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Volumn 26, Issue 7, 2015, Pages 349-356

Lost in translocation: The functions of the 18-kD translocator protein

Author keywords

Cholesterol; Heme metabolism; Mitochondrial permeability transition pore; Neuroimaging; Neuroinflammation; Peripheral benzodiazepine receptor; REV ERB

Indexed keywords

CARRIER PROTEIN; NEUROSTEROID; 4 AMINOBUTYRIC ACID RECEPTOR; BZRP PROTEIN, MOUSE; CHOLESTEROL; TSPO PROTEIN, HUMAN;

EID: 84937520495     PISSN: 10432760     EISSN: 18793061     Source Type: Journal    
DOI: 10.1016/j.tem.2015.04.001     Document Type: Review
Times cited : (56)

References (84)
  • 1
    • 0022574416 scopus 로고
    • The peripheral-type benzodiazepine receptor. Localization to the mitochondrial outer membrane
    • Anholt R.R., et al. The peripheral-type benzodiazepine receptor. Localization to the mitochondrial outer membrane. J. Biol. Chem. 1986, 261:576-583.
    • (1986) J. Biol. Chem. , vol.261 , pp. 576-583
    • Anholt, R.R.1
  • 2
    • 0023713397 scopus 로고
    • Molecular characterization and mitochondrial density of a recognition site for peripheral-type benzodiazepine ligands
    • Antkiewicz-Michaluk L., et al. Molecular characterization and mitochondrial density of a recognition site for peripheral-type benzodiazepine ligands. Mol. Pharmacol. 1988, 34:272-278.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 272-278
    • Antkiewicz-Michaluk, L.1
  • 3
    • 0021340209 scopus 로고
    • In vivo labelling in several rat tissues of 'peripheral type' benzodiazepine binding sites
    • Benavides J., et al. In vivo labelling in several rat tissues of 'peripheral type' benzodiazepine binding sites. Eur. J. Pharmacol. 1984, 99:1-7.
    • (1984) Eur. J. Pharmacol. , vol.99 , pp. 1-7
    • Benavides, J.1
  • 4
    • 0031031675 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis
    • Papadopoulos V., et al. Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis. Steroids 1997, 62:21-28.
    • (1997) Steroids , vol.62 , pp. 21-28
    • Papadopoulos, V.1
  • 5
    • 0021992304 scopus 로고
    • Depletion of peripheral-type benzodiazepine receptors after hypophysectomy in rat adrenal gland and testis
    • Anholt R.R., et al. Depletion of peripheral-type benzodiazepine receptors after hypophysectomy in rat adrenal gland and testis. Eur. J. Pharmacol. 1985, 110:41-46.
    • (1985) Eur. J. Pharmacol. , vol.110 , pp. 41-46
    • Anholt, R.R.1
  • 6
    • 0026649978 scopus 로고
    • Pregnenolone biosynthesis in C6-2B glioma cell mitochondria: regulation by a mitochondrial diazepam binding inhibitor receptor
    • Papadopoulos V., et al. Pregnenolone biosynthesis in C6-2B glioma cell mitochondria: regulation by a mitochondrial diazepam binding inhibitor receptor. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:5113-5117.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5113-5117
    • Papadopoulos, V.1
  • 7
    • 0026051933 scopus 로고
    • Diazepam binding inhibitor and its processing products stimulate mitochondrial steroid biosynthesis via an interaction with mitochondrial benzodiazepine receptors
    • Papadopoulos V., et al. Diazepam binding inhibitor and its processing products stimulate mitochondrial steroid biosynthesis via an interaction with mitochondrial benzodiazepine receptors. Endocrinology 1991, 129:1481-1488.
    • (1991) Endocrinology , vol.129 , pp. 1481-1488
    • Papadopoulos, V.1
  • 8
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li H., Papadopoulos V. Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 1998, 139:4991-4997.
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 9
    • 0032707529 scopus 로고    scopus 로고
