P. A. Maguire and M. J. Druse, The influence of cholesterol on synaptic fluidity, dopamine D1 binding and dopamine-stimulated adenylate cyclase, Brain Research Bulletin, vol.23, issue.1-2, pp.69-74, 1989.
DOI : 10.1016/0361-9230(89)90165-2

A. El-battari, E. Ah-kye, J. M. Muller, H. Sari, and J. Marvaldi, Modification of HT 29 cell response to the vasoactive intestinal peptide (VIP) by membrane fluidization, Biochimie, vol.67, issue.12, pp.1217-1223, 1985.
DOI : 10.1016/S0300-9084(85)80130-9

D. F. Lazar and F. Medzihradsky, Altered Microviscosity at Brain Membrane Surface Induces Distinct and Reversible Inhibition of Opioid Receptor Binding, Journal of Neurochemistry, vol.976, issue.4, pp.1233-1240, 1992.
DOI : 10.1111/j.1471-4159.1983.tb13567.x

S. O. Yesylevskyy, A. P. Demchenko, S. Kraszewski, and C. Ramseyer, Cholesterol Induces Uneven Curvature of Asymmetric Lipid Bilayers, The Scientific World Journal, vol.4, issue.3, p.965230, 2013.
DOI : 10.1021/ja076641c

URL : https://hal.archives-ouvertes.fr/hal-01666169

A. G. Lee, How lipids affect the activities of integral membrane proteins, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1666, issue.1-2, pp.62-87, 2004.
DOI : 10.1016/j.bbamem.2004.05.012

J. L. Popot, R. A. Demel, A. Sobel, L. L. Van-deenen, and J. P. Changeux, Preferential affinity of acetylcholine receptor protein for certain lipids studied using monolayer cultures, C. R. Acad. Sci. Hebd. Seances Acad. Sci. D, vol.285, pp.1005-1008, 1977.

F. J. Barrantes, Structural basis for lipid modulation of nicotinic acetylcholine receptor function, Brain Research Reviews, vol.47, issue.1-3, pp.71-95, 2004.
DOI : 10.1016/j.brainresrev.2004.06.008

C. J. Baier, J. Fantini, and F. J. Barrantes, 21907 | DOI: 10 Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor, Scientific RepoRts | Sci. Rep, vol.6, issue.1, p.69, 1038.

J. Fantini and F. J. Barrantes, How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains, Frontiers in Physiology, vol.4, p.31, 2013.
DOI : 10.3389/fphys.2013.00031

I. M. Posada, A Cholesterol Recognition Motif in Human Phospholipid Scramblase 1, Biophysical Journal, vol.107, issue.6, pp.1383-1392, 2014.
DOI : 10.1016/j.bpj.2014.07.039

M. A. Hanson, A Specific Cholesterol Binding Site Is Established by the 2.8 ?? Structure of the Human ??2-Adrenergic Receptor, Structure, vol.16, issue.6, pp.897-905, 2008.
DOI : 10.1016/j.str.2008.05.001

J. Fantini and F. J. Barrantes, Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1788, issue.11, pp.2345-2361, 2009.
DOI : 10.1016/j.bbamem.2009.08.016

URL : https://hal.archives-ouvertes.fr/hal-00481491

N. Jamin, Characterization of the Cholesterol Recognition Amino Acid Consensus Sequence of the Peripheral-Type Benzodiazepine Receptor, Molecular Endocrinology, vol.19, issue.3, pp.588-594, 2005.
DOI : 10.1210/me.2004-0308

R. M. Epand, Proteins and cholesterol-rich domains, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1778, issue.7-8, pp.1576-1582, 2008.
DOI : 10.1016/j.bbamem.2008.03.016

URL : https://doi.org/10.1016/j.bbamem.2008.03.016

R. M. Epand, A. Thomas, R. Brasseur, and R. F. Epand, Cholesterol Interaction with Proteins That Partition into Membrane Domains: An Overview, Subcell. Biochem, vol.51, pp.253-278, 2010.
DOI : 10.1007/978-90-481-8622-8_9

E. Strandberg and J. A. Killian, Snorkeling of lysine side chains in transmembrane helices: how easy can it get?, FEBS Letters, vol.35, issue.1-3, pp.69-73, 2003.
DOI : 10.1021/bi961770j

D. Scala, C. Chahinian, H. Yahi, N. Garmy, N. Fantini et al., Interaction of Alzheimer???s ??-Amyloid Peptides with Cholesterol: Mechanistic Insights into Amyloid Pore Formation, Biochemistry, vol.53, issue.28, pp.4489-4502, 2014.
DOI : 10.1021/bi500373k

G. Thakur, C. Pao, M. Micic, S. Johnson, and R. M. Leblanc, Surface chemistry of lipid raft and amyloid A?? (1-40) Langmuir monolayer, Colloids and Surfaces B: Biointerfaces, vol.87, issue.2, pp.369-377, 2011.
DOI : 10.1016/j.colsurfb.2011.05.047

N. Yahi and J. Fantini, Deciphering the Glycolipid Code of Alzheimer's and Parkinson's Amyloid Proteins Allowed the Creation of a Universal Ganglioside-Binding Peptide, PLoS ONE, vol.7, issue.8, p.104751, 2014.
DOI : 10.1371/journal.pone.0104751.t001

A. Seelig, Local anesthetics and pressure: a comparison of dibucaine binding to lipid monolayers and bilayers, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.899, issue.2, pp.196-204, 1987.
DOI : 10.1016/0005-2736(87)90400-7

J. Fantini, D. Carlus, and N. Yahi, The fusogenic tilted peptide (67???78) of ??-synuclein is a cholesterol binding domain, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1808, issue.10, pp.2343-2351, 2011.
DOI : 10.1016/j.bbamem.2011.06.017

P. T. Williamson, G. Zandomeneghi, F. J. Barrantes, A. Watts, and B. H. Meier, Structural and dynamic studies of the ??-M4 trans-membrane domain of the nicotinic acetylcholine receptor, Molecular Membrane Biology, vol.36, issue.6, pp.485-496, 2005.
DOI : 10.1021/bi972357u

M. Mehring, Principles of high-resolution NMR in solids, 1983.
DOI : 10.1007/978-3-642-68756-3

R. F. De-almeida, Cholesterol Modulates the Organization of the ??M4 Transmembrane Domain of the Muscle Nicotinic Acetylcholine Receptor, Biophysical Journal, vol.86, issue.4, pp.2261-2272, 2004.
DOI : 10.1016/S0006-3495(04)74284-8

L. Jaremko, M. Jaremko, K. Giller, S. Becker, and M. Zweckstetter, Structure of the Mitochondrial Translocator Protein in Complex with a Diagnostic Ligand, Science, vol.98, issue.18, pp.1363-1366, 2014.
DOI : 10.1073/pnas.181342398

J. J. Lacapere, Structural and Functional Study of Reconstituted Peripheral Benzodiazepine Receptor, Biochemical and Biophysical Research Communications, vol.284, issue.2, pp.536-541, 2001.
DOI : 10.1006/bbrc.2001.4975

V. Papadopoulos, Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function, Trends in Pharmacological Sciences, vol.27, issue.8, pp.402-409, 2006.
DOI : 10.1016/j.tips.2006.06.005

J. S. Harris, D. E. Epps, S. R. Davio, and F. J. Kezdy, Evidence for Transbilayer, Tail-to-Tail Cholesterol Dimers in Dipalmitoylglycerophosphocholine Liposomes, Biochemistry, vol.34, issue.11, pp.3851-3857, 1995.
DOI : 10.1021/bi00011a043

R. Rukmini, S. S. Rawat, S. C. Biswas, and A. Chattopadhyay, Cholesterol Organization in Membranes at Low Concentrations: Effects of Curvature Stress and Membrane Thickness, Biophysical Journal, vol.81, issue.4, pp.2122-2134, 2001.
DOI : 10.1016/S0006-3495(01)75860-2

M. Nishio, Y. Umezawa, J. Fantini, M. S. Weiss, and P. Chakrabarti, CH????? hydrogen bonds in biological macromolecules, Phys. Chem. Chem. Phys., vol.25, issue.Suppl. 2, pp.12648-12683, 2014.
DOI : 10.1080/10610278.2013.814779

M. Opekarova and W. Tanner, Specific lipid requirements of membrane proteins???a putative bottleneck in heterologous expression, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1610, issue.1, pp.11-22, 1610.
DOI : 10.1016/S0005-2736(02)00708-3

J. Czub and M. Baginski, Comparative Molecular Dynamics Study of Lipid Membranes Containing Cholesterol and Ergosterol, Biophysical Journal, vol.90, issue.7, pp.2368-2382, 2006.
DOI : 10.1529/biophysj.105.072801

M. Baginski, A. Tempczyk, and E. Borowski, Comparative conformational analysis of cholesterol and ergosterol by molecular mechanics, European Biophysics Journal, vol.599, issue.3, pp.159-166, 1989.
DOI : 10.1128/AAC.5.4.377

Z. Gál, Mutations of the central tyrosines of putative cholesterol recognition amino acid consensus (CRAC) sequences modify folding, activity, and sterol-sensing of the human ABCG2 multidrug transporter, Biochimica et Biophysica Acta (BBA) - Biomembranes, vol.1848, issue.2, pp.477-487, 2015.
DOI : 10.1016/j.bbamem.2014.11.006

A. Telbisz, C. Hegedüs, A. Váradi, B. Sarkadi, and C. Özvegy-laczka, Regulation of the Function of the Human ABCG2 Multidrug Transporter by Cholesterol and Bile Acids: Effects of Mutations in Potential Substrate and Steroid Binding Sites, Drug Metabolism and Disposition, vol.42, issue.4, pp.575-585, 2014.
DOI : 10.1124/dmd.113.055731

A. T. Clay, P. Lu, and F. J. Sharom, Interaction of the P-Glycoprotein Multidrug Transporter with Sterols, Biochemistry, vol.54, issue.43, pp.6586-6597, 2015.
DOI : 10.1021/acs.biochem.5b00904

S. G. Aller, Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding, Science, vol.44, issue.6, pp.1718-1722, 2009.
DOI : 10.1074/jbc.M609899200

J. Fantini and N. Yahi, Brain lipids in synaptic function and neurological disease. Clues to innovative therapeutic strategies for brain disorders, 2015.

J. Fantini, Bexarotene Blocks Calcium-Permeable Ion Channels Formed by Neurotoxic Alzheimer???s ??-Amyloid Peptides, ACS Chemical Neuroscience, vol.5, issue.3, pp.216-224, 2014.
DOI : 10.1021/cn400183w

URL : https://doi.org/10.1021/cn400183w

D. Scala and C. , Broad neutralization of calcium-permeable amyloid pore channels with a chimeric Alzheimer/Parkinson peptide targeting brain gangliosides, Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, vol.1862, issue.2, pp.213-222, 2016.
DOI : 10.1016/j.bbadis.2015.11.012

URL : https://hal.archives-ouvertes.fr/hal-01471935

A. W. Partridge, A. G. Therien, and C. M. Deber, Missense mutations in transmembrane domains of proteins: Phenotypic propensity of polar residues for human disease, Proteins: Structure, Function, and Bioinformatics, vol.18, issue.Suppl, pp.648-656, 2004.
DOI : 10.1002/elps.1150181505

B. R. Brooks, CHARMM: The biomolecular simulation program, Journal of Computational Chemistry, vol.103, issue.13, pp.1545-1614, 2009.
DOI : 10.1021/ci034261e

D. Scala and C. , Mechanism of cholesterol-assisted oligomeric channel formation by a short Alzheimer ??-amyloid peptide, Journal of Neurochemistry, vol.70, issue.1, pp.186-195, 2014.
DOI : 10.1016/S0006-3495(96)79561-9

D. Scala and C. , Biochemical Identification of a Linear Cholesterol-Binding Domain within Alzheimer???s ?? Amyloid Peptide, ACS Chemical Neuroscience, vol.4, issue.3, pp.509-517, 2013.
DOI : 10.1021/cn300203a

R. Thomsen and M. H. Christensen, MolDock:?? A New Technique for High-Accuracy Molecular Docking, Journal of Medicinal Chemistry, vol.49, issue.11, pp.3315-3321, 2006.
DOI : 10.1021/jm051197e

URL : http://www.daimi.au.dk/~cstorm/courses/AiBTaS_e07/papers/Molegro_paper_2006.pdf

N. Guex and M. C. Peitsch, 21907 | DOI: 10.1038/srep21907 50 SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Scientific RepoRts | Electrophoresis, vol.6, issue.18, pp.2714-2723, 1997.

M. Hibino and H. Tsuchiya, Self-Assembled Monolayers of Cholesterol and Cholesteryl Esters on Graphite, Langmuir, vol.30, issue.23, pp.6852-6857, 2014.
DOI : 10.1021/la500944t

K. Sabatini, J. P. Mattila, and P. K. Kinnunen, Interfacial Behavior of Cholesterol, Ergosterol, and Lanosterol in Mixtures with DPPC and DMPC, Biophysical Journal, vol.95, issue.5, pp.2340-2355, 2008.
DOI : 10.1529/biophysj.108.132076

J. Van-beek, matNMR: A flexible toolbox for processing, analyzing and visualizing magnetic resonance data in Matlab??, Journal of Magnetic Resonance, vol.187, issue.1, pp.19-26, 2007.
DOI : 10.1016/j.jmr.2007.03.017