D. Agnello, L. Carvelli, V. Muzio, P. Villa, B. Bottazzi et al., Increased peripheral benzodiazepine binding sites and pentraxin 3 expression in the spinal cord during EAE: relation to inflammatory cytokines and modulation by dexamethasone and rolipram, J. Neuroimmunol, vol.109, pp.105-111, 2000.

M. A. Van-agtmael, T. A. Eggelte, and C. J. Van-boxtel, Artemisinin drugs in the treatment of malaria: from medicinal herb to registered medication, Trends Pharmacol. Sci, vol.20, pp.199-205, 1999.

C. Amaratunga, S. Sreng, S. Suon, E. S. Phelps, K. Stepniewska et al., Artemisinin-resistant Plasmodium falciparum in Pursat province, western Cambodia: a parasite clearance rate study, Lancet Infect. Dis, vol.12, pp.851-858, 2012.

C. J. Austin, J. Kahlert, M. Kassiou, and L. M. Rendina, The translocator protein (TSPO): a novel target for cancer chemotherapy, Int. J. Biochem. Cell Biol, vol.45, pp.1212-1216, 2013.

R. B. Banati, R. J. Middleton, R. Chan, C. R. Hatty, W. W. Kam et al., Positron emission tomography and functional characterization of a complete PBR/TSPO knockout, Nat. Commun, vol.5, p.5452, 2014.

M. Bayrhuber, T. Meins, M. Habeck, S. Becker, K. Giller et al., Structure of the human voltage-dependent anion channel, Proc Natl Acad Sci, vol.105, pp.15370-15375, 2008.

J. Bénavidès, F. Guilloux, D. E. Allam, A. Uzan, J. Mizoule et al., Opposite effects of an agonist, R05-4864, and an antagonist, PK 11195, of the peripheral type benzodiazepine binding sites on audiogenic seizures in DBA/2J mice, Life Sci, vol.34, pp.2613-2620, 1984.

J. M. Bernassau, J. L. Reversat, P. Ferrara, D. Caput, and G. Lefur, A 3D model of the peripheral benzodiazepine receptor and its implication in intra mitochondrial cholesterol transport, J. Mol. Graph, vol.11, pp.236-244, 1993.

M. J. Besman, K. Yanagibashi, T. D. Lee, M. Kawamura, P. F. Hall et al., Identification of des-(Gly-Ile)-endozepine as an effector of corticotropin-dependent adrenal steroidogenesis: stimulation of cholesterol delivery is mediated by the peripheral benzodiazepine receptor, Proc Natl Acad Sci, vol.86, pp.4897-4901, 1989.

N. H. Bhoola, Z. Mbita, R. Hull, and Z. Dlamini, Translocator protein (TSPO) as a potential biomarker in human cancers, Int. J. Mol. Sci, vol.19, 2018.

F. Bono, I. Lamarche, V. Prabonnaud, G. Le-fur, and J. M. Herbert, Peripheral benzodiazepine receptor agonists exhibit potent antiapoptotic activities, Biochem. Biophys. Res. Commun, vol.265, pp.457-461, 1999.

F. Bonsack, C. H. Alleyne, and S. Sukumari-ramesh, Augmented expression of TSPO after intracerebral hemorrhage: a role in inflammation?, J. Neuroinflammation, vol.13, p.151, 2016.

T. Bordet, B. Buisson, M. Michaud, C. Drouot, P. Galéa et al., Identification and characterization of cholest-4-en-3-one, oxime (TRO19622), a novel drug candidate for amyotrophic lateral sclerosis, J. Pharmacol. Exp. Ther, vol.322, pp.709-720, 2007.

M. Bose, R. M. Whittal, W. L. Miller, and H. S. Bose, Steroidogenic activity of StAR requires contact with mitochondrial VDAC1 and phosphate carrier protein, J. Biol. Chem, vol.283, pp.8837-8845, 2008.

G. Bouyer, A. Cueff, S. Egée, J. Kmiecik, Y. Maksimova et al., Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum, Blood, vol.118, pp.2305-2312, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00623072

C. Braestrup and R. F. Squires, Specific benzodiazepine receptors in rat brain characterized by high-affinity (3H)diazepam binding, Proc Natl Acad Sci, vol.74, pp.3805-3809, 1977.

M. M. Budelier, W. W. Cheng, L. Bergdoll, Z. Chen, J. W. Janetka et al., Photoaffinity labeling with cholesterol analogues precisely maps a cholesterol-binding site in voltage-dependent anion channel-1, J. Biol. Chem, vol.292, pp.9294-9304, 2017.

L. Cantoni, M. Rizzardini, M. Skorupska, A. Cagnotto, A. Codegoni et al., Hepatic protoporphyria is associated with a decrease in ligand binding for the mitochondrial benzodiazepine receptors in the liver, Biochem. Pharmacol, vol.44, pp.1159-1164, 1992.

R. S. Chang and S. H. Snyder, Benzodiazepine receptors: labeling in intact animals with [3H] flunitrazepam, Eur. J. Pharmacol, vol.48, pp.213-218, 1978.

P. Chardenot, C. Roubert, S. Galiègue, P. Casellas, G. Le-fur et al., Expression profile and up-regulation of PRAX-1 mRNA by antidepressant treatment in the rat brain, Mol. Pharmacol, vol.62, pp.1314-1320, 2002.

O. V. Chechneva and W. Deng, Mitochondrial translocator protein (TSPO), astrocytes and neuroinflammation, Neural Regen. Res, vol.11, pp.1056-1057, 2016.

B. Chelli, A. Lena, R. Vanacore, E. Da-pozzo, B. Costa et al., Peripheral benzodiazepine receptor ligands: mitochondrial transmembrane potential depolarization and apoptosis induction in rat C6 glioma cells, Biochem. Pharmacol, vol.68, pp.125-134, 2004.

M. Chen and T. R. Guilarte, Translocator protein 18 kDa (TSPO): molecular sensor of brain injury and repair, Pharmacol. Ther, vol.118, pp.1-17, 2008.

A. Colasanti, D. R. Owen, D. Grozeva, E. A. Rabiner, P. M. Matthews et al., Bipolar Disorder is associated with the rs6971 polymorphism in the gene encoding 18 kDa Translocator Protein (TSPO), Psychoneuroendocrinology, vol.38, pp.2826-2829, 2013.

B. Costa, S. Pini, P. Gabelloni, E. Da-pozzo, M. Abelli et al., The spontaneous Ala147Thr amino acid substitution within the translocator protein influences pregnenolone production in lymphomonocytes of healthy individuals, Endocrinology, vol.150, pp.5438-5445, 2009.

M. Crompton, S. Virji, and J. M. Ward, Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore, Eur. J. Biochem, vol.258, pp.729-735, 1998.

M. Culty, H. Li, N. Boujrad, H. Amri, B. Vidic et al., In vitro studies on the role of the peripheral-type benzodiazepine receptor in steroidogenesis, J. Steroid Biochem. Mol. Biol, vol.69, pp.123-130, 1999.

S. Daniele, V. La-pietra, E. Barresi, S. Di-maro, E. Da-pozzo et al., Lead Optimization of 2-Phenylindolylglyoxylyldipeptide Murine Double Minute (MDM)2/Translocator Protein (TSPO) Dual Inhibitors for the Treatment of Gliomas, J. Med. Chem, vol.59, pp.4526-4538, 2016.

S. Das, B. Saha, A. K. Hati, R. , and S. , Evidence of Artemisinin-Resistant Plasmodium falciparum Malaria in Eastern India, N. Engl. J. Med, vol.379, pp.1962-1964, 2018.

D. J. Daugherty, V. Selvaraj, O. V. Chechneva, X. Liu, D. E. Pleasure et al., A TSPO ligand is protective in a mouse model of multiple sclerosis, EMBO Mol. Med, vol.5, pp.891-903, 2013.

M. E. Davey and F. J. De-bruijn, A homologue of the tryptophan-rich sensory protein TspO and FixL regulate a novel nutrient deprivation-induced Sinorhizobium meliloti locus, Appl. Environ. Microbiol, vol.66, pp.5353-5359, 2000.

W. L. Delano, Pymol: An open-source molecular graphics tool, CCP4 Newsletter On Protein Crystallography, vol.40, pp.82-92, 2002.

J. Duneau, A. P. Vegh, and J. N. Sturgis, A dimerization hierarchy in the transmembrane domains of the HER receptor family, Biochemistry, vol.46, pp.2010-2019, 2007.

M. Eilers, A. B. Patel, W. Liu, and S. O. Smith, Comparison of helix interactions in membrane and soluble alpha-bundle proteins, Biophys. J, vol.82, pp.2720-2736, 2002.

J. Fan, M. B. Rone, P. , and V. , Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis, J. Biol. Chem, vol.284, pp.30484-30497, 2009.

J. Fan, J. Liu, M. Culty, P. , and V. , Acyl-coenzyme A binding domain containing 3 (ACBD3; PAP7; GCP60): an emerging signaling molecule, Prog. Lipid Res, vol.49, pp.218-234, 2010.

J. Fan, P. Lindemann, M. G. Feuilloley, P. , and V. , Structural and functional evolution of the translocator protein (18 kDa), Curr. Mol. Med, vol.12, pp.369-386, 2012.

J. Fan, K. Wang, B. Zirkin, P. , and V. , CRISPR/Cas9-Mediated Tspo Gene Mutations Lead to Reduced Mitochondrial Membrane Potential and Steroid Formation, 2018.

, Mouse Tumor Leydig Cells. Endocrinology, vol.159, pp.1130-1146

J. Fantini, C. Di-scala, L. S. Evans, P. T. Williamson, and F. J. Barrantes, A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes, Sci. Rep, vol.6, p.21907, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01772916

R. Farges, E. Joseph-liauzun, D. Shire, D. Caput, G. Le-fur et al., Site-directed mutagenesis of the peripheral benzodiazepine receptor: identification of amino acids implicated in the binding site of Ro5-4864, Mol. Pharmacol, vol.46, pp.1160-1167, 1994.

W. Frank, K. Baar, E. Qudeimat, M. Woriedh, A. Alawady et al., A mitochondrial protein homologous to the mammalian peripheral-type benzodiazepine receptor is essential for stress adaptation in plants, Plant J, vol.51, pp.1004-1018, 2007.

S. Galiègue, O. Jbilo, T. Combes, E. Bribes, P. Carayon et al., , 1999.

, Cloning and characterization of PRAX-1. A new protein that specifically interacts with the peripheral benzodiazepine receptor, J. Biol. Chem, vol.274, pp.2938-2952

M. Garnier, A. B. Dimchev, N. Boujrad, J. M. Price, N. A. Musto et al., In vitro reconstitution of a functional peripheral-type benzodiazepine receptor from mouse Leydig tumor cells, Mol. Pharmacol, vol.45, pp.201-211, 1994.

J. Gatliff and M. Campanella, TSPO: kaleidoscopic 18-kDa amid biochemical pharmacology, control and targeting of mitochondria, Biochem. J, vol.473, pp.107-121, 2016.

J. Gatliff, D. East, J. Crosby, R. Abeti, R. Harvey et al., TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control, Autophagy, vol.10, pp.2279-2296, 2014.

A. Gerhard, N. Pavese, G. Hotton, F. Turkheimer, M. Es et al., In vivo imaging of microglial activation with [11C](R)-PK11195 PET in idiopathic Parkinson's disease, Neurobiol. Dis, vol.21, pp.404-412, 2006.

H. Ginsburg and W. D. Stein, How many functional transport pathways does Plasmodium falciparum induce in the membrane of its host erythrocyte?, Trends Parasitol, vol.21, pp.118-121, 2005.

H. Ginsburg, M. Krugliak, O. Eidelman, and Z. I. Cabantchik, New permeability pathways induced in membranes of Plasmodium falciparum infected erythrocytes, Mol. Biochem. Parasitol, vol.8, pp.177-190, 1983.

H. Ginsburg, S. Kutner, M. Krugliak, and Z. I. Cabantchik, Characterization of permeation pathways appearing in the host membrane of Plasmodium falciparum infected red blood cells, Mol. Biochem. Parasitol, vol.14, pp.313-322, 1985.

C. Ginter, I. Kiburu, and O. Boudker, Chemical catalysis by the translocator protein (18 kDa), Biochemistry, vol.52, pp.3609-3611, 2013.

D. Guillaumot, S. Guillon, T. Déplanque, C. Vanhee, C. Gumy et al., The Arabidopsis TSPO-related protein is a stress and abscisic acid-regulated, endoplasmic reticulum-Golgi-localized membrane protein, Plant J, vol.60, pp.242-256, 2009.

Y. Guo, R. C. Kalathur, Q. Liu, B. Kloss, R. Bruni et al., Protein structure. Structure and activity of tryptophan-rich TSPO proteins, vol.347, pp.551-555, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02116001

P. Gut, Targeting mitochondrial energy metabolism with TSPO ligands, Biochem. Soc. Trans, vol.43, pp.537-542, 2015.

A. P. Halestrap, G. P. Mcstay, C. , and S. J. , The permeability transition pore complex: another view, Biochimie, vol.84, pp.153-166, 2002.

M. J. Hansson, O. Llwyd, D. Morin, D. De-paulis, T. Arnoux et al., Differences in the profile of protection afforded by TRO40303 and mild hypothermia in models of cardiac ischemia/reperfusion injury, Eur. J. Pharmacol, vol.760, pp.7-19, 2015.

T. Hauet, J. Liu, H. Li, M. Gazouli, M. Culty et al., PBR, StAR, and PKA: partners in cholesterol transport in steroidogenic cells, Endocr. Res, vol.28, pp.395-401, 2002.

O. W. Health, World malaria report, 2017.

S. Hiller, R. G. Garces, T. J. Malia, V. Y. Orekhov, M. Colombini et al., Solution structure of the integral human membrane protein VDAC-1 in detergent micelles, Science, vol.321, pp.1206-1210, 2008.