    • Enigma of the peripheral benzodiazepine receptor
    • Gavish M., et al. Enigma of the peripheral benzodiazepine receptor. Pharmacol. Rev. 1999, 51:629-650.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 629-650
    • Gavish, M.1
  • 10
    • 33746035655 scopus 로고    scopus 로고
    • Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function
    • Papadopoulos V., et al. Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function. Trends Pharmacol. Sci. 2006, 27:402-409.
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 402-409
    • Papadopoulos, V.1
  • 11
    • 84912016664 scopus 로고    scopus 로고
    • The 18kDa translocator protein, microglia and neuroinflammation
    • Liu G.J., et al. The 18kDa translocator protein, microglia and neuroinflammation. Brain Pathol. 2014, 24:631-653.
    • (2014) Brain Pathol. , vol.24 , pp. 631-653
    • Liu, G.J.1
  • 12
    • 0030977125 scopus 로고    scopus 로고
    • A mammalian mitochondrial drug receptor functions as a bacterial "oxygen" sensor
    • Yeliseev A.A., et al. A mammalian mitochondrial drug receptor functions as a bacterial "oxygen" sensor. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:5101-5106.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 5101-5106
    • Yeliseev, A.A.1
  • 13
    • 78649687576 scopus 로고    scopus 로고
    • Translocator protein (18kDa) (TSPO) as a therapeutic target for neurological and psychiatric disorders
    • Rupprecht R., et al. Translocator protein (18kDa) (TSPO) as a therapeutic target for neurological and psychiatric disorders. Nat. Rev. Drug Discov. 2010, 9:971-988.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 971-988
    • Rupprecht, R.1
  • 14
    • 84894170581 scopus 로고    scopus 로고
    • Translocator protein 18kDa (TSPO) is regulated in white and brown adipose tissue by obesity
    • Thompson M.M., et al. Translocator protein 18kDa (TSPO) is regulated in white and brown adipose tissue by obesity. PLoS ONE 2013, 8:e79980.
    • (2013) PLoS ONE , vol.8 , pp. e79980
    • Thompson, M.M.1
  • 15
    • 0030916343 scopus 로고    scopus 로고
    • 3H]PK11195 binding to activated microglia
    • 3H]PK11195 binding to activated microglia. J. Neurocytol. 1997, 26:77-82.
    • (1997) J. Neurocytol. , vol.26 , pp. 77-82
    • Banati, R.B.1
  • 16
    • 0020576925 scopus 로고
    • Peripheral benzodiazepine binding sites: effect of PK 11195, 1-(2-chlorophenyl)-N-methyl-N-(1-methylpropyl)-3-isoquinolinecarboxamide. I. In vitro studies
    • Le Fur G., et al. Peripheral benzodiazepine binding sites: effect of PK 11195, 1-(2-chlorophenyl)-N-methyl-N-(1-methylpropyl)-3-isoquinolinecarboxamide. I. In vitro studies. Life Sci. 1983, 32:1839-1847.
    • (1983) Life Sci. , vol.32 , pp. 1839-1847
    • Le Fur, G.1
  • 17
    • 84923241444 scopus 로고    scopus 로고
    • Positron emission tomography and functional characterization of a complete PBR/TSPO knockout
    • Banati R.B., et al. Positron emission tomography and functional characterization of a complete PBR/TSPO knockout. Nat. Commun. 2014, 5:5452.
    • (2014) Nat. Commun. , vol.5 , pp. 5452
    • Banati, R.B.1
  • 18
    • 84878704476 scopus 로고    scopus 로고
    • A TSPO ligand is protective in a mouse model of multiple sclerosis
    • Daugherty D.J., et al. A TSPO ligand is protective in a mouse model of multiple sclerosis. EMBO Mol. Med. 2013, 5:891-903.
    • (2013) EMBO Mol. Med. , vol.5 , pp. 891-903
    • Daugherty, D.J.1
  • 19
    • 84877753769 scopus 로고    scopus 로고
    • Ligand for translocator protein reverses pathology in a mouse model of Alzheimer's disease
    • Barron A.M., et al. Ligand for translocator protein reverses pathology in a mouse model of Alzheimer's disease. J. Neurosci. 2013, 33:8891-8897.
