Malhotra, K., Alder, N.N. (2014) Advances in the use of nanoscale bilayers to study membrane protein structure and
function. Biotechnol. Genet. Eng. Rev. 30:79–93.
Marcotte, I., Auger, M. (2005) Bicelles as model membranes for solid- and solution-state NMR studies of membrane
peptides and proteins. Concepts Magn. Reson. 24A:17–37.
Marty, M.T., Hoi, K.K., Robinson, C.V. (2016) Interfacing membrane mimetics with mass spectrometry. Acc. Chem.
Res. 49:2459–2467.
Marty, M.T., Wilcox, K.C., Klein, W.L., Sligar, S.G. (2013) Nanodisc-solubilized membrane protein library reflects the
membrane proteome. Anal. Bioanal. Chem. 405:4009–4016.
Matsumoto, K., Vaughn, M., Bruce, B.D., Koutsopoulos, S., Zhang, S. (2009) Designer peptide surfactants stabilize
functional photosystem I membrane complex in aqueous solution for extended time. J. Phys. Chem. B 113:75–83.
Matthies, D., Dalmas, O., Borgnia, M.J., Dominik, P.K., Merk, A., Rao, P., Reddy, B.G., Islam, S., Bartesaghi, A.,
Perozo, E., Subramaniam, S. (2016) Cryo-EM structures of the magnesium channel CorA reveal symmetry break
upon gating. Cell 164:747–756.
McGregor, C.-L., Chen, L., Pomroy, N.C., Hwang, P., Go, S., Chakrabartty, A., Privé, G.G. (2003) Lipopeptide
detergents designed for the structural study of membrane proteins. Nat. Biotechnol. 21:171–176.
McKibbin, C., Farmer, N.A., Edwards, P.C., Villa, C., Booth, P.J. (2009) Urea unfolding of opsin in phospholipid
bicelles. Photochem. Photobiol. 85:494–500.
McKibbin, C., Farmer, N.A., Jeans, C., Reeves, P.J., Khorana, H.G., Wallace, B.A., Edwards, P.C., Villa, C., Booth,
P.J. (2007) Opsin stability and folding: modulation by phospholipid bicelles. J. Mol. Biol. 374:1319–1332.
Midtgaard, S.R., Pedersen, M.C., Kirkensgaard, J.J.K., Sorensen, K.K., Mortensen, K., Jensen, K.J., Arleth, L. (2014)
Self-assembling peptides form nanodiscs that stabilize membrane proteins. Soft Matter 10:738–752.
Mineev, K.S., Goncharuk, S.A., Kuzmichev, P.K., Vilar, M., Arseniev, A.S. (2015) NMR dynamics of transmembrane
and intracellular domains of p75NTR in lipid-protein nanodiscs. Biophys. J. 109:772–782.
Mineev, K.S., Nadezhdin, K.D. (2017) Membrane mimetics for solution NMR studies of membrane proteins. Nanotech.
Rev. 6:15–32.
Mineev, K.S., Nadezhdin, K.D., Goncharuk, S.A., Arseniev, A.S. (2017) Facade detergents as bicelle rim-forming agents
for solution NMR spectroscopy. Nanotech. Rev. 6:93–103.
Mitra, N., Liu, Y., Liu, J., Serebryany, E., Mooney, V., DeVree, B.T., Sunahara, R.K., Yan, E.C.Y. (2013) Calciumdependent ligand binding and G protein signaling of family B GPCR parathyroid hormone 1 receptor purified in
nanodiscs. ACS Chem. Biol. 8:617–625.
Miyazaki, M., Nakano, M., Fukuda, M., Handa, T. (2009) Smaller discoidal high-density lipoprotein particles form
saddle surfaces, but not planar bilayers. Biochemistry 48:7756–7763.
Mizrachi, D., Robinson, M.-P., Ren, G., Ke, N., Berkmen, M., DeLisa, M.P. (2017) A water-soluble DsbB variant that
catalyzes disulfide-bond formation in vivo. Nat. Chem. Biol. 13:1022–1028.
Morgado, L., Zeth, K., Burmann, B.M., Maier, T., Hiller, S. (2015) Characterization of the insertase BamA in three
different membrane mimetics by solution NMR spectroscopy. J. Biomol. NMR 61:333–345.
