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function and dynamics of biological membranes after more than 40 years. Biochim. Biophys. Acta 1838:1451–1466.
Nogi, T., Fathir, I., Kobayashi, M., Nozawa, T., Miki, K. (2000) Crystal structures of photosynthetic reaction center and
high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl.
Acad. Sci. USA 97:13561–13566.
Norimatsu, Y., Hasegawa, K., Shimizu, N., Toyoshima, C. (2017) Protein-phospholipid interplay revealed with crystals
of a calcium pump. Nature 545:193–198.
Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J.M., Delarue,
M., Corringer, P.-J. (2011) X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel.
Nature 469:428–431.
Nys, M., Kesters, D., Ulens, C. (2013) Structural insights into Cys-loop receptor function and ligand recognition.
Biochim. Biophys. Acta 86:1042–1053.
Obara, K., Miyashita, N., Xu, C., Toyoshima, I., Sugita, Y., Inesi, G., Toyoshima, C. (2005) Structural role of
countertransport revealed in Ca
2+ pump crystal structure in the absence of Ca
2+ . Proc. Natl. Acad. Sci. USA
102:14489–14496.
Opekarová, M., Tanner, W. (2003) Specific lipid requirements of membrane proteins – a putative bottleneck in
heterologous expression. Biochim. Biophys. Acta 1610:11–22.
Ostermeier, C., Harrenga, A., Ermler, U., Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans
two-subunit cytochrome c oxidase complexed with an antibody F v fragment. Proc. Natl. Acad. Sci. USA
94:10547–10553.
Otzen, D.E., Andersen, K.K. (2013) Folding of outer membrane proteins. Arch. Biochem. Biophys. 531:34–43.
Palsdottir, H., Hunte, C. (2004) Lipids in membrane protein structures. Biochim. Biophys. Acta 1666:2–18.
Pankratov, Y., Lalo, U. (2014) Calcium permeability of ligand-gated Ca
2+ channels. Eur. J. Pharmacol. 739:60–73.
Park, E., Rapoport, T.A. (2012) Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu.
Rev. Biophys. 41:21–40.
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P., Landau, E. (1997) X-ray structure of bacteriorhodopsin at 2.5 Å from
microcrystals grown in lipidic cubic phases. Science 277:1676–1881.
Pedersen, P.L. (2007) Transport ATPases into the year 2008: a brief overview related to types, structures, functions and
roles in health and disease. J. Bioenerg. Biomem. 39:349–355.
Peters, R. (1986) Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility.
Biochim. Biophys. Acta 864:305–359.
Phillips, R., Ursell, T., Wiggins, P., Sens, P. (2009) Emerging roles for lipids in shaping membrane protein function.
Nature 459:379–385.
Planas-Iglesias, J., Dwarakanath, H., Mohammadyani, D., Yanamala, N., Kagan, V.E., Klein-Seetharaman, J. (2015)
Cardiolipin interactions with proteins. Biophys. J. 109:1282–1294.
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.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., de Vitry, C. (1990) On the microassembly of integral membrane proteins. Annu. Rev. Biophys. Biophys.
Chem. 19:369–403.
Popot, J.-L., Engelman, D.M. (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry
29:4031–4037.
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.
Prévost, M.S., Sauguet, L., Nury, H., Van Renterghem, C., Huon, C., Poitevin, F., Baaden, M., Delarue, M., Corringer,
P.-J. (2012) A locally closed conformation of a bacterial pentameric proton-gated ion channel. Nat. Struct. Molec.
Biol. 19:642–649.
Prince, S.M., Papiz, M.Z., Freer, A.A., McDermott, G., Hawthornwaite-Lawless, A.M., Cogdell, R.J., Isaacs,
N.W. (1997) Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050 : modular
assembly and protein-pigment interactions. J. Mol. Biol. 268:412–423.
Pryor, E.E., Jr., Horanyi, P.S., Clark, K.M., Fedoriw, N., Connelly, S.M., Koszelak-Rosenblum, M., Zhu, G.,
Malkowski, M.G., Wiener, M.C., Dumont, M.E. (2013) Structure of the integral membrane protein CAAX protease
Ste24p. Science 339:1600–1604.
Qin, L., Hiser, C., Mulichak, A., Garavito, R.M., Ferguson-Miller, S. (2006) Identification of conserved lipid/detergentbinding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc. Natl. Acad. Sci. USA
103:16117–16122.
References
55
function and dynamics of biological membranes after more than 40 years. Biochim. Biophys. Acta 1838:1451–1466.