    • (2013) J. Neurosci. , vol.33 , pp. 8891-8897
    • Barron, A.M.1
  • 20
    • 66349100806 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor antagonist is effective in relieving neuropathic pain in mice
    • Kondo D., et al. Peripheral-type benzodiazepine receptor antagonist is effective in relieving neuropathic pain in mice. J. Pharmacol. Sci. 2009, 110:55-63.
    • (2009) J. Pharmacol. Sci. , vol.110 , pp. 55-63
    • Kondo, D.1
  • 21
    • 0036494315 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor ligands reverse apoptosis resistance of cancer cells in vitro and in vivo
    • Decaudin D., et al. Peripheral benzodiazepine receptor ligands reverse apoptosis resistance of cancer cells in vitro and in vivo. Cancer Res. 2002, 62:1388-1393.
    • (2002) Cancer Res. , vol.62 , pp. 1388-1393
    • Decaudin, D.1
  • 22
    • 0037183733 scopus 로고    scopus 로고
    • Involvement of the peripheral benzodiazepine receptor in the development of rheumatoid arthritis in Mrl/lpr mice
    • Bribes E., et al. Involvement of the peripheral benzodiazepine receptor in the development of rheumatoid arthritis in Mrl/lpr mice. Eur. J. Pharmacol. 2002, 452:111-122.
    • (2002) Eur. J. Pharmacol. , vol.452 , pp. 111-122
    • Bribes, E.1
  • 23
    • 84872681212 scopus 로고    scopus 로고
    • Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism
    • Gut P., et al. Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism. Nat. Chem. Biol. 2013, 9:97-104.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 97-104
    • Gut, P.1
  • 24
    • 34548861265 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor-induced myocardial protection is mediated by inhibition of mitochondrial membrane permeabilization
    • Obame F.N., et al. Peripheral benzodiazepine receptor-induced myocardial protection is mediated by inhibition of mitochondrial membrane permeabilization. J. Pharmacol. Exp. Ther. 2007, 323:336-345.
    • (2007) J. Pharmacol. Exp. Ther. , vol.323 , pp. 336-345
    • Obame, F.N.1
  • 25
    • 67651117272 scopus 로고    scopus 로고
    • Translocator protein (18kD) as target for anxiolytics without benzodiazepine-like side effects
    • Rupprecht R., et al. Translocator protein (18kD) as target for anxiolytics without benzodiazepine-like side effects. Science 2009, 325:490-493.
    • (2009) Science , vol.325 , pp. 490-493
    • Rupprecht, R.1
  • 26
    • 84860279460 scopus 로고    scopus 로고
    • The role of 18kDa mitochondrial translocator protein (TSPO) in programmed cell death, and effects of steroids on TSPO expression
    • Veenman L., Gavish M. The role of 18kDa mitochondrial translocator protein (TSPO) in programmed cell death, and effects of steroids on TSPO expression. Curr. Mol. Med. 2012, 12:398-412.
    • (2012) Curr. Mol. Med. , vol.12 , pp. 398-412
    • Veenman, L.1    Gavish, M.2
  • 27
    • 84901008605 scopus 로고    scopus 로고
    • Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (translocator protein of 18kDa (TSPO))
    • Sileikyte J., et al. Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (translocator protein of 18kDa (TSPO)). J. Biol. Chem. 2014, 289:13769-13781.
    • (2014) J. Biol. Chem. , vol.289 , pp. 13769-13781
    • Sileikyte, J.1
  • 28
    • 84907293074 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis
    • Tu L.N., et al. Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis. J. Biol. Chem. 2014, 289:27444-27454.
    • (2014) J. Biol. Chem. , vol.289 , pp. 27444-27454
    • Tu, L.N.1
  • 29
    • 84891379545 scopus 로고    scopus 로고
    • Translocator protein/peripheral benzodiazepine receptor is not required for steroid hormone biosynