor channels: from bacteria to brain. Structure 20:941–956.
Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., Rosenbusch, J.P. (1992)
Crystal structures explain functional properties of two E. coli porins. Nature 358:727–733.
Cymer, F., von Heijne, G., White, S.H. (2015) Mechanisms of integral membrane protein insertion and folding. J. Mol.
Biol. 427:999–1022.
daCosta, C.J.B., Baenziger, F.E. (2013) Gating of pentameric ligand-gated ion channels: Structural insights and
ambiguities. Structure 21:1271–1283.
daCosta, C.J.B., Baenziger, J.E. (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol.
Chem. 284:17819–17825.
Debnath, D., Nielsen, K.L., Otzen, D.E. (2010) In vitro association of fragments of a β-sheet membrane protein. Biophys.
Chem. 148:112–120.
Deisenhofer, J., Epp, O., Miki, K., Huber, R., Michel, H. (1985) Structure of the protein subunits in the photosynthetic
reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature 318:618–624.
Dilger, J.P., Fisher, L.R., Haydon, D.A. (1982) A critical comparison of electrical and optical methods for bilayer
thickness determination. Chem. Phys. Lipids 30:159–176.
Doyle, D.A., Cabral, J.M., Pfuetzner, R.A., Kuo, A., Gulbis, J.M., Cohen, S.L., Chait, B.T., MacKinnon, R. (1998) The
structure of the potassium channel: Molecular basis of K
+ conduction and selectivity. Science 280:69–77.
Dracheva, S., Bose, S., Hendler, R.W. (1996) Chemical and functional studies on the importance of purple membrane
lipids in bacteriorhodopsin photocycle behavior. FEBS Lett. 382:209–212.
Drachmann, N.D., Olesen, C., Møller, J.V., Guo, Z., Nissen, P., Bublitz, M. (2014) Comparing crystal structures of Ca
2+ -
ATPase in the presence of different lipids. FEBS J. 281:4249–4262.
Du, J., Lü, W., Wu, S., Cheng, Y., Gouaux, E. (2015) Glycine receptor mechanism elucidated by electron cryomicroscopy. Nature 526:224–229.
Efremov, R.G., Baradaran, R., Sazanov, L.A. (2010) The architecture of respiratory complex I. Nature 465:441–445.
Engelman, D.M. (2005) Membranes are more mosaic than fluid. Nature 438:578–580.
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.
Engelman, D.M., Steitz, T.A. (1981) The spontaneous insertion of proteins into and across membranes: the helical
hairpin hypothesis. Cell 23:411–422.
Fernández, C., Hilty, C., Wider, G., Wüthrich, K. (2002) Lipid-protein interactions in DHPC micelles containing the
integral membrane protein OmpX investigated by NMR spectroscopy. Proc. Natl. Acad. Sci. USA 99:13533–13537.
Ferrand, M., Dianoux, A.J., Petry, W., Zaccai, G. (1993) Thermal motions and function of bacteriorhodopsin in purple
membranes: effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA
90:9668–9672.
Fyfe, P.K., McAuley, K.E., Roszak, A.W., Isaacs, N.W., Cogdell, R.J., Jones, M.R. (2001) Probing the interface between
membrane proteins and membrane lipids by X-ray crystallography. Trends Biochem. Sci. 26:106–112.
Gonen, T., Cheng, Y., Sliz, P., Hiroaki, Y., Fujiyoshi, Y., Harrison, S.C., Walz, T. (2005) Lipid-protein interactions in
double-layered two-dimensional AQP0 crystals. Nature 438:633–638.
52
1 Membrane Proteins and Their Natural Environment