Nogi, T., Fathir, I., Kobayashi, M., Nozawa, T., Miki, K. (2000) Crystal structures of photosynthetic reaction center and
high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl.
Acad. Sci. USA 97:13561–13566.
Norimatsu, Y., Hasegawa, K., Shimizu, N., Toyoshima, C. (2017) Protein-phospholipid interplay revealed with crystals
of a calcium pump. Nature 545:193–198.
Nury, H., Van Renterghem, C., Weng, Y., Tran, A., Baaden, M., Dufresne, V., Changeux, J.-P., Sonner, J.M., Delarue,
M., Corringer, P.-J. (2011) X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel.
Nature 469:428–431.
Nys, M., Kesters, D., Ulens, C. (2013) Structural insights into Cys-loop receptor function and ligand recognition.
Biochim. Biophys. Acta 86:1042–1053.
Obara, K., Miyashita, N., Xu, C., Toyoshima, I., Sugita, Y., Inesi, G., Toyoshima, C. (2005) Structural role of
countertransport revealed in Ca
2+ pump crystal structure in the absence of Ca
2+ . Proc. Natl. Acad. Sci. USA
102:14489–14496.
Opekarová, M., Tanner, W. (2003) Specific lipid requirements of membrane proteins – a putative bottleneck in
heterologous expression. Biochim. Biophys. Acta 1610:11–22.
Ostermeier, C., Harrenga, A., Ermler, U., Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans
two-subunit cytochrome c oxidase complexed with an antibody F v fragment. Proc. Natl. Acad. Sci. USA
94:10547–10553.
Otzen, D.E., Andersen, K.K. (2013) Folding of outer membrane proteins. Arch. Biochem. Biophys. 531:34–43.
Palsdottir, H., Hunte, C. (2004) Lipids in membrane protein structures. Biochim. Biophys. Acta 1666:2–18.
Pankratov, Y., Lalo, U. (2014) Calcium permeability of ligand-gated Ca
2+ channels. Eur. J. Pharmacol. 739:60–73.
Park, E., Rapoport, T.A. (2012) Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu.
Rev. Biophys. 41:21–40.
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P., Landau, E. (1997) X-ray structure of bacteriorhodopsin at 2.5 Å from
microcrystals grown in lipidic cubic phases. Science 277:1676–1881.
Pedersen, P.L. (2007) Transport ATPases into the year 2008: a brief overview related to types, structures, functions and
roles in health and disease. J. Bioenerg. Biomem. 39:349–355.
Peters, R. (1986) Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility.
Biochim. Biophys. Acta 864:305–359.
Phillips, R., Ursell, T., Wiggins, P., Sens, P. (2009) Emerging roles for lipids in shaping membrane protein function.
Nature 459:379–385.
Planas-Iglesias, J., Dwarakanath, H., Mohammadyani, D., Yanamala, N., Kagan, V.E., Klein-Seetharaman, J. (2015)
Cardiolipin interactions with proteins. Biophys. J. 109:1282–1294.
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.
Popot, J.-L. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., de Vitry, C. (1990) On the microassembly of integral membrane proteins. Annu. Rev. Biophys. Biophys.
Chem. 19:369–403.
Popot, J.-L., Engelman, D.M. (1990) Membrane protein folding and oligomerization: the two-stage model. Biochemistry
29:4031–4037.
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.
Prévost, M.S., Sauguet, L., Nury, H., Van Renterghem, C., Huon, C., Poitevin, F., Baaden, M., Delarue, M., Corringer,
P.-J. (2012) A locally closed conformation of a bacterial pentameric proton-gated ion channel. Nat. Struct. Molec.
Biol. 19:642–649.
Prince, S.M., Papiz, M.Z., Freer, A.A., McDermott, G., Hawthornwaite-Lawless, A.M., Cogdell, R.J., Isaacs,
N.W. (1997) Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050 : modular
assembly and protein-pigment interactions. J. Mol. Biol. 268:412–423.
Pryor, E.E., Jr., Horanyi, P.S., Clark, K.M., Fedoriw, N., Connelly, S.M., Koszelak-Rosenblum, M., Zhu, G.,
Malkowski, M.G., Wiener, M.C., Dumont, M.E. (2013) Structure of the integral membrane protein CAAX protease
Ste24p. Science 339:1600–1604.
Qin, L., Hiser, C., Mulichak, A., Garavito, R.M., Ferguson-Miller, S. (2006) Identification of conserved lipid/detergentbinding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc. Natl. Acad. Sci. USA
103:16117–16122.
References
55