K. Hinsen, A. Vaitinadapoule, M. A. Ostuni, C. Etchebest, and J. Lacapere, Construction and validation of an atomic model for bacterial TSPO from electron microscopy density, evolutionary constraints, and biochemical and biophysical data, Biochim. Biophys. Acta, vol.1848, pp.568-580, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01171268

J. D. Hirsch, C. F. Beyer, L. Malkowitz, B. Beer, and A. J. Blume, Mitochondrial benzodiazepine receptors mediate inhibition of mitochondrial respiratory control, Mol. Pharmacol, vol.35, pp.157-163, 1989.

W. Humphrey, A. Dalke, and K. Schulten, VMD: visual molecular dynamics, J. Mol. Graph, vol.14, pp.33-38, 1996.

O. Inoue, T. Yamasaki, K. Hashimoto, and M. Kojima, , 1985.

, Kaku Igaku, vol.22, pp.1385-1389

N. Jamin, J. Neumann, M. A. Ostuni, T. K. Vu, Z. Yao et al., Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor, Mol. Endocrinol, vol.19, pp.588-594, 2005.

L. Jaremko, M. Jaremko, S. Becker, and M. Zweckstetter, Toward the functional oligomerization state of tryptophan-rich sensory proteins, Protein Sci, vol.23, pp.1154-1160, 2014.

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.343, pp.1363-1366, 2014.

M. Jaremko, ?. Jaremko, G. Jaipuria, S. Becker, and M. Zweckstetter, Structure of the mammalian TSPO/PBR protein, Biochem. Soc. Trans, vol.43, pp.566-571, 2015.

?. Jaremko, M. Jaremko, K. Giller, S. Becker, and M. Zweckstetter, Conformational flexibility in the transmembrane protein TSPO, Chem. Eur. J, vol.21, pp.16555-16563, 2015.

E. Joseph-liazun, E. Farges, P. Delmas, P. Ferrara, and G. Loison, The Mr 18,000 subunit of the peripheral-type benzodiazepine receptor exhibits both benzodiazepine and isoquinoline carboxamide binding sites in the absence of the voltage-dependent anion channel or the adenine nucleotide carrier, J. Biol. Chem, vol.272, pp.28102-28106, 1997.

G. Kleiger, R. Grothe, P. Mallick, and D. Eisenberg, GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles, Biochemistry, vol.41, pp.5990-5997, 2002.

E. Y. Klein, Antimalarial drug resistance: a review of the biology and strategies to delay emergence and spread, Int. J. Antimicrob. Agents, vol.41, pp.311-317, 2013.

M. Klima, D. J. Tóth, R. Hexnerova, A. Baumlova, D. Chalupska et al., Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein, Sci. Rep, vol.6, p.23641, 2016.

M. Klima, D. Chalupska, B. Ró?ycki, J. Humpolickova, L. Rezabkova et al., Kobuviral Non-structural 3A Proteins Act as Molecular Harnesses to Hijack the Host ACBD3 Protein, Structure, vol.25, pp.219-230, 2017.

J. Knudsen, Acyl-CoA-binding and transport, an alternative function for diazepam binding inhibitor (DBI), which is identical with acyl-CoA-binding protein, Neuropharmacology, vol.30, pp.1405-1410, 1991.

J. E. Kokoszka, K. G. Waymire, S. E. Levy, J. E. Sligh, J. Cai et al., The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore, Nature, vol.427, pp.461-465, 2004.

V. M. Korkhov, C. Sachse, J. M. Short, and C. G. Tate, Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals, Structure, vol.18, pp.677-687, 2010.

E. Krammer, F. Homblé, and M. Prévost, Concentration dependent ion selectivity in VDAC: a molecular dynamics simulation study, PLoS ONE, vol.6, 2011.

E. Krammer, F. Homblé, and M. Prévost, Molecular origin of VDAC selectivity towards inorganic ions: a combined molecular and Brownian dynamics study, Biochim. Biophys. Acta, vol.1828, pp.1284-1292, 2013.

E. Krammer, G. T. Vu, F. Homblé, and M. Prévost, Dual mechanism of ion permeation through VDAC revealed with inorganic phosphate ions and phosphate metabolites, PLoS ONE, vol.10, 2015.

W. C. Kreisl, C. H. Lyoo, M. Mcgwier, J. Snow, K. J. Jenko et al., In vivo radioligand binding to translocator protein correlates with severity of Alzheimer's disease, Brain, vol.136, pp.2228-2238, 2013.

K. E. Krueger, P. , and V. , Peripheral-type benzodiazepine receptors mediate translocation of cholesterol from outer to inner mitochondrial membranes in adrenocortical cells, J. Biol. Chem, vol.265, pp.15015-15022, 1990.

W. Kugler, L. Veenman, Y. Shandalov, S. Leschiner, I. Spanier et al., Ligands of the mitochondrial 18 kDa translocator protein attenuate apoptosis of human glioblastoma cells exposed to erucylphosphohomocholine, Cell. Oncol, vol.30, pp.435-450, 2008.

O. R. Kunduzova, G. Escourrou, F. De-la-farge, R. Salvayre, M. Séguélas et al., Involvement of peripheral benzodiazepine receptor in the oxidative stress, death-signaling pathways, and renal injury induced by ischemia-reperfusion, J. Am. Soc. Nephrol, vol.15, pp.2152-2160, 2004.

J. J. Lacapère, F. Delavoie, H. Li, G. Péranzi, J. Maccario et al., Structural and functional study of reconstituted peripheral benzodiazepine receptor, Biochem. Biophys. Res. Commun, vol.284, pp.536-541, 2001.

S. Lavisse, M. Guillermier, A. Hérard, F. Petit, M. Delahaye et al., Reactive astrocytes overexpress TSPO and are detected by TSPO positron emission tomography imaging, J. Neurosci, vol.32, pp.10809-10818, 2012.
URL : https://hal.archives-ouvertes.fr/hal-02110993

Y. Lee, F. G. Siméon, E. Briard, and V. W. Pike, Solution structures of the prototypical 18 kDa translocator protein ligand, PK 11195, elucidated with 1H/13C NMR spectroscopy and quantum chemistry, ACS Chem. Neurosci, vol.3, pp.325-335, 2012.

M. A. Lemmon, J. M. Flanagan, J. F. Hunt, B. D. Adair, B. J. Bormann et al., Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices, J. Biol. Chem, vol.267, pp.7683-7689, 1992.

M. A. Lemmon, J. M. Flanagan, H. R. Treutlein, J. Zhang, and D. M. Engelman, Sequence specificity in the dimerization of transmembrane alpha-helices, Biochemistry, vol.31, pp.12719-12725, 1992.

E. Leonelli, J. G. Yague, M. Ballabio, I. Azcoitia, V. Magnaghi et al., Ro5-4864, a synthetic ligand of peripheral benzodiazepine receptor, reduces aging-associated myelin degeneration in the sciatic nerve of male rats, Mech. Ageing Dev, vol.126, pp.1159-1163, 2005.

E. Levin, A. Premkumar, L. Veenman, W. Kugler, S. Leschiner et al., The peripheral-type benzodiazepine receptor and tumorigenicity: isoquinoline binding protein (IBP) antisense knockdown in the C6 glioma cell line, Biochemistry, vol.44, pp.9924-9935, 2005.

H. Li, P. , and V. , Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern, Endocrinology, vol.139, pp.4991-4997, 1998.

E. Li, W. C. Wimley, and K. Hristova, Transmembrane helix dimerization: beyond the search for sequence motifs, Biochim. Biophys. Acta, vol.1818, pp.183-193, 2012.

F. Li, Y. Xia, J. Meiler, and S. Ferguson-miller, Characterization and modeling of the oligomeric state and ligand binding behavior of purified translocator protein 18 kDa from Rhodobacter sphaeroides, Biochemistry, vol.52, pp.5884-5899, 2013.

F. Li, J. Liu, L. Valls, C. Hiser, and S. Ferguson-miller, Identification of a key cholesterol binding enhancement motif in translocator protein 18 kDa, Biochemistry, vol.54, pp.1441-1443, 2015.

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.347, pp.555-558, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02143564

F. Li, J. Liu, R. M. Garavito, and S. Ferguson-miller, Evolving understanding of translocator protein 18 kDa (TSPO), Pharmacol. Res, vol.99, pp.404-409, 2015.

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Response to Comment on "Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.350, p.519, 2015.

F. Li, J. Liu, N. Liu, L. A. Kuhn, R. M. Garavito et al., Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?, Biochemistry, vol.55, pp.2821-2831, 2016.

H. Li, Z. Yao, B. Degenhardt, G. Teper, P. et al., Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide, Proc Natl Acad Sci, vol.98, pp.1267-1272, 2001.

H. Li, B. Degenhardt, D. Tobin, Z. X. Yao, K. Tasken et al., , 2001.

, Identification, localization, and function in steroidogenesis of PAP7: a peripheral-type benzodiazepine receptor-and PKA (RIalpha)-associated protein, Mol. Endocrinol, vol.15, pp.2211-2228

J. Li, Z. Zhang, L. Lv, H. Qiao, X. Chen et al., A bispecific antibody (ScBsAbAgn-2/TSPO) target for Ang-2 and TSPO resulted in therapeutic effects against glioblastomas, Biochem. Biophys. Res. Commun, vol.472, pp.384-391, 2016.

D. Lin, T. Sugawara, J. F. Strauss, B. J. Clark, D. M. Stocco et al., Role of steroidogenic acute regulatory protein in adrenal and gonadal steroidogenesis, Science, vol.267, pp.1828-1831, 1995.

P. Lindemann, A. Koch, B. Degenhardt, G. Hause, B. Grimm et al., A novel Arabidopsis thaliana protein is a functional peripheral-type benzodiazepine receptor, Plant Cell Physiol, vol.45, pp.723-733, 2004.

B. Liu, K. X. Le, M. Park, S. Wang, A. P. Belanger et al., In Vivo Detection of Age-and Disease-Related Increases in Neuroinflammation by 18F-GE180 TSPO MicroPET Imaging in Wild-Type and Alzheimer's Transgenic Mice, J. Neurosci, vol.35, pp.15716-15730, 2015.

G. Liu, R. J. Middleton, C. R. Hatty, W. W. Kam, .. Chan et al., The 18 kDa translocator protein, microglia and neuroinflammation, Brain Pathol, vol.24, pp.631-653, 2014.

G. Liu, R. J. Middleton, W. W. Kam, .. Chin, D. Y. Hatty et al., Functional gains in energy and cell metabolism after TSPO gene insertion, Cell Cycle, vol.16, pp.436-447, 2017.

J. Liu, M. B. Rone, P. , and V. , Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis, J. Biol. Chem, vol.281, pp.38879-38893, 2006.

A. Lockhart, B. Davis, J. C. Matthews, H. Rahmoune, G. Hong et al., The peripheral benzodiazepine receptor ligand PK11195 binds with high affinity to the acute phase reactant alpha1-acid glycoprotein: implications for the use of the ligand as a CNS inflammatory marker, Nucl. Med. Biol, vol.30, pp.199-206, 2003.

M. A. Lomize, I. D. Pogozheva, H. Joo, H. I. Mosberg, and A. L. Lomize, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res, vol.40, pp.370-376, 2012.

K. Maaser, M. Höpfner, A. Jansen, G. Weisinger, M. Gavish et al., Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human colorectal cancer cells, Br. J. Cancer, vol.85, pp.1771-1780, 2001.

P. J. Marangos, J. Patel, J. P. Boulenger, and R. Clark-rosenberg, Characterization of peripheral-type benzodiazepine binding sites in brain using [3H]Ro 5-4864, Mol. Pharmacol, vol.22, pp.26-32, 1982.

I. Marginedas-freixa, C. Hattab, G. Bouyer, F. Halle, A. Chene et al., TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to the inhibition of P. falciparum growth in human blood, Sci. Rep, vol.6, p.33516, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01369499

A. T. Mazzeo, A. Beat, A. Singh, and M. R. Bullock, The role of mitochondrial transition pore, and its modulation, in traumatic brain injury and delayed neurodegeneration after TBI, Exp. Neurol, vol.218, pp.363-370, 2009.

M. W. Mcenery, A. M. Snowman, R. R. Trifiletti, and S. H. Snyder, Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier, Proc Natl Acad Sci, vol.89, pp.3170-3174, 1992.

J. A. Mcphail, E. H. Ottosen, M. L. Jenkins, and J. E. Burke, The Molecular Basis of Aichi Virus 3A Protein Activation of Phosphatidylinositol 4 Kinase III?, PI4KB, through ACBD3, Structure, vol.25, pp.121-131, 2017.

M. C. Mendonça-torres and S. S. Roberts, The translocator protein (TSPO) ligand PK11195 induces apoptosis and cell cycle arrest and sensitizes to chemotherapy treatment in pre-and post-relapse neuroblastoma cell lines, Cancer Biol. Ther, vol.14, pp.319-326, 2013.

C. Mills, M. Makwana, A. Wallace, S. Benn, H. Schmidt et al., Ro5-4864 promotes neonatal motor neuron survival and nerve regeneration in adult rats, Eur. J. Neurosci, vol.27, pp.937-946, 2008.

D. Morin, J. Musman, S. Pons, A. Berdeaux, and B. Ghaleh, Mitochondrial translocator protein (TSPO): From physiology to cardioprotection, Biochem. Pharmacol, vol.105, pp.1-13, 2016.

K. Morohaku, S. H. Pelton, D. J. Daugherty, W. R. Butler, W. Deng et al., , 2014.

, Translocator protein/peripheral benzodiazepine receptor is not required for steroid hormone biosynthesis, Endocrinology, vol.155, pp.89-97

B. K. Mueller, S. Subramaniam, and A. Senes, A frequent, GxxxG-mediated, transmembrane association motif is optimized for the formation of interhelical C?-H hydrogen bonds, Proc Natl Acad Sci, vol.111, pp.888-95, 2014.

A. G. Mukhin, V. Papadopoulos, E. Costa, and K. E. Krueger, Mitochondrial benzodiazepine receptors regulate steroid biosynthesis, Proc Natl Acad Sci, vol.86, pp.9813-9816, 1989.

S. Murail, J. Robert, Y. Coïc, J. Neumann, M. A. Ostuni et al., Secondary and tertiary structures of the transmembrane domains of the translocator protein TSPO determined by NMR. Stabilization of the TSPO tertiary fold upon ligand binding, Biochim. Biophys. Acta, vol.1778, pp.1375-1381, 2008.

K. Nakamura, K. Yamada, Y. Iwayama, T. Toyota, A. Furukawa et al., Evidence that variation in the peripheral benzodiazepine receptor (PBR) gene influences susceptibility to panic disorder, Am. J. Med. Genet. B Neuropsychiatr. Genet, vol.141, pp.222-226, 2006.

F. Nakazawa, C. Alev, M. Shin, Y. Nakaya, L. M. Jakt et al., PBRL, a putative peripheral benzodiazepine receptor, in primitive erythropoiesis, Gene Expr. Patterns, vol.9, pp.114-121, 2009.

C. Nothdurfter, T. C. Baghai, C. Schüle, and R. Rupprecht, Translocator protein (18 kDa) (TSPO) as a therapeutic target for anxiety and neurologic disorders, Eur. Arch. Psychiatry Clin. Neurosci, vol.262, issue.2, pp.107-119, 2012.

F. N. Obame, R. Zini, R. Souktani, A. Berdeaux, and D. Morin, Peripheral benzodiazepine receptor-induced myocardial protection is mediated by inhibition of mitochondrial membrane permeabilization, J. Pharmacol. Exp. Ther, vol.323, pp.336-345, 2007.

J. M. Olson, L. Junck, A. B. Young, J. B. Penney, and W. R. Mancini, Isoquinoline and peripheral-type benzodiazepine binding in gliomas: implications for diagnostic imaging, Cancer Res, vol.48, pp.5837-5841, 1988.

J. M. Olson, W. Mcneel, A. B. Young, and W. R. Mancini, Localization of the peripheral-type benzodiazepine binding site to mitochondria of human glioma cells, J Neurooncol, vol.13, pp.35-42, 1992.

V. Papadopoulos and L. Lecanu, Translocator protein (18 kDa) TSPO: an emerging therapeutic target in neurotrauma, Exp. Neurol, vol.219, pp.53-57, 2009.

V. Papadopoulos, A. G. Mukhin, E. Costa, and K. E. Krueger, The peripheral-type benzodiazepine receptor is functionally linked to Leydig cell steroidogenesis, J. Biol. Chem, vol.265, pp.3772-3779, 1990.

V. Papadopoulos, F. B. Nowzari, and K. E. Krueger, Hormone-stimulated steroidogenesis is coupled to mitochondrial benzodiazepine receptors. Tropic hormone action on steroid biosynthesis is inhibited by flunitrazepam, J. Biol. Chem, vol.266, pp.3682-3687, 1991.

V. Papadopoulos, N. Boujrad, M. D. Ikonomovic, P. Ferrara, and B. Vidic, Topography of the Leydig cell mitochondrial peripheral-type benzodiazepine receptor, Mol. Cell. Endocrinol, vol.104, pp.5-9, 1994.

V. Papadopoulos, H. Amri, N. Boujrad, C. Cascio, M. Culty et al., Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis, Steroids, vol.62, pp.21-28, 1997.

V. Papadopoulos, H. Amri, H. Li, N. Boujrad, B. Vidic et al., Targeted disruption of the peripheral-type benzodiazepine receptor gene inhibits steroidogenesis in the R2C Leydig tumor cell line, J. Biol. Chem, vol.272, pp.32129-32135, 1997.

V. Papadopoulos, M. Baraldi, T. R. Guilarte, T. B. Knudsen, J. Lacapère et al., Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function, Trends Pharmacol. Sci, vol.27, pp.402-409, 2006.

V. Papadopoulos, J. Liu, and M. Culty, Is there a mitochondrial signaling complex facilitating cholesterol import?, Mol. Cell. Endocrinol, pp.59-64, 2007.

V. Papadopoulos, J. Fan, and B. Zirkin, Translocator protein (18 kDa): an update on its function in steroidogenesis, J. Neuroendocrinol, vol.30, 2017.

S. Paradis, V. Leoni, C. Caccia, A. Berdeaux, and D. Morin, Cardioprotection by the TSPO ligand 4'-chlorodiazepam is associated with inhibition of mitochondrial accumulation of cholesterol at reperfusion, Cardiovasc. Res, vol.98, pp.420-427, 2013.
URL : https://hal.archives-ouvertes.fr/inserm-00841658

J. G. Pastorino, G. Simbula, E. Gilfor, J. B. Hoek, and J. L. Farber, Protoporphyrin IX, an endogenous ligand of the peripheral benzodiazepine receptor, potentiates induction of the mitochondrial permeability transition and the killing of cultured hepatocytes by rotenone, J. Biol. Chem, vol.269, pp.31041-31046, 1994.

E. Pebay-peyroula, C. Dahout-gonzalez, R. Kahn, V. Trézéguet, G. J. Lauquin et al., Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside, Nature, vol.426, pp.39-44, 2003.

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera-a visualization system for exploratory research and analysis, J. Comput. Chem, vol.25, pp.1605-1612, 2004.

D. Pogoryelov, A. L. Klyszejko, G. O. Krasnoselska, E. Heller, V. Leone et al., Engineering rotor ring stoichiometries in the ATP synthase, Proc Natl Acad Sci, vol.109, pp.1599-608, 2012.

D. Raeburn, L. G. Miller, and W. R. Summer, Peripheral type benzodiazepine receptor and airway smooth muscle relaxation, J. Pharmacol. Exp. Ther, vol.245, pp.557-562, 1988.

R. Rao, V. L. Dogan, A. Bowen, K. K. Dempsey, and R. J. , Traumatic brain injury leads to increased expression of peripheral-type benzodiazepine receptors, neuronal death, and activation of astrocytes and microglia in rat thalamus, Exp. Neurol, vol.161, pp.102-114, 2000.

C. Rampon, M. Bouzaffour, M. A. Ostuni, P. Dufourcq, C. Girard et al., Translocator protein (18 kDa) is involved in primitive erythropoiesis in zebrafish, FASEB J, vol.23, pp.4181-4192, 2009.

M. Rechichi, A. Salvetti, B. Chelli, B. Costa, E. Da-pozzo et al., TSPO over-expression increases motility, transmigration and proliferation properties of C6 rat glioma cells, Biochim. Biophys. Acta, vol.1782, pp.118-125, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00501558

J. Repalli, Translocator protein (TSPO) role in aging and Alzheimer's disease, Curr. Aging Sci, vol.7, pp.168-175, 2014.

C. Rey, C. Mauduit, O. Naureils, M. Benahmed, P. Louisot et al., Up-regulation of mitochondrial peripheral benzodiazepine receptor expression by tumor necrosis factor alpha in testicular leydig cells. Possible involvement in cell survival, Biochem. Pharmacol, vol.60, pp.1639-1646, 2000.

E. M. Richards, P. Zanotti-fregonara, M. Fujita, L. Newman, C. Farmer et al., PET radioligand binding to translocator protein (TSPO) is increased in unmedicated depressed subjects, EJNMMI Res, vol.8, p.57, 2018.

S. Rojas, A. Martín, M. J. Arranz, D. Pareto, J. Purroy et al., Imaging brain inflammation with [(11)C]PK11195 by PET and induction of the peripheral-type benzodiazepine receptor after transient focal ischemia in rats, J. Cereb. Blood Flow Metab, vol.27, pp.1975-1986, 2007.

M. B. Rone, A. S. Midzak, L. Issop, G. Rammouz, S. Jagannathan et al., Identification of a dynamic mitochondrial protein complex driving cholesterol import, trafficking, and metabolism to steroid hormones, Mol. Endocrinol, vol.26, pp.1868-1882, 2012.

R. Rupprecht, V. Papadopoulos, G. Rammes, T. C. Baghai, J. Fan et al., Translocator protein (18 kDa) (TSPO) as a therapeutic target for neurological and psychiatric disorders, Nat. Rev. Drug Discov, vol.9, pp.971-988, 2010.

A. F. Santidrián, A. M. Cosialls, L. Coll-mulet, D. Iglesias-serret, M. De-frias et al., The potential anticancer agent PK11195 induces apoptosis irrespective of p53 and ATM status in chronic lymphocytic leukemia cells, Haematologica, vol.92, pp.1631-1638, 2007.

S. Schaller, S. Paradis, G. A. Ngoh, R. Assaly, B. Buisson et al., TRO40303, a new cardioprotective compound, inhibits mitochondrial permeability transition, J. Pharmacol. Exp. Ther, vol.333, pp.696-706, 2010.
URL : https://hal.archives-ouvertes.fr/inserm-00497589

V. Selvaraj and D. M. Stocco, The changing landscape in translocator protein (TSPO) function, Trends Endocrinol. Metab, vol.26, pp.341-348, 2015.

J. ?ileikyt?, E. Blachly-dyson, R. Sewell, A. Carpi, R. Menabò et al., Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (Translocator Protein of 18 kDa (TSPO)), J. Biol. Chem, vol.289, pp.13769-13781, 2014.

S. H. Snyder, A. Verma, and R. R. Trifiletti, The peripheral-type benzodiazepine receptor: a protein of mitochondrial outer membranes utilizing porphyrins as endogenous ligands, FASEB J, vol.1, pp.282-288, 1987.

Z. Su, F. Roncaroli, P. F. Durrenberger, D. J. Coope, K. Karabatsou et al., The 18-kDa mitochondrial translocator protein in human gliomas: an 11C-(R)PK11195 PET imaging and neuropathology study, J. Nucl. Med, vol.56, pp.512-517, 2015.

E. S. Sulistijo and K. R. Mackenzie, Structural basis for dimerization of the BNIP3 transmembrane domain, Biochemistry, vol.48, pp.5106-5120, 2009.

A. P. Sutter, K. Maaser, M. Höpfner, B. Barthel, P. Grabowski et al., Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human esophageal cancer cells, Int. J. Cancer, vol.102, pp.318-327, 2002.

A. P. Sutter, K. Maaser, B. Barthel, and H. Scherübl, Ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in oesophageal cancer cells: involvement of the p38MAPK signalling pathway, Br. J. Cancer, vol.89, pp.564-572, 2003.

A. P. Sutter, K. Maaser, P. Grabowski, G. Bradacs, K. Vormbrock et al., Peripheral benzodiazepine receptor ligands induce apoptosis and cell cycle arrest in human hepatocellular carcinoma cells and enhance chemosensitivity to paclitaxel, docetaxel, doxorubicin and the Bcl-2 inhibitor HA14-1, J. Hepatol, vol.41, pp.799-807, 2004.

I. Szabó, V. De-pinto, and M. Zoratti, The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel, FEBS Lett, vol.330, pp.206-210, 1993.

S. Taketani, H. Kohno, T. Furukawa, and R. Tokunaga, Involvement of peripheral-type benzodiazepine receptors in the intracellular transport of heme and porphyrins, J. Biochem, vol.117, pp.875-880, 1995.

Y. Tanimoto, Y. Onishi, Y. Sato, and H. Kizaki, Benzodiazepine receptor agonists modulate thymocyte apoptosis through reduction of the mitochondrial transmembrane potential, Jpn J Pharmacol, vol.79, pp.177-183, 1999.

M. G. Teese and D. Langosch, Role of gxxxg motifs in transmembrane domain interactions, Biochemistry, vol.54, pp.5125-5135, 2015.

S. R. Torres, T. S. Fröde, G. M. Nardi, N. Vita, R. Reeb et al., Anti-inflammatory effects of peripheral benzodiazepine receptor ligands in two mouse models of inflammation, Eur. J. Pharmacol, vol.408, pp.199-211, 2000.

Y. Tsujishita and J. H. Hurley, Structure and lipid transport mechanism of a StAR-related domain, Nat. Struct. Biol, vol.7, pp.408-414, 2000.

L. N. Tu, K. Morohaku, P. R. Manna, S. H. Pelton, W. R. Butler et al., Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis, J. Biol. Chem, vol.289, pp.27444-27454, 2014.

L. N. Tu, A. H. Zhao, D. M. Stocco, and V. Selvaraj, PK11195 effect on steroidogenesis is not mediated through the translocator protein (TSPO), Endocrinology, vol.156, pp.1033-1039, 2015.

R. Ujwal, D. Cascio, J. Colletier, S. Faham, J. Zhang et al., The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating, Proc Natl Acad Sci, vol.105, pp.17742-17747, 2008.

S. Unterreitmeier, A. Fuchs, T. Schäffler, R. G. Heym, D. Frishman et al., , 2007.

, Phenylalanine promotes interaction of transmembrane domains via GxxxG motifs, J. Mol. Biol, vol.374, pp.705-718

A. D. Vaitinadapoulé, K. G. Milne, J. Y. Zou, G. J. Kleywegt, T. Bergfors et al., TSPO and VDAC, two Membrane Proteins of Red Blood Cell involved in Malaria. A bioinformatics and Molecular Modelling Study, Doctorate thesis van Aalten, vol.309, pp.181-182, 2001.

C. Vanhee, G. Zapotoczny, D. Masquelier, M. Ghislain, and H. Batoko, The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism, Plant Cell, vol.23, pp.785-805, 2011.

L. Veenman and M. Gavish, The role of 18 kDa mitochondrial translocator protein (TSPO) in programmed cell death, and effects of steroids on TSPO expression, Curr. Mol. Med, vol.12, pp.398-412, 2012.