Morrison, E.A., DeKoster, G.T., Dutta, S., Vafabakhsh, R., Clarkson, M.W., Bahl, A., Kern, D., Ha, T., HenzlerWildman, K.A. (2011) Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature
481:45–50.
Morrison, E.A., Henzler-Wildman, K.A. (2012) Reconstitution of integral membrane proteins into isotropic bicelles with
improved sample stability and expanded lipid composition profile. Biochim. Biophys. Acta 1818:814–820.
Mörs, K., Roos, C., Scholz, F., Wachtveitl, J., Dötsch, V., Bernhard, F., Glaubitz, C. (2013) Modified lipid and protein
dynamics in nanodiscs. Biochim. Biophys. Acta 1828:1222–1229.
Mukerjee, P. (1994) Fluorocarbon-hydrocarbon interactions in micelles and other lipid assemblies, at interfaces, and in
solutions. Colloids Surf. A 84:1–10.
Muller, K. (1981) Structural dimorphism in bile salt/lecithin mixed micelles. X-ray structural analysis. Biochemistry
20:404–414.
Nakano, T.Y., Sugihara, G., Nakashima, T., Yu, S.C. (2002) Thermodynamic study of mixed hydrocarbon/fluorocarbon
surfactant system by conductometric and fluorimetric techniques. Langmuir 18:8777–8785.
Nasr, M.L., Baptista, D., Strauss, M., Sun, Z.J., Grigoriu, S., Huser, S., Plückthun, A., Hagn, F., Walz, T., Hogle, J.M.,
Wagner, G. (2017) Covalently circularized nanodiscs for studying membrane proteins and viral entry. Nat. Meth.
14:49–52.
Nath, A., Atkins, W.M., Sligar, S.G. (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes
and membrane proteins. Biochemistry 46:2059–2069.
Nath, A., Koo, P.K., Rhoades, E., Atkins, W.M. (2008) Allosteric effects on substrate dissociation from cytochrome
P450 3A4 in nanodiscs observed by ensemble and single-molecule fluorescence spectroscopy. J. Am. Chem. Soc.
130:15746–15747.
References
143
function. Biotechnol. Genet. Eng. Rev. 30:79–93.
Marcotte, I., Auger, M. (2005) Bicelles as model membranes for solid- and solution-state NMR studies of membrane
peptides and proteins. Concepts Magn. Reson. 24A:17–37.
Marty, M.T., Hoi, K.K., Robinson, C.V. (2016) Interfacing membrane mimetics with mass spectrometry. Acc. Chem.
Res. 49:2459–2467.
Marty, M.T., Wilcox, K.C., Klein, W.L., Sligar, S.G. (2013) Nanodisc-solubilized membrane protein library reflects the
membrane proteome. Anal. Bioanal. Chem. 405:4009–4016.
Matsumoto, K., Vaughn, M., Bruce, B.D., Koutsopoulos, S., Zhang, S. (2009) Designer peptide surfactants stabilize
functional photosystem I membrane complex in aqueous solution for extended time. J. Phys. Chem. B 113:75–83.
Matthies, D., Dalmas, O., Borgnia, M.J., Dominik, P.K., Merk, A., Rao, P., Reddy, B.G., Islam, S., Bartesaghi, A.,
Perozo, E., Subramaniam, S. (2016) Cryo-EM structures of the magnesium channel CorA reveal symmetry break
upon gating. Cell 164:747–756.
McGregor, C.-L., Chen, L., Pomroy, N.C., Hwang, P., Go, S., Chakrabartty, A., Privé, G.G. (2003) Lipopeptide
detergents designed for the structural study of membrane proteins. Nat. Biotechnol. 21:171–176.
McKibbin, C., Farmer, N.A., Edwards, P.C., Villa, C., Booth, P.J. (2009) Urea unfolding of opsin in phospholipid
bicelles. Photochem. Photobiol. 85:494–500.
McKibbin, C., Farmer, N.A., Jeans, C., Reeves, P.J., Khorana, H.G., Wallace, B.A., Edwards, P.C., Villa, C., Booth,
P.J. (2007) Opsin stability and folding: modulation by phospholipid bicelles. J. Mol. Biol. 374:1319–1332.