L. Veenman, V. Papadopoulos, and M. Gavish, Channel-like functions of the 18-kDa translocator protein (TSPO): regulation of apoptosis and steroidogenesis as part of the host-defense response, Curr. Pharm. Des, vol.13, pp.2385-2405, 2007.

L. Veenman, Y. Shandalov, and M. Gavish, VDAC activation by the 18 kDa translocator protein (TSPO), implications for apoptosis, J. Bioenerg. Biomembr, vol.40, pp.199-205, 2008.

L. Veenman, A. Vainshtein, N. Yasin, M. Azrad, and M. Gavish, Tetrapyrroles as Endogenous TSPO Ligands in Eukaryotes and Prokaryotes: Comparisons with Synthetic Ligands, Int. J. Mol. Sci, vol.17, 2016.

A. Verma and S. H. Snyder, Peripheral type benzodiazepine receptors, Annu. Rev. Pharmacol. Toxicol, vol.29, pp.307-322, 1989.

A. Verma, J. S. Nye, and S. H. Snyder, Porphyrins are endogenous ligands for the mitochondrial (peripheral-type) benzodiazepine receptor, Proc Natl Acad Sci, vol.84, pp.2256-2260, 1987.

E. Vowinckel, D. Reutens, B. Becher, G. Verge, A. Evans et al., and experimental autoimmune encephalomyelitis, J. Neurosci. Res, vol.50, pp.345-353, 1997.

R. B. Walter, J. L. Pirga, M. R. Cronk, S. Mayer, F. R. Appelbaum et al., , 2005.

, PK11195, a peripheral benzodiazepine receptor (pBR) ligand, broadly blocks drug efflux to chemosensitize leukemia and myeloma cells by a pBR-independent, direct transporter-modulating mechanism, Blood, vol.106, pp.3584-3593

J. Wang, Comment on "Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.350, p.519, 2015.

M. Weber and D. Schneider, Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding, FEBS Lett, vol.587, pp.1592-1596, 2013.

G. Wendler, P. Lindemann, J. Lacapère, P. , and V. , Protoporphyrin IX binding and transport by recombinant mouse PBR, Biochem. Biophys. Res. Commun, vol.311, pp.847-852, 2003.

E. L. Werry, M. L. Barron, and M. Kassiou, TSPO as a target for glioblastoma therapeutics, Biochem. Soc. Trans, vol.43, pp.531-536, 2015.

X. Wu and K. A. Gallo, The 18-kDa translocator protein (TSPO) disrupts mammary epithelial morphogenesis and promotes breast cancer cell migration, PLoS ONE, vol.8, 2013.

A. A. Yeliseev and S. Kaplan, A sensory transducer homologous to the mammalian peripheral-type benzodiazepine receptor regulates photosynthetic membrane complex formation in Rhodobacter sphaeroides 2.4.1, J. Biol. Chem, vol.270, pp.21167-21175, 1995.

A. A. Yeliseev and S. Kaplan, A novel mechanism for the regulation of photosynthesis gene expression by the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1, J. Biol. Chem, vol.274, pp.21234-21243, 1999.

A. A. Yeliseev and S. Kaplan, TspO of rhodobacter sphaeroides. A structural and functional model for the mammalian peripheral benzodiazepine receptor, J. Biol. Chem, vol.275, pp.5657-5667, 2000.

A. A. Yeliseev, K. E. Krueger, and S. Kaplan, A mammalian mitochondrial drug receptor functions as a bacterial "oxygen" sensor, Proc Natl Acad Sci, vol.94, pp.5101-5106, 1997.

A. H. Zhao, L. N. Tu, C. Mukai, M. P. Sirivelu, V. V. Pillai et al., Mitochondrial translocator protein (TSPO) function is not essential for heme biosynthesis, J. Biol. Chem, vol.291, pp.1591-1603, 2016.

Y. Zhao, J. Yu, Q. Li, C. Ma, C. Lu et al., TSPO-specific ligand vinpocetine exerts a neuroprotective effect by suppressing microglial inflammation, Neuron Glia Biol, vol.7, pp.187-197, 2011.

J. Zheng, R. Boisgard, K. Siquier-pernet, D. Decaudin, F. Dollé et al., Differential expression of the 18 kDa translocator protein (TSPO) by neoplastic and inflammatory cells in mouse tumors of breast cancer, Mol. Pharm, vol.8, pp.823-832, 2011.

N. R. Zürcher, M. L. Loggia, R. Lawson, D. B. Chonde, D. Izquierdo-garcia et al., Increased in vivo glial activation in patients with amyotrophic lateral sclerosis: assessed with, Neuroimage Clin, vol.7, issue.11, pp.409-414, 2015.

A. E. Aliev, M. Kulke, H. S. Khaneja, V. Chudasama, T. D. Sheppard et al., Motional timescale predictions by molecular dynamics simulations: case study using proline and hydroxyproline sidechain dynamics, Proteins, vol.82, pp.195-215, 2014.

A. Amadei, A. B. Linssen, and H. J. Berendsen, Essential dynamics of proteins, Proteins, vol.17, pp.412-425, 1993.

H. Ashkenazy, O. Penn, A. Doron-faigenboim, O. Cohen, G. Cannarozzi et al., FastML: a web server for probabilistic reconstruction of ancestral sequences, Nucleic Acids Res, vol.40, pp.580-584, 2012.

A. R. Atilgan, S. R. Durell, R. L. Jernigan, M. C. Demirel, O. Keskin et al., , 2001.

, Anisotropy of fluctuation dynamics of proteins with an elastic network model, Biophys. J, vol.80, pp.505-515

I. Bahar, T. R. Lezon, A. Bakan, and I. H. Shrivastava, Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins, Chem. Rev, vol.110, pp.1463-1497, 2010.

C. I. Bayly, P. Cieplak, W. Cornell, and P. A. Kollman, A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model, J. Phys. Chem, vol.97, pp.10269-10280, 1993.

E. E. Benson and K. Linderstrom-lang, Deuterium exchange between myoglobin and water, Biochim. Biophys. Acta, vol.32, pp.579-581, 1959.

W. D. Cornell, P. Cieplak, C. I. Bayly, I. R. Gould, K. M. Merz et al., A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules, J. Am. Chem. Soc, vol.117, pp.5179-5197, 1995.

M. A. Cuendet and O. Michielin, Protein-protein interaction investigated by steered molecular dynamics: the TCR-pMHC complex, Biophys. J, vol.95, pp.3575-3590, 2008.

C. C. David and D. J. Jacobs, Principal component analysis: a method for determining the essential dynamics of proteins, Methods Mol. Biol, vol.1084, pp.193-226, 2014.

M. O. Dayhoff, A model of evolutionary change in proteins, Atlas of Protein Sequence and Structure, vol.5, pp.89-99, 1972.

R. C. Edgar, MUSCLE: multiple sequence alignment with high accuracy and high throughput, Nucleic Acids Res, vol.32, pp.1792-1797, 2004.

S. W. Englander, L. Mayne, Y. Bai, and T. R. Sosnick, Hydrogen exchange: the modern legacy of Linderstrøm-Lang, Protein Sci, vol.6, pp.1101-1109, 1997.

J. Fan, M. B. Rone, P. , and V. , Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis, J. Biol. Chem, vol.284, pp.30484-30497, 2009.

W. M. Fitch, On the problem of discovering the most parsimonious tree, Am. Nat, vol.111, pp.223-257, 1977.

A. E. García and K. Y. Sanbonmatsu, Alpha-helical stabilization by side chain shielding of backbone hydrogen bonds, Proc Natl Acad Sci, vol.99, pp.2782-2787, 2002.

A. Gavezzotti, Molecular aggregation: structure analysis and molecular simulation of crystals and liquids, 2007.

M. Girvan and M. E. Newman, Community structure in social and biological networks, Proc Natl Acad Sci, vol.99, pp.7821-7826, 2002.

M. A. González, Force fields and molecular dynamics simulations, JDN, vol.12, pp.169-200, 2011.

B. J. Grant, A. P. Rodrigues, K. M. Elsawy, J. A. Mccammon, and L. S. Caves, Bio3d: an R package for the comparative analysis of protein structures, Bioinformatics, vol.22, pp.2695-2696, 2006.

S. Guindon, F. Lethiec, P. Duroux, and O. Gascuel, PHYML Online--a web server for fast maximum likelihood-based phylogenetic inference, Nucleic Acids Res, vol.33, pp.557-566, 2005.
URL : https://hal.archives-ouvertes.fr/lirmm-00105317

S. Guindon, J. Dufayard, V. Lefort, M. Anisimova, W. Hordijk et al., New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0, Syst. Biol, vol.59, pp.307-321, 2010.
URL : https://hal.archives-ouvertes.fr/lirmm-00511784

A. T. Hagler and S. Lifson, Energy functions for peptides and proteins. II. The amide hydrogen bond and calculation of amide crystal properties, J. Am. Chem. Soc, vol.96, pp.5327-5335, 1974.

G. Von-heijne, Proline kinks in transmembrane alpha-helices, J. Mol. Biol, vol.218, pp.499-503, 1991.

S. Henikoff and J. G. Henikoff, Amino acid substitution matrices from protein blocks, Proc Natl Acad Sci, vol.89, pp.10915-10919, 1992.

V. Hornak, R. Abel, A. Okur, B. Strockbine, A. Roitberg et al., Comparison of multiple Amber force fields and development of improved protein backbone parameters, Proteins, vol.65, pp.712-725, 2006.

N. Hurwitz, D. Schneidman-duhovny, and H. J. Wolfson, Memdock: an ?-helical membrane protein docking algorithm, Bioinformatics, vol.32, pp.2444-2450, 2016.

A. Hvidt and K. Linderstrøm-lang, Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions, Biochim. Biophys. Acta, vol.14, pp.574-575, 1954.

J. P. Jämbeck and A. P. Lyubartsev, Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids, J. Phys. Chem. B, vol.116, pp.3164-3179, 2012.

J. P. Jämbeck and A. P. Lyubartsev, An Extension and Further Validation of an All-Atomistic Force Field for Biological Membranes, J. Chem. Theory Comput, vol.8, pp.2938-2948, 2012.

D. T. Jones, Protein secondary structure prediction based on position-specific scoring matrices, J. Mol. Biol, vol.292, pp.195-202, 1999.

D. H. De-jong, G. Singh, W. F. Bennett, C. Arnarez, T. A. Wassenaar et al., Improved parameters for the MARTINI coarse-grained protein force field, J. Chem. Theory Comput, vol.9, pp.687-697, 2013.

W. Kabsch and C. Sander, Secondary structure definition by the program DSSP, Biopolymers, vol.22, pp.2577-2637, 1983.

A. A. Kaczor, J. Selent, F. Sanz, and M. Pastor, Modeling complexes of transmembrane proteins: systematic analysis of protein protein docking tools, Mol. Inform, vol.32, pp.717-733, 2013.

M. Karplus and J. Kuriyan, Molecular dynamics and protein function, Proc Natl Acad Sci, vol.102, pp.6679-6685, 2005.

M. Karplus and J. A. Mccammon, Molecular dynamics simulations of biomolecules, Nat. Struct. Biol, vol.9, pp.646-652, 2002.

K. Katoh, K. Misawa, K. Kuma, and T. Miyata, MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform, Nucleic Acids Res, vol.30, pp.3059-3066, 2002.

M. Kimura, The neutral theory of molecular evolution, Sci. Am, vol.241, pp.98-100, 1979.

J. B. Klauda, R. M. Venable, J. A. Freites, J. W. O'connor, D. J. Tobias et al., Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types, J. Phys. Chem. B, vol.114, pp.7830-7843, 2010.

S. Kundu, J. S. Melton, D. C. Sorensen, and G. N. Phillips, Dynamics of proteins in crystals: comparison of experiment with simple models, Biophys. J, vol.83, pp.723-732, 2002.

K. Linderstromlang, Deuterium exchange between peptides and water, Chemistry & Industry, vol.503, 1955.

K. Lindorff-larsen, S. Piana, K. Palmo, P. Maragakis, J. L. Klepeis et al., Improved side-chain torsion potentials for the Amber ff99SB protein force field, Proteins, vol.78, pp.1950-1958, 2010.

H. Liu, A. E. Mark, and W. F. Van-gunsteren, Estimating the Relative Free Energy of Different Molecular States with Respect to a Single Reference State, J. Phys. Chem, vol.100, pp.9485-9494, 1996.

A. L. Lomize, I. D. Pogozheva, M. A. Lomize, and H. I. Mosberg, Positioning of proteins in membranes: a computational approach, Protein Sci, vol.15, pp.1318-1333, 2006.

A. L. Lomize, I. D. Pogozheva, and H. I. Mosberg, Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes, J. Chem. Inf. Model, vol.51, pp.930-946, 2011.

M. A. Lomize, I. D. Pogozheva, H. Joo, H. I. Mosberg, and A. L. Lomize, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res, vol.40, pp.370-376, 2012.

S. J. Marrink and D. P. Tieleman, Perspective on the Martini model, Chem. Soc. Rev, vol.42, pp.6801-6822, 2013.

S. J. Marrink, A. H. De-vries, and A. E. Mark, Coarse grained model for semiquantitative lipid simulations, J. Phys. Chem. B, vol.108, pp.750-760, 2004.

S. J. Marrink, H. J. Risselada, S. Yefimov, D. P. Tieleman, and A. H. De-vries, The MARTINI force field: coarse grained model for biomolecular simulations, J. Phys. Chem. B, vol.111, pp.7812-7824, 2007.

J. A. Mccammon, B. R. Gelin, and M. Karplus, Dynamics of folded proteins, Nature, vol.267, pp.585-590, 1977.

L. Monticelli, S. K. Kandasamy, X. Periole, R. G. Larson, D. P. Tieleman et al., , 2008.

, The MARTINI coarse-grained force field: Extension to proteins, J. Chem. Theory Comput, vol.4, pp.819-834

H. Na, D. Ben-avraham, and M. M. Tirion, Slow normal modes of proteins are accurately reproduced across different platforms, Phys. Biol, vol.16, p.16003, 2018.

A. Okur, B. Strockbine, V. Hornak, and C. Simmerling, Using PC clusters to evaluate the transferability of molecular mechanics force fields for proteins, J. Comput. Chem, vol.24, pp.21-31, 2003.

E. Papaleo, P. Mereghetti, P. Fantucci, R. Grandori, D. Gioia et al., Free-energy landscape, principal component analysis, and structural clustering to identify representative conformations from molecular dynamics simulations: the myoglobin case, J. Mol. Graph. Model, vol.27, pp.889-899, 2009.

J. Pei and N. V. Grishin, PROMALS3D: multiple protein sequence alignment enhanced with evolutionary and three-dimensional structural information, Methods Mol. Biol, vol.1079, pp.263-271, 2014.

J. Pei, B. Kim, and N. V. Grishin, PROMALS3D: a tool for multiple protein sequence and structure alignments, Nucleic Acids Res, vol.36, pp.2295-2300, 2008.

J. W. Ponder and D. A. Case, Force fields for protein simulations, Adv. Protein Chem, vol.66, pp.27-85, 2003.

C. Rakers, M. Bermudez, B. G. Keller, J. Mortier, and G. Wolber, Computational close up on protein-protein interactions: how to unravel the invisible using molecular dynamics simulations?, WIREs Comput Mol Sci, vol.5, pp.345-359, 2015.

P. Sang, L. Yang, X. Ji, Y. Fu, and S. Liu, Insight derived from molecular dynamics simulations into molecular motions, thermodynamics and kinetics of HIV-1 gp120, PLoS ONE, vol.9, 2014.

D. Schneidman-duhovny, Y. Inbar, R. Nussinov, and H. J. Wolfson, PatchDock and SymmDock: servers for rigid and symmetric docking, Nucleic Acids Res, vol.33, pp.363-370, 2005.

O. Serçinoglu and P. Ozbek, gRINN: a tool for calculation of residue interaction energies and protein energy network analysis of molecular dynamics simulations, Nucleic Acids Res, vol.46, pp.554-562, 2018.

S. A. Showalter and R. Brüschweiler, Validation of molecular dynamics simulations of biomolecules using NMR spin relaxation as benchmarks: application to the AMBER99SB force field, J. Chem. Theory Comput, vol.3, pp.961-975, 2007.

J. D. Thompson, T. J. Gibson, and D. G. Higgins, Multiple sequence alignment using ClustalW and ClustalX, Curr. Protoc. Bioinformatics Chapter, 2002.

M. M. Tirion, Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis, Phys. Rev. Lett, vol.77, pp.1905-1908, 1996.

A. Tovchigrechko and I. A. Vakser, GRAMM-X public web server for protein-protein docking, Nucleic Acids Res, vol.34, pp.310-314, 2006.

D. Van-der-spoel, E. Lindahl, and B. Hess, GROMACS development team, 2014.

S. Vishveshwara, K. V. Brinda, and N. Kannan, Protein Structure: Insights from graph theory, J. Theor. Comput. Chem, vol.01, pp.187-211, 2002.

S. Vishveshwara, A. Ghosh, and P. Hansia, Intra and inter-molecular communications through protein structure network, Curr. Protein Pept. Sci, vol.10, pp.146-160, 2009.

J. Wang, P. Cieplak, and P. A. Kollman, How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?, J. Comput. Chem, vol.21, pp.1049-1074, 2000.

S. J. Weiner, P. A. Kollman, D. A. Case, U. C. Singh, C. Ghio et al., A new force field for molecular mechanical simulation of nucleic acids and proteins, J. Am. Chem. Soc, vol.106, pp.765-784, 1984.

L. Yang, E. Eyal, C. Chennubhotla, J. Jee, A. M. Gronenborn et al., Insights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions, Structure, vol.15, pp.741-749, 2007.

S. O. Yesylevskyy, L. V. Schäfer, D. Sengupta, and S. J. Marrink, Polarizable water model for the coarse-grained MARTINI force field, PLoS Comput. Biol, vol.6, 2010.

H. Ashkenazy, S. Abadi, E. Martz, O. Chay, I. Mayrose et al., ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules, Nucleic Acids Res, vol.44, pp.344-50, 2016.

T. Azarashvili, Y. Baburina, D. Grachev, O. Krestinina, V. Papadopoulos et al., Carbenoxolone induces permeability transition pore opening in rat mitochondria via the translocator protein TSPO and connexin43, Arch. Biochem. Biophys, vol.558, pp.87-94, 2014.

A. Bakan, L. M. Meireles, and I. Bahar, ProDy: protein dynamics inferred from theory and experiments, Bioinformatics, vol.27, pp.1575-1577, 2011.

E. R. Barnea, F. Fares, and M. Gavish, Modulatory action of benzodiazepines on human term placental steroidogenesis in vitro, Mol. Cell. Endocrinol, vol.64, pp.155-159, 1989.

H. J. Berendsen, D. Van-der-spoel, and R. Van-drunen, GROMACS: A message-passing parallel molecular dynamics implementation, Comput. Phys. Commun, vol.91, pp.43-56, 1995.

H. S. Bose, V. R. Lingappa, and W. L. Miller, The steroidogenic acute regulatory protein, StAR, works only at the outer mitochondrial membrane, Endocr. Res, vol.28, pp.295-308, 2002.

G. Bouyer, A. Cueff, S. Egée, J. Kmiecik, Y. Maksimova et al., Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum, Blood, vol.118, pp.2305-2312, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00623072

A. E. Calogero, T. C. Kamilaris, R. Bernardini, E. O. Johnson, G. P. Chrousos et al., Effects of peripheral benzodiazepine receptor ligands on hypothalamic-pituitary-adrenal axis function in the rat, J. Pharmacol. Exp. Ther, vol.253, pp.729-737, 1990.

B. Costa, S. Pini, P. Gabelloni, E. Da-pozzo, M. Abelli et al., The spontaneous Ala147Thr amino acid substitution within the translocator protein influences pregnenolone production in lymphomonocytes of healthy individuals, Endocrinology, vol.150, pp.5438-5445, 2009.

W. L. Delano, Pymol: An open-source molecular graphics tool, CCP4 Newsletter On Protein Crystallography, vol.40, pp.82-92, 2002.

F. Delavoie, H. Li, M. Hardwick, J. Robert, C. Giatzakis et al., In vivo and in vitro peripheral-type benzodiazepine receptor polymerization: functional significance in drug ligand and cholesterol binding, Biochemistry, vol.42, pp.4506-4519, 2003.

D. Scala, C. Baier, C. J. Evans, L. S. Williamson, P. T. Fantini et al., Relevance of CARC and CRAC Cholesterol-Recognition Motifs in the Nicotinic Acetylcholine Receptor and Other Membrane-Bound Receptors, Curr. Top. Membr, vol.80, pp.3-23, 2017.

J. Fan, M. B. Rone, P. , and V. , Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis, J. Biol. Chem, vol.284, pp.30484-30497, 2009.

J. Fantini, C. Di-scala, L. S. Evans, P. T. Williamson, and F. J. Barrantes, A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes. Sci. Rep. 6 , 21907. Cloning and characterization of PRAX-1. A new protein that specifically interacts with the peripheral benzodiazepine receptor, J. Biol. Chem, vol.274, pp.2938-2952, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01772916

M. Gavish and L. Veenman, Regulation of mitochondrial, cellular, and organismal functions by TSPO, Adv. Pharmacol, vol.82, pp.103-136, 2018.

C. Ginter, I. Kiburu, and O. Boudker, Chemical catalysis by the translocator protein (18 kDa), Biochemistry, vol.52, pp.3609-3611, 2013.

F. Glaser, T. Pupko, I. Paz, R. E. Bell, D. Bechor-shental et al., , 2003.

, ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information, Bioinformatics, vol.19, pp.163-164

B. J. Grant, A. P. Rodrigues, K. M. Elsawy, J. A. Mccammon, and L. S. Caves, Bio3d: an R package for the comparative analysis of protein structures, Bioinformatics, vol.22, pp.2695-2696, 2006.

Y. Guo, R. C. Kalathur, Q. Liu, B. Kloss, R. Bruni et al., Protein structure. Structure and activity of tryptophan-rich TSPO proteins, vol.347, pp.551-555, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02116001

A. Hacisuleyman and B. Erman, Entropy Transfer between Residue Pairs and Allostery in Proteins: Quantifying Allosteric Communication in Ubiquitin, PLoS Comput. Biol, vol.13, p.1005319, 2017.

M. Hardwick, D. Fertikh, M. Culty, H. Li, B. Vidic et al., Peripheral-type benzodiazepine receptor (PBR) in human breast cancer: correlation of breast cancer cell aggressive phenotype with PBR expression, nuclear localization, and PBR-mediated cell proliferation and nuclear transport of cholesterol, Cancer Res, vol.59, pp.831-842, 1999.

G. Von-heijne, Proline kinks in transmembrane alpha-helices, J. Mol. Biol, vol.218, pp.499-503, 1991.

J. D. Hirsch, C. F. Beyer, L. Malkowitz, B. Beer, and A. J. Blume, Mitochondrial benzodiazepine receptors mediate inhibition of mitochondrial respiratory control, Mol. Pharmacol, vol.35, pp.157-163, 1989.

N. Jamin, J. Neumann, M. A. Ostuni, T. K. Vu, Z. Yao et al., Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor, Mol. Endocrinol, vol.19, pp.588-594, 2005.

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.343, pp.1363-1366, 2014.

M. Jaremko, ?. Jaremko, G. Jaipuria, S. Becker, and M. Zweckstetter, Structure of the mammalian TSPO/PBR protein, Biochem. Soc. Trans, vol.43, pp.566-571, 2015.

?. Jaremko, M. Jaremko, K. Giller, S. Becker, and M. Zweckstetter, Conformational flexibility in the transmembrane protein TSPO, Chem. Eur. J, vol.21, pp.16555-16563, 2015.

A. R. Jayakumar, K. S. Panickar, and M. D. Norenberg, Effects on free radical generation by ligands of the peripheral benzodiazepine receptor in cultured neural cells, J. Neurochem, vol.83, pp.1226-1234, 2002.

D. H. De-jong, G. Singh, W. F. Bennett, C. Arnarez, T. A. Wassenaar et al., Improved parameters for the MARTINI coarse-grained protein force field, J. Chem. Theory Comput, vol.9, pp.687-697, 2013.

W. Kabsch and C. Sander, Secondary structure definition by the program DSSP, Biopolymers, vol.22, pp.2577-2637, 1983.

M. Karplus and J. Kuriyan, Molecular dynamics and protein function, Proc Natl Acad Sci, vol.102, pp.6679-6685, 2005.

M. Karplus and J. A. Mccammon, Molecular dynamics simulations of biomolecules, Nat. Struct. Biol, vol.9, pp.646-652, 2002.

O. V. Krestinina, D. E. Grachev, I. V. Odinokova, G. Reiser, Y. V. Evtodienko et al., Effect of peripheral benzodiazepine receptor (PBR/TSPO) ligands on opening of Ca2+-induced pore and phosphorylation of 3.5-kDa polypeptide in rat brain mitochondria, Biochemistry Mosc, vol.74, pp.421-429, 2009.

W. Kugler, L. Veenman, Y. Shandalov, S. Leschiner, I. Spanier et al., Ligands of the mitochondrial 18 kDa translocator protein attenuate apoptosis of human glioblastoma cells exposed to erucylphosphohomocholine, Cell. Oncol, vol.30, pp.435-450, 2008.

J. J. Lacapère, F. Delavoie, H. Li, G. Péranzi, J. Maccario et al., Structural and functional study of reconstituted peripheral benzodiazepine receptor, Biochem. Biophys. Res. Commun, vol.284, pp.536-541, 2001.

Y. Lee, F. G. Siméon, E. Briard, and V. W. Pike, Solution structures of the prototypical 18 kDa translocator protein ligand, PK 11195, elucidated with 1H/13C NMR spectroscopy and quantum chemistry, ACS Chem. Neurosci, vol.3, pp.325-335, 2012.

H. Li, P. , and V. , Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern, Endocrinology, vol.139, pp.4991-4997, 1998.

F. Li, J. Liu, L. Valls, C. Hiser, and S. Ferguson-miller, Identification of a key cholesterol binding enhancement motif in translocator protein 18 kDa, Biochemistry, vol.54, pp.1441-1443, 2015.

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.347, pp.555-558, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02143564

F. Li, J. Liu, R. M. Garavito, and S. Ferguson-miller, Evolving understanding of translocator protein 18 kDa (TSPO), Pharmacol. Res, vol.99, pp.404-409, 2015.

H. Li, Z. Yao, B. Degenhardt, G. Teper, P. et al., Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide, Proc Natl Acad Sci, vol.98, pp.1267-1272, 2001.

H. Li, B. Degenhardt, D. Tobin, Z. X. Yao, K. Tasken et al., , 2001.

, Identification, localization, and function in steroidogenesis of PAP7: a peripheral-type benzodiazepine receptor-and PKA (RIalpha)-associated protein, Mol. Endocrinol, vol.15, pp.2211-2228

G. Liu, R. J. Middleton, W. W. Kam, .. Chin, D. Y. Hatty et al., Functional gains in energy and cell metabolism after TSPO gene insertion, Cell Cycle, vol.16, pp.436-447, 2017.

J. Liu, M. B. Rone, P. , and V. , Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis, J. Biol. Chem, vol.281, pp.38879-38893, 2006.

A. L. Lomize, I. D. Pogozheva, M. A. Lomize, and H. I. Mosberg, Positioning of proteins in membranes: a computational approach, Protein Sci, vol.15, pp.1318-1333, 2006.

A. L. Lomize, I. D. Pogozheva, and H. I. Mosberg, Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes, J. Chem. Inf. Model, vol.51, pp.930-946, 2011.

M. A. Lomize, I. D. Pogozheva, H. Joo, H. I. Mosberg, and A. L. Lomize, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res, vol.40, pp.370-376, 2012.

I. Marginedas-freixa, C. Hattab, G. Bouyer, F. Halle, A. Chene et al., TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to the inhibition of P. falciparum growth in human blood, Sci. Rep, vol.6, p.33516, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01369499

S. J. Marrink, H. J. Risselada, S. Yefimov, D. P. Tieleman, and A. H. De-vries, The MARTINI force field: coarse grained model for biomolecular simulations, J. Phys. Chem. B, vol.111, pp.7812-7824, 2007.

A. P. Mathieu, A. Fleury, L. Ducharme, P. Lavigne, and J. G. Lehoux, Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR, J. Mol. Endocrinol, vol.29, pp.327-345, 2002.

L. D. Mccauley, C. H. Park, N. C. Lan, J. M. Tomich, J. E. Shively et al., , 1995.

, Benzodiazepines and peptides stimulate pregnenolone synthesis in brain mitochondria, Eur. J. Pharmacol, vol.276, pp.145-153

M. W. Mcenery, A. M. Snowman, R. R. Trifiletti, and S. H. Snyder, Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier, Proc Natl Acad Sci, vol.89, pp.3170-3174, 1992.

M. C. Mendonça-torres and S. S. Roberts, The translocator protein (TSPO) ligand PK11195 induces apoptosis and cell cycle arrest and sensitizes to chemotherapy treatment in pre-and post-relapse neuroblastoma cell lines, Cancer Biol. Ther, vol.14, pp.319-326, 2013.

M. Mezei, Simulaid: a simulation facilitator and analysis program, J. Comput. Chem, vol.31, pp.2658-2668, 2010.

M. Mezei and M. Filizola, TRAJELIX: a computational tool for the geometric characterization of protein helices during molecular dynamics simulations, J. Comput. Aided Mol. Des, vol.20, pp.97-107, 2006.

L. Monticelli, S. K. Kandasamy, X. Periole, R. G. Larson, D. P. Tieleman et al., , 2008.

, The MARTINI coarse-grained force field: Extension to proteins, J. Chem. Theory Comput, vol.4, pp.819-834

D. Morin, J. Musman, S. Pons, A. Berdeaux, and B. Ghaleh, Mitochondrial translocator protein (TSPO): From physiology to cardioprotection, Biochem. Pharmacol, vol.105, pp.1-13, 2016.

K. Morohaku, S. H. Pelton, D. J. Daugherty, W. R. Butler, W. Deng et al., , 2014.

, Translocator protein/peripheral benzodiazepine receptor is not required for steroid hormone biosynthesis, Endocrinology, vol.155, pp.89-97

A. G. Mukhin, V. Papadopoulos, E. Costa, and K. E. Krueger, Mitochondrial benzodiazepine receptors regulate steroid biosynthesis, Proc Natl Acad Sci, vol.86, pp.9813-9816, 1989.

S. Murail, J. Robert, Y. Coïc, J. Neumann, M. A. Ostuni et al., Secondary and tertiary structures of the transmembrane domains of the translocator protein TSPO determined by NMR. Stabilization of the TSPO tertiary fold upon ligand binding, Biochim. Biophys. Acta, vol.1778, pp.1375-1381, 2008.

J. M. Olson, W. Mcneel, A. B. Young, and W. R. Mancini, Localization of the peripheral-type benzodiazepine binding site to mitochondria of human glioma cells, J Neurooncol, vol.13, pp.35-42, 1992.

S. Páll, M. J. Abraham, C. Kutzner, B. Hess, and E. Lindahl, Tackling Exascale Software Challenges in Molecular Dynamics Simulations with GROMACS, Solving Software Challenges for, pp.3-27, 2015.

J. Pan, S. Tristram-nagle, N. Kucerka, and J. F. Nagle, Temperature dependence of structure, bending rigidity, and bilayer interactions of dioleoylphosphatidylcholine bilayers, Biophys. J, vol.94, pp.117-124, 2008.

V. Papadopoulos, J. Liu, and M. Culty, Is there a mitochondrial signaling complex facilitating cholesterol import?, Mol. Cell. Endocrinol, pp.59-64, 2007.

V. Papadopoulos, J. Fan, and B. Zirkin, Translocator protein (18 kDa): an update on its function in steroidogenesis, J. Neuroendocrinol, vol.30, 2018.

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera-a visualization system for exploratory research and analysis, J. Comput. Chem, vol.25, pp.1605-1612, 2004.

C. Rampon, M. Bouzaffour, M. A. Ostuni, P. Dufourcq, C. Girard et al., Translocator protein (18 kDa) is involved in primitive erythropoiesis in zebrafish, FASEB J, vol.23, pp.4181-4192, 2009.

M. B. Rone, A. S. Midzak, L. Issop, G. Rammouz, S. Jagannathan et al., Identification of a dynamic mitochondrial protein complex driving cholesterol import, trafficking, and metabolism to steroid hormones, Mol. Endocrinol, vol.26, pp.1868-1882, 2012.

R. Rupprecht, V. Papadopoulos, G. Rammes, T. C. Baghai, J. Fan et al., Translocator protein (18 kDa) (TSPO) as a therapeutic target for neurological and psychiatric disorders, Nat. Rev. Drug Discov, vol.9, pp.971-988, 2010.

A. F. Santidrián, A. M. Cosialls, L. Coll-mulet, D. Iglesias-serret, M. De-frias et al., The potential anticancer agent PK11195 induces apoptosis irrespective of p53 and ATM status in chronic lymphocytic leukemia cells, Haematologica, vol.92, pp.1631-1638, 2007.

T. Schreiber, Measuring information transfer, Phys. Rev. Lett, vol.85, pp.461-464, 2000.

D. P. Tieleman, I. H. Shrivastava, M. R. Ulmschneider, and M. S. Sansom, Proline-induced hinges in transmembrane helices: possible roles in ion channel gating, Proteins, vol.44, pp.63-72, 2001.

Y. Tsujishita and J. H. Hurley, Structure and lipid transport mechanism of a StAR-related domain, Nat. Struct. Biol, vol.7, pp.408-414, 2000.

L. N. Tu, K. Morohaku, P. R. Manna, S. H. Pelton, W. R. Butler et al., Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis, J. Biol. Chem, vol.289, pp.27444-27454, 2014.

C. Vanhee, G. Zapotoczny, D. Masquelier, M. Ghislain, and H. Batoko, The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism, Plant Cell, vol.23, pp.785-805, 2011.

L. Veenman, V. Papadopoulos, and M. Gavish, Channel-like functions of the 18-kDa translocator protein (TSPO): regulation of apoptosis and steroidogenesis as part of the host-defense response, Curr. Pharm. Des, vol.13, pp.2385-2405, 2007.

L. Veenman, Y. Shandalov, and M. Gavish, VDAC activation by the 18 kDa translocator protein (TSPO), implications for apoptosis, J. Bioenerg. Biomembr, vol.40, pp.199-205, 2008.

L. Veenman, A. Vainshtein, N. Yasin, M. Azrad, and M. Gavish, Tetrapyrroles as Endogenous TSPO Ligands in Eukaryotes and Prokaryotes: Comparisons with Synthetic Ligands, Int. J. Mol. Sci, vol.17, 2016.

A. Verma, J. S. Nye, and S. H. Snyder, Porphyrins are endogenous ligands for the mitochondrial (peripheral-type) benzodiazepine receptor, Proc Natl Acad Sci, vol.84, pp.2256-2260, 1987.

A. C. Wallace, R. A. Laskowski, and J. M. Thornton, LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Protein Eng, vol.8, pp.127-134, 1995.

T. A. Wassenaar, K. Pluhackova, R. A. Böckmann, S. J. Marrink, and D. P. Tieleman, Going Backward: A Flexible Geometric Approach to Reverse Transformation from Coarse Grained to Atomistic Models, J. Chem. Theory Comput, vol.10, pp.676-690, 2014.

G. Wendler, P. Lindemann, J. Lacapère, P. , and V. , Protoporphyrin IX binding and transport by recombinant mouse PBR, Biochem. Biophys. Res. Commun, vol.311, pp.847-852, 2003.

L. A. West, R. D. Horvat, D. A. Roess, B. G. Barisas, J. L. Juengel et al., , 2001.

, Steroidogenic acute regulatory protein and peripheral-type benzodiazepine receptor associate at the mitochondrial membrane, Endocrinology, vol.142, pp.502-505

A. A. Yeliseev and S. Kaplan, A novel mechanism for the regulation of photosynthesis gene expression by the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1, J. Biol. Chem, vol.274, pp.21234-21243, 1999.

A. H. Zhao, L. N. Tu, C. Mukai, M. P. Sirivelu, V. V. Pillai et al., Mitochondrial translocator protein (TSPO) function is not essential for heme biosynthesis, J. Biol. Chem, vol.291, pp.1591-1603, 2016.

, Chapter, vol.4

H. J. Berendsen, D. Van-der-spoel, and R. Van-drunen, GROMACS: A message-passing parallel molecular dynamics implementation, Comput. Phys. Commun, vol.91, pp.43-56, 1995.

J. M. Bernassau, J. L. Reversat, P. Ferrara, D. Caput, and G. Lefur, A 3D model of the peripheral benzodiazepine receptor and its implication in intra mitochondrial cholesterol transport, J. Mol. Graph, vol.11, pp.236-244, 1993.

F. Bonsack, C. H. Alleyne, and S. Sukumari-ramesh, Augmented expression of TSPO after intracerebral hemorrhage: a role in inflammation?, J. Neuroinflammation, vol.13, p.151, 2016.

G. Bouyer, A. Cueff, S. Egée, J. Kmiecik, Y. Maksimova et al., Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum, Blood, vol.118, pp.2305-2312, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00623072

C. Braestrup and R. F. Squires, Specific benzodiazepine receptors in rat brain characterized by high-affinity (3H)diazepam binding, Proc Natl Acad Sci, vol.74, pp.3805-3809, 1977.

O. V. Chechneva and W. Deng, Mitochondrial translocator protein (TSPO), astrocytes and neuroinflammation, Neural Regen. Res, vol.11, pp.1056-1057, 2016.

F. Delavoie, H. Li, M. Hardwick, J. Robert, C. Giatzakis et al., In vivo and in vitro peripheral-type benzodiazepine receptor polymerization: functional significance in drug ligand and cholesterol binding, Biochemistry, vol.42, pp.4506-4519, 2003.

J. Duneau, A. P. Vegh, and J. N. Sturgis, A dimerization hierarchy in the transmembrane domains of the HER receptor family, Biochemistry, vol.46, pp.2010-2019, 2007.

M. Eilers, A. B. Patel, W. Liu, and S. O. Smith, Comparison of helix interactions in membrane and soluble alpha-bundle proteins, Biophys. J, vol.82, pp.2720-2736, 2002.

J. Fan, M. B. Rone, P. , and V. , Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis, J. Biol. Chem, vol.284, pp.30484-30497, 2009.

J. Fan, K. Wang, B. Zirkin, P. , and V. , CRISPR/Cas9-Mediated Tspo Gene Mutations Lead to Reduced Mitochondrial Membrane Potential and Steroid Formation, 2018.

, Mouse Tumor Leydig Cells. Endocrinology, vol.159, pp.1130-1146

J. Fantini, C. Di-scala, L. S. Evans, P. T. Williamson, and F. J. Barrantes, A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes, Sci. Rep, vol.6, p.21907, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01772916

B. J. Grant, A. P. Rodrigues, K. M. Elsawy, J. A. Mccammon, and L. S. Caves, Bio3d: an R package for the comparative analysis of protein structures, Bioinformatics, vol.22, pp.2695-2696, 2006.

Y. Guo, R. C. Kalathur, Q. Liu, B. Kloss, R. Bruni et al., Protein structure. Structure and activity of tryptophan-rich TSPO proteins, vol.347, pp.551-555, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02116001

M. Hardwick, D. Fertikh, M. Culty, H. Li, B. Vidic et al., Peripheral-type benzodiazepine receptor (PBR) in human breast cancer: correlation of breast cancer cell aggressive phenotype with PBR expression, nuclear localization, and PBR-mediated cell proliferation and nuclear transport of cholesterol, Cancer Res, vol.59, pp.831-842, 1999.

K. Hinsen, A. Vaitinadapoule, M. A. Ostuni, C. Etchebest, and J. Lacapere, Construction and validation of an atomic model for bacterial TSPO from electron microscopy density, evolutionary constraints, and biochemical and biophysical data, Biochim. Biophys. Acta, vol.1848, pp.568-580, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01171268

S. J. Hubbard and T. Naccess, Computer program. Department of Biochemistry and Molecular Biology, 1993.

N. Hurwitz, D. Schneidman-duhovny, and H. J. Wolfson, Memdock: an ?-helical membrane protein docking algorithm, Bioinformatics, vol.32, pp.2444-2450, 2016.

G. Jaipuria, A. Leonov, K. Giller, S. K. Vasa, ?. Jaremko et al., Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure, Nat. Commun, vol.8, p.14893, 2017.

L. Jaremko, M. Jaremko, S. Becker, and M. Zweckstetter, Toward the functional oligomerization state of tryptophan-rich sensory proteins, Protein Sci, vol.23, pp.1154-1160, 2014.

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.343, pp.1363-1366, 2014.

M. Jaremko, ?. Jaremko, G. Jaipuria, S. Becker, and M. Zweckstetter, Structure of the mammalian TSPO/PBR protein, Biochem. Soc. Trans, vol.43, pp.566-571, 2015.

M. Javanainen, H. Martinez-seara, and I. Vattulainen, Excessive aggregation of membrane proteins in the Martini model, PLoS ONE, vol.12, 2017.

C. Jefcoate, High-flux mitochondrial cholesterol trafficking, a specialized function of the adrenal cortex, J. Clin. Invest, vol.110, pp.881-890, 2002.

G. Kleiger, R. Grothe, P. Mallick, and D. Eisenberg, GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles, Biochemistry, vol.41, pp.5990-5997, 2002.

V. M. Korkhov, C. Sachse, J. M. Short, and C. G. Tate, Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals, Structure, vol.18, pp.677-687, 2010.

K. E. Krueger, P. , and V. , Peripheral-type benzodiazepine receptors mediate translocation of cholesterol from outer to inner mitochondrial membranes in adrenocortical cells, J. Biol. Chem, vol.265, pp.15015-15022, 1990.

W. Kugler, L. Veenman, Y. Shandalov, S. Leschiner, I. Spanier et al., Ligands of the mitochondrial 18 kDa translocator protein attenuate apoptosis of human glioblastoma cells exposed to erucylphosphohomocholine, Cell. Oncol, vol.30, pp.435-450, 2008.

J. J. Lacapère, F. Delavoie, H. Li, G. Péranzi, J. Maccario et al., Structural and functional study of reconstituted peripheral benzodiazepine receptor, Biochem. Biophys. Res. Commun, vol.284, pp.536-541, 2001.

M. A. Lemmon, J. M. Flanagan, H. R. Treutlein, J. Zhang, and D. M. Engelman, Sequence specificity in the dimerization of transmembrane alpha-helices, Biochemistry, vol.31, pp.12719-12725, 1992.

M. A. Lemmon, J. M. Flanagan, J. F. Hunt, B. D. Adair, B. J. Bormann et al., Glycophorin A dimerization is driven by specific interactions between transmembrane alpha-helices, J. Biol. Chem, vol.267, pp.7683-7689, 1992.

H. Li, P. , and V. , Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern, Endocrinology, vol.139, pp.4991-4997, 1998.

E. Li, W. C. Wimley, and K. Hristova, Transmembrane helix dimerization: beyond the search for sequence motifs, Biochim. Biophys. Acta, vol.1818, pp.183-193, 2012.

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.347, pp.555-558, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02143564

H. Li, Z. Yao, B. Degenhardt, G. Teper, P. et al., Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide, Proc Natl Acad Sci, vol.98, pp.1267-1272, 2001.

G. Liu, R. J. Middleton, C. R. Hatty, W. W. Kam, .. Chan et al., The 18 kDa translocator protein, microglia and neuroinflammation, Brain Pathol, vol.24, pp.631-653, 2014.

K. Maaser, M. Höpfner, A. Jansen, G. Weisinger, M. Gavish et al., Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human colorectal cancer cells, Br. J. Cancer, vol.85, pp.1771-1780, 2001.

M. R. Machado, E. E. Barrera, F. Klein, M. Sóñora, S. Silva et al., The SIRAH force field 2.0: Altius, Fortius, Citius, J. Chem. Theory Comput, 2019.

L. D. Mccauley, C. H. Park, N. C. Lan, J. M. Tomich, J. E. Shively et al., , 1995.

, Benzodiazepines and peptides stimulate pregnenolone synthesis in brain mitochondria, Eur. J. Pharmacol, vol.276, pp.145-153

D. Mercadante, F. Gräter, and C. Daday, CONAN: A Tool to Decode Dynamical Information from Molecular Interaction Maps, Biophys. J, vol.114, pp.1267-1273, 2018.

K. Morohaku, S. H. Pelton, D. J. Daugherty, W. R. Butler, W. Deng et al., , 2014.

, Translocator protein/peripheral benzodiazepine receptor is not required for steroid hormone biosynthesis, Endocrinology, vol.155, pp.89-97

B. K. Mueller, S. Subramaniam, and A. Senes, A frequent, GxxxG-mediated, transmembrane association motif is optimized for the formation of interhelical C?-H hydrogen bonds, Proc Natl Acad Sci, vol.111, pp.888-95, 2014.

A. G. Mukhin, V. Papadopoulos, E. Costa, and K. E. Krueger, Mitochondrial benzodiazepine receptors regulate steroid biosynthesis, Proc Natl Acad Sci, vol.86, pp.9813-9816, 1989.

S. Páll, M. J. Abraham, C. Kutzner, B. Hess, and E. Lindahl, Tackling Exascale Software Challenges in Molecular Dynamics Simulations with GROMACS, Solving Software Challenges for, pp.3-27, 2015.

V. Papadopoulos, F. B. Nowzari, and K. E. Krueger, Hormone-stimulated steroidogenesis is coupled to mitochondrial benzodiazepine receptors. Tropic hormone action on steroid biosynthesis is inhibited by flunitrazepam, J. Biol. Chem, vol.266, pp.3682-3687, 1991.

V. Papadopoulos, N. Boujrad, M. D. Ikonomovic, P. Ferrara, and B. Vidic, Topography of the Leydig cell mitochondrial peripheral-type benzodiazepine receptor, Mol. Cell. Endocrinol, vol.104, pp.5-9, 1994.

V. Papadopoulos, H. Amri, H. Li, N. Boujrad, B. Vidic et al., Targeted disruption of the peripheral-type benzodiazepine receptor gene inhibits steroidogenesis in the R2C Leydig tumor cell line, J. Biol. Chem, vol.272, pp.32129-32135, 1997.

V. Papadopoulos, H. Amri, N. Boujrad, C. Cascio, M. Culty et al., Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis, Steroids, vol.62, pp.21-28, 1997.

V. Papadopoulos, M. Baraldi, T. R. Guilarte, T. B. Knudsen, J. Lacapère et al., Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function, Trends Pharmacol. Sci, vol.27, pp.402-409, 2006.

V. Papadopoulos, J. Liu, and M. Culty, Is there a mitochondrial signaling complex facilitating cholesterol import?, Mol. Cell. Endocrinol, pp.59-64, 2007.

V. Papadopoulos, J. Fan, and B. Zirkin, Translocator protein (18 kDa): an update on its function in steroidogenesis, J. Neuroendocrinol, vol.30, 2018.

D. Pogoryelov, A. L. Klyszejko, G. O. Krasnoselska, E. Heller, V. Leone et al., Engineering rotor ring stoichiometries in the ATP synthase, Proc Natl Acad Sci, vol.109, pp.1599-608, 2012.

C. Rampon, M. Bouzaffour, M. A. Ostuni, P. Dufourcq, C. Girard et al., Translocator protein (18 kDa) is involved in primitive erythropoiesis in zebrafish, FASEB J, vol.23, pp.4181-4192, 2009.

A. Ridder, P. Skupjen, S. Unterreitmeier, and D. Langosch, Tryptophan supports interaction of transmembrane helices, J. Mol. Biol, vol.354, pp.894-902, 2005.

V. Selvaraj and D. M. Stocco, The changing landscape in translocator protein (TSPO) function, Trends Endocrinol. Metab, vol.26, pp.341-348, 2015.

E. S. Sulistijo and K. R. Mackenzie, Structural basis for dimerization of the BNIP3 transmembrane domain, Biochemistry, vol.48, pp.5106-5120, 2009.

L. N. Tu, K. Morohaku, P. R. Manna, S. H. Pelton, W. R. Butler et al., Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis, J. Biol. Chem, vol.289, pp.27444-27454, 2014.

S. Unterreitmeier, A. Fuchs, T. Schäffler, R. G. Heym, D. Frishman et al., , 2007.

, Phenylalanine promotes interaction of transmembrane domains via GxxxG motifs, J. Mol. Biol, vol.374, pp.705-718

L. Veenman and M. Gavish, The role of 18 kDa mitochondrial translocator protein (TSPO) in programmed cell death, and effects of steroids on TSPO expression, Curr. Mol. Med, vol.12, pp.398-412, 2012.

L. Veenman, Y. Shandalov, and M. Gavish, VDAC activation by the 18 kDa translocator protein (TSPO), implications for apoptosis, J. Bioenerg. Biomembr, vol.40, pp.199-205, 2008.

M. Weber and D. Schneider, Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding, FEBS Lett, vol.587, pp.1592-1596, 2013.

J. Zeng, R. Guareschi, M. Damre, R. Cao, A. Kless et al., Structural prediction of the dimeric form of the mammalian translocator membrane protein TSPO: A key target for brain diagnostics, Int. J. Mol. Sci, vol.19, 2018.

S. Zeno, L. Veenman, Y. Katz, J. Bode, M. Gavish et al., The 18 kDa mitochondrial translocator protein (TSPO) prevents accumulation of protoporphyrin IX. Involvement of reactive oxygen species (ROS), Curr. Mol. Med, vol.12, pp.494-501, 2012.

F. X. Zhou, H. J. Merianos, A. T. Brunger, and D. M. Engelman, Polar residues drive association of polyleucine transmembrane helices, Proc Natl Acad Sci, vol.98, pp.2250-2255, 2001.

A. Zoued, J. Duneau, E. Durand, A. P. España, L. Journet et al., Tryptophan-mediated Dimerization of the TssL Transmembrane Anchor Is Required for Type VI Secretion System Activity, J. Mol. Biol, vol.430, pp.987-1003, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01780763

, Chapter, vol.5

A. E. Aliev, M. Kulke, H. S. Khaneja, V. Chudasama, T. D. Sheppard et al., Motional timescale predictions by molecular dynamics simulations: case study using proline and hydroxyproline sidechain dynamics, Proteins, vol.82, pp.195-215, 2014.

H. Ashkenazy, S. Abadi, E. Martz, O. Chay, I. Mayrose et al., ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules, Nucleic Acids Res, vol.44, pp.344-50, 2016.

A. Bakan, L. M. Meireles, and I. Bahar, ProDy: protein dynamics inferred from theory and experiments, Bioinformatics, vol.27, pp.1575-1577, 2011.

E. Balsemão-pires, Y. Jaillais, B. J. Olson, L. R. Andrade, J. G. Umen et al., The Arabidopsis translocator protein (AtTSPO) is regulated at multiple levels in response to salt stress and perturbations in tetrapyrrole metabolism, BMC Plant Biol, vol.11, p.108, 2011.

A. Bateman, L. Coin, R. Durbin, R. D. Finn, V. Hollich et al., The Pfam protein families database, Nucleic Acids Res, vol.32, pp.138-179, 2004.
URL : https://hal.archives-ouvertes.fr/hal-01294685

A. W. Busch and B. L. Montgomery, The Tryptophan-Rich Sensory Protein (TSPO) is Involved in Stress-Related and Light-Dependent Processes in the Cyanobacterium Fremyella diplosiphon, Front. Microbiol, vol.6, p.1393, 2015.

A. W. Busch and B. L. Montgomery, Distinct light-, stress-, and nutrient-dependent regulation of multiple tryptophan-rich sensory protein (TSPO) genes in the cyanobacterium Fremyella diplosiphon, Plant Signal. Behav, vol.12, p.1293221, 2017.

A. W. Busch, Z. Warejoncas, and B. L. Montgomery, Tryptophan-Rich Sensory Protein/Translocator Protein (TSPO) from Cyanobacterium Fremyella diplosiphon Binds a Broad Range of Functionally Relevant Tetrapyrroles, Biochemistry, vol.56, pp.73-84, 2017.

A. Colasanti, D. R. Owen, D. Grozeva, E. A. Rabiner, P. M. Matthews et al., Bipolar Disorder is associated with the rs6971 polymorphism in the gene encoding 18 kDa Translocator Protein (TSPO), Psychoneuroendocrinology, vol.38, pp.2826-2829, 2013.

B. Costa, S. Pini, P. Gabelloni, E. Da-pozzo, M. Abelli et al., The spontaneous Ala147Thr amino acid substitution within the translocator protein influences pregnenolone production in lymphomonocytes of healthy individuals, Endocrinology, vol.150, pp.5438-5445, 2009.

B. Costa, S. Pini, C. Martini, M. Abelli, P. Gabelloni et al., Ala147Thr substitution in translocator protein is associated with adult separation anxiety in patients with depression, Psychiatr. Genet, vol.19, pp.110-111, 2009.

A. Drozdetskiy, C. Cole, J. Procter, and G. J. Barton, JPred4: a protein secondary structure prediction server, Nucleic Acids Res, vol.43, pp.389-94, 2015.

S. El-gebali, J. Mistry, A. Bateman, S. R. Eddy, A. Luciani et al., The Pfam protein families database in 2019, Nucleic Acids Res, vol.47, pp.427-432, 2019.

J. Fan, P. Lindemann, M. G. Feuilloley, P. , and V. , Structural and functional evolution of the translocator protein (18 kDa), Curr. Mol. Med, vol.12, pp.369-386, 2012.

J. Fantini, C. Di-scala, L. S. Evans, P. T. Williamson, and F. J. Barrantes, A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes, Sci. Rep, vol.6, p.21907, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01772916

R. D. Finn, P. Coggill, R. Y. Eberhardt, S. R. Eddy, J. Mistry et al., The Pfam protein families database: towards a more sustainable future, Nucleic Acids Res, vol.44, pp.279-85, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01294685

C. Ginter, I. Kiburu, and O. Boudker, Chemical catalysis by the translocator protein (18 kDa), Biochemistry, vol.52, pp.3609-3611, 2013.

F. Glaser, T. Pupko, I. Paz, R. E. Bell, D. Bechor-shental et al., , 2003.

, ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information, Bioinformatics, vol.19, pp.163-164

Y. Guo, R. C. Kalathur, Q. Liu, B. Kloss, R. Bruni et al., Protein structure. Structure and activity of tryptophan-rich TSPO proteins, vol.347, pp.551-555, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02116001

W. Humphrey, A. Dalke, and K. Schulten, VMD: visual molecular dynamics, J. Mol. Graph, vol.14, pp.33-38, 1996.

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.343, pp.1363-1366, 2014.

C. Leneveu-jenvrin, N. Connil, E. Bouffartigues, V. Papadopoulos, M. G. Feuilloley et al., Structure-to-function relationships of bacterial translocator protein (TSPO): a focus on, Pseudomonas. Front. Microbiol, vol.5, p.631, 2014.

C. Leneveu-jenvrin, E. Bouffartigues, O. Maillot, P. Cornelis, M. G. Feuilloley et al., Expression of the translocator protein (TSPO) from Pseudomonas fluorescens Pf0-1 requires the stress regulatory sigma factors AlgU and RpoH, Front. Microbiol, vol.6, p.1023, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02386393

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.347, pp.555-558, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02143564

F. Li, J. Liu, R. M. Garavito, and S. Ferguson-miller, Evolving understanding of translocator protein 18 kDa (TSPO), Pharmacol. Res, vol.99, pp.404-409, 2015.

A. L. Lomize, I. D. Pogozheva, and H. I. Mosberg, Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes, J. Chem. Inf. Model, vol.51, pp.930-946, 2011.

M. A. Lomize, I. D. Pogozheva, H. Joo, H. I. Mosberg, and A. L. Lomize, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res, vol.40, pp.370-376, 2012.

I. Marginedas-freixa, C. Hattab, G. Bouyer, F. Halle, A. Chene et al., TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to the inhibition of P. falciparum growth in human blood, Sci. Rep, vol.6, p.33516, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01369499

V. Papadopoulos, J. Fan, and B. Zirkin, Translocator protein (18 kDa): an update on its function in steroidogenesis, J. Neuroendocrinol, vol.30, 2018.

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera-a visualization system for exploratory research and analysis, J. Comput. Chem, vol.25, pp.1605-1612, 2004.

C. Rampon, M. Bouzaffour, M. A. Ostuni, P. Dufourcq, C. Girard et al., Translocator protein (18 kDa) is involved in primitive erythropoiesis in zebrafish, FASEB J, vol.23, pp.4181-4192, 2009.

C. Vanhee, G. Zapotoczny, D. Masquelier, M. Ghislain, and H. Batoko, The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism, Plant Cell, vol.23, pp.785-805, 2011.

A. C. Wallace, R. A. Laskowski, and J. M. Thornton, LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions, Protein Eng, vol.8, pp.127-134, 1995.

A. M. Waterhouse, J. B. Procter, D. M. Martin, M. Clamp, and G. J. Barton, Jalview Version 2--a multiple sequence alignment editor and analysis workbench, Bioinformatics, vol.25, pp.1189-1191, 2009.

G. Wendler, P. Lindemann, J. Lacapère, P. , and V. , Protoporphyrin IX binding and transport by recombinant mouse PBR, Biochem. Biophys. Res. Commun, vol.311, pp.847-852, 2003.

A. A. Yeliseev and S. Kaplan, A sensory transducer homologous to the mammalian peripheral-type benzodiazepine receptor regulates photosynthetic membrane complex formation in Rhodobacter sphaeroides 2.4.1, J. Biol. Chem, vol.270, pp.21167-21175, 1995.

A. A. Yeliseev and S. Kaplan, TspO of rhodobacter sphaeroides. A structural and functional model for the mammalian peripheral benzodiazepine receptor, J. Biol. Chem, vol.275, pp.5657-5667, 2000.

X. Zeng and S. Kaplan, TspO as a modulator of the repressor/antirepressor (PpsR/AppA) regulatory system in Rhodobacter sphaeroides 2.4.1, J. Bacteriol, vol.183, pp.6355-6364, 2001.

S. Zeno, L. Veenman, Y. Katz, J. Bode, M. Gavish et al., The 18 kDa mitochondrial translocator protein (TSPO) prevents accumulation of protoporphyrin IX. Involvement of reactive oxygen species (ROS), Curr. Mol. Med, vol.12, pp.494-501, 2012.

, Chapter, vol.6

M. K. Anderson, X. Sun, A. L. Miracle, G. W. Litman, and E. V. Rothenberg, Evolution of hematopoiesis: Three members of the PU.1 transcription factor family in a cartilaginous fish, Raja eglanteria, Proc Natl Acad Sci, vol.98, pp.553-558, 2001.

A. Bakan, L. M. Meireles, and I. Bahar, ProDy: protein dynamics inferred from theory and experiments, Bioinformatics, vol.27, pp.1575-1577, 2011.

G. Bouyer, A. Cueff, S. Egée, J. Kmiecik, Y. Maksimova et al., Erythrocyte peripheral type benzodiazepine receptor/voltage-dependent anion channels are upregulated by Plasmodium falciparum, Blood, vol.118, pp.2305-2312, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00623072

R. Brüschweiler, Collective protein dynamics and nuclear spin relaxation, J. Chem. Phys, vol.102, p.3396, 1995.

R. Brüschweiler and D. A. Case, Collective NMR relaxation model applied to protein dynamics, Phys. Rev. Lett, vol.72, pp.940-943, 1994.

A. Colasanti, D. R. Owen, D. Grozeva, E. A. Rabiner, P. M. Matthews et al., Bipolar Disorder is associated with the rs6971 polymorphism in the gene encoding 18 kDa Translocator Protein (TSPO), Psychoneuroendocrinology, vol.38, pp.2826-2829, 2013.

B. Costa, S. Pini, P. Gabelloni, E. Da-pozzo, M. Abelli et al., The spontaneous Ala147Thr amino acid substitution within the translocator protein influences pregnenolone production in lymphomonocytes of healthy individuals, Endocrinology, vol.150, pp.5438-5445, 2009.

B. Costa, S. Pini, C. Martini, M. Abelli, P. Gabelloni et al., Ala147Thr substitution in translocator protein is associated with adult separation anxiety in patients with depression, Psychiatr. Genet, vol.19, pp.110-111, 2009.

C. C. David and D. J. Jacobs, Principal component analysis: a method for determining the essential dynamics of proteins, Methods Mol. Biol, vol.1084, pp.193-226, 2014.

D. Scala, C. Baier, C. J. Evans, L. S. Williamson, P. T. Fantini et al., Relevance of CARC and CRAC Cholesterol-Recognition Motifs in the Nicotinic Acetylcholine Receptor and Other Membrane-Bound Receptors, Curr. Top. Membr, vol.80, pp.3-23, 2017.

J. Fan, M. B. Rone, P. , and V. , Translocator protein 2 is involved in cholesterol redistribution during erythropoiesis, J. Biol. Chem, vol.284, pp.30484-30497, 2009.

J. Fan, P. Lindemann, M. G. Feuilloley, P. , and V. , Structural and functional evolution of the translocator protein (18 kDa), Curr. Mol. Med, vol.12, pp.369-386, 2012.

J. Fantini, C. Di-scala, L. S. Evans, P. T. Williamson, and F. J. Barrantes, A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes, Sci. Rep, vol.6, p.21907, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01772916

C. Ginter, I. Kiburu, and O. Boudker, Chemical catalysis by the translocator protein (18 kDa), Biochemistry, vol.52, pp.3609-3611, 2013.

Y. Guo, R. C. Kalathur, Q. Liu, B. Kloss, R. Bruni et al., Protein structure. Structure and activity of tryptophan-rich TSPO proteins, vol.347, pp.551-555, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02116001

M. Hardwick, D. Fertikh, M. Culty, H. Li, B. Vidic et al., Peripheral-type benzodiazepine receptor (PBR) in human breast cancer: correlation of breast cancer cell aggressive phenotype with PBR expression, nuclear localization, and PBR-mediated cell proliferation and nuclear transport of cholesterol, Cancer Res, vol.59, pp.831-842, 1999.

M. J. Harms and J. W. Thornton, Analyzing protein structure and function using ancestral gene reconstruction, Curr. Opin. Struct. Biol, vol.20, pp.360-366, 2010.

P. W. Holland, J. Garcia-fernàndez, N. A. Williams, and A. Sidow, Gene duplications and the origins of vertebrate development, Dev, pp.125-133, 1994.

T. M. Holm, A. Braun, B. L. Trigatti, C. Brugnara, M. Sakamoto et al., Failure of red blood cell maturation in mice with defects in the high-density lipoprotein receptor SR-BI, Blood, vol.99, pp.1817-1824, 2002.

B. Isin, K. C. Tirupula, Z. N. Oltvai, J. Klein-seetharaman, and I. Bahar, Identification of motions in membrane proteins by elastic network models and their experimental validation, Methods Mol. Biol, vol.914, pp.285-317, 2012.

N. Jamin, J. Neumann, M. A. Ostuni, T. K. Vu, Z. Yao et al., Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor, Mol. Endocrinol, vol.19, pp.588-594, 2005.

Z. Johanson, J. A. Long, J. A. Talent, P. Janvier, and J. W. Warren, Oldest coelacanth, from the Early Devonian of Australia, Biol. Lett, vol.2, pp.443-446, 2006.
URL : https://hal.archives-ouvertes.fr/hal-00162912

K. Katoh, K. Misawa, K. Kuma, and T. Miyata, MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform, Nucleic Acids Res, vol.30, pp.3059-3066, 2002.

V. Kurauskas, A. Hessel, P. Ma, P. Lunette, K. Weinhaupl et al., How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine, Phys. Chem. Lett, vol.9, pp.933-938, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02336372

F. Li, J. Liu, L. Valls, C. Hiser, and S. Ferguson-miller, Identification of a key cholesterol binding enhancement motif in translocator protein 18 kDa, Biochemistry, vol.54, pp.1441-1443, 2015.

F. Li, J. Liu, R. M. Garavito, and S. Ferguson-miller, Evolving understanding of translocator protein 18 kDa (TSPO), Pharmacol. Res, vol.99, pp.404-409, 2015.

F. Li, J. Liu, Y. Zheng, R. M. Garavito, and S. Ferguson-miller, Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism, Science, vol.347, pp.555-558, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02143564

H. Li, Z. Yao, B. Degenhardt, G. Teper, P. et al., Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide, Proc Natl Acad Sci, vol.98, pp.1267-1272, 2001.

A. L. Lomize, I. D. Pogozheva, and H. I. Mosberg, Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranes, J. Chem. Inf. Model, vol.51, pp.930-946, 2011.

M. A. Lomize, I. D. Pogozheva, H. Joo, H. I. Mosberg, and A. L. Lomize, OPM database and PPM web server: resources for positioning of proteins in membranes, Nucleic Acids Res, vol.40, pp.370-376, 2012.

I. Marginedas-freixa, C. Hattab, G. Bouyer, F. Halle, A. Chene et al., TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to the inhibition of P. falciparum growth in human blood, Sci. Rep, vol.6, p.33516, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01369499

V. Papadopoulos, J. Fan, and B. Zirkin, Translocator protein (18 kDa): an update on its function in steroidogenesis, J. Neuroendocrinol, vol.30, 2018.

M. J. Pébusque, F. Coulier, D. Birnbaum, and P. Pontarotti, Ancient large-scale genome duplications: phylogenetic and linkage analyses shed light on chordate genome evolution, Mol. Biol. Evol, vol.15, pp.1145-1159, 1998.

E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt et al., UCSF Chimera-a visualization system for exploratory research and analysis, J. Comput. Chem, vol.25, pp.1605-1612, 2004.

G. Postic, Y. Ghouzam, and J. Gelly, OREMPRO web server: orientation and assessment of atomistic and coarse-grained structures of membrane proteins, Bioinformatics, vol.32, pp.2548-2550, 2016.

M. B. Rone, A. S. Midzak, L. Issop, G. Rammouz, S. Jagannathan et al., Identification of a dynamic mitochondrial protein complex driving cholesterol import, trafficking, and metabolism to steroid hormones, Mol. Endocrinol, vol.26, pp.1868-1882, 2012.

G. Simos, C. Maison, and S. D. Georgatos, Characterization of p18, a component of the lamin B receptor complex and a new integral membrane protein of the avian erythrocyte nuclear envelope, J. Biol. Chem, vol.271, pp.12617-12625, 1996.

J. W. Thornton, E. Need, and D. Crews, Resurrecting the ancestral steroid receptor: ancient origin of estrogen signaling, Science, vol.301, pp.1714-1717, 2003.

D. P. Tieleman, I. H. Shrivastava, M. R. Ulmschneider, and M. S. Sansom, Proline-induced hinges in transmembrane helices: possible roles in ion channel gating, Proteins, vol.44, pp.63-72, 2001.

C. Vanhee, G. Zapotoczny, D. Masquelier, M. Ghislain, and H. Batoko, The Arabidopsis multistress regulator TSPO is a heme binding membrane protein and a potential scavenger of porphyrins via an autophagy-dependent degradation mechanism, Plant Cell, vol.23, pp.785-805, 2011.

A. Verma, J. S. Nye, and S. H. Snyder, Porphyrins are endogenous ligands for the mitochondrial (peripheral-type) benzodiazepine receptor, Proc Natl Acad Sci, vol.84, pp.2256-2260, 1987.

A. M. Waterhouse, J. B. Procter, D. M. Martin, M. Clamp, and G. J. Barton, Jalview Version 2--a multiple sequence alignment editor and analysis workbench, Bioinformatics, vol.25, pp.1189-1191, 2009.

G. Wendler, P. Lindemann, J. Lacapère, P. , and V. , Protoporphyrin IX binding and transport by recombinant mouse PBR, Biochem. Biophys. Res. Commun, vol.311, pp.847-852, 2003.

A. A. Yeliseev and S. Kaplan, A novel mechanism for the regulation of photosynthesis gene expression by the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1, J. Biol. Chem, vol.274, pp.21234-21243, 1999.

, model for the mammalian peripheral benzodiazepine receptor, J. Biol. Chem, vol.275, pp.5657-5667

S. Yokoyama and F. B. Radlwimmer, The molecular genetics of red and green color vision in mammals, Genetics, vol.153, pp.919-932, 1999.

, Projection of ensemble of all TSPO conformations in presence of PK11195 (blue) as well as in absence of PK11195 (red), projected onto the subspace of PC1 and PC2. The PCA was performed on all the residues, including TM regions as well as extracellular loops, Annexure-1 PCA on TSPO conformations, residues, pp.6-157