Midtgaard, S.R., Pedersen, M.C., Kirkensgaard, J.J.K., Sorensen, K.K., Mortensen, K., Jensen, K.J., Arleth, L. (2014)
Self-assembling peptides form nanodiscs that stabilize membrane proteins. Soft Matter 10:738–752.
Mineev, K.S., Goncharuk, S.A., Kuzmichev, P.K., Vilar, M., Arseniev, A.S. (2015) NMR dynamics of transmembrane
and intracellular domains of p75NTR in lipid-protein nanodiscs. Biophys. J. 109:772–782.
Mineev, K.S., Nadezhdin, K.D. (2017) Membrane mimetics for solution NMR studies of membrane proteins. Nanotech.
Rev. 6:15–32.
Mineev, K.S., Nadezhdin, K.D., Goncharuk, S.A., Arseniev, A.S. (2017) Facade detergents as bicelle rim-forming agents
for solution NMR spectroscopy. Nanotech. Rev. 6:93–103.
Mitra, N., Liu, Y., Liu, J., Serebryany, E., Mooney, V., DeVree, B.T., Sunahara, R.K., Yan, E.C.Y. (2013) Calciumdependent ligand binding and G protein signaling of family B GPCR parathyroid hormone 1 receptor purified in
nanodiscs. ACS Chem. Biol. 8:617–625.
Miyazaki, M., Nakano, M., Fukuda, M., Handa, T. (2009) Smaller discoidal high-density lipoprotein particles form
saddle surfaces, but not planar bilayers. Biochemistry 48:7756–7763.
Mizrachi, D., Robinson, M.-P., Ren, G., Ke, N., Berkmen, M., DeLisa, M.P. (2017) A water-soluble DsbB variant that
catalyzes disulfide-bond formation in vivo. Nat. Chem. Biol. 13:1022–1028.
Morgado, L., Zeth, K., Burmann, B.M., Maier, T., Hiller, S. (2015) Characterization of the insertase BamA in three
different membrane mimetics by solution NMR spectroscopy. J. Biomol. NMR 61:333–345.
Morrison, E.A., DeKoster, G.T., Dutta, S., Vafabakhsh, R., Clarkson, M.W., Bahl, A., Kern, D., Ha, T., HenzlerWildman, K.A. (2011) Antiparallel EmrE exports drugs by exchanging between asymmetric structures. Nature
481:45–50.
Morrison, E.A., Henzler-Wildman, K.A. (2012) Reconstitution of integral membrane proteins into isotropic bicelles with
improved sample stability and expanded lipid composition profile. Biochim. Biophys. Acta 1818:814–820.
Mörs, K., Roos, C., Scholz, F., Wachtveitl, J., Dötsch, V., Bernhard, F., Glaubitz, C. (2013) Modified lipid and protein
dynamics in nanodiscs. Biochim. Biophys. Acta 1828:1222–1229.
Mukerjee, P. (1994) Fluorocarbon-hydrocarbon interactions in micelles and other lipid assemblies, at interfaces, and in
solutions. Colloids Surf. A 84:1–10.
Muller, K. (1981) Structural dimorphism in bile salt/lecithin mixed micelles. X-ray structural analysis. Biochemistry
20:404–414.
Nakano, T.Y., Sugihara, G., Nakashima, T., Yu, S.C. (2002) Thermodynamic study of mixed hydrocarbon/fluorocarbon
surfactant system by conductometric and fluorimetric techniques. Langmuir 18:8777–8785.
Nasr, M.L., Baptista, D., Strauss, M., Sun, Z.J., Grigoriu, S., Huser, S., Plückthun, A., Hagn, F., Walz, T., Hogle, J.M.,
Wagner, G. (2017) Covalently circularized nanodiscs for studying membrane proteins and viral entry. Nat. Meth.
14:49–52.
Nath, A., Atkins, W.M., Sligar, S.G. (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes
and membrane proteins. Biochemistry 46:2059–2069.
Nath, A., Koo, P.K., Rhoades, E., Atkins, W.M. (2008) Allosteric effects on substrate dissociation from cytochrome
P450 3A4 in nanodiscs observed by ensemble and single-molecule fluorescence spectroscopy. J. Am. Chem. Soc.
130:15746–15747.
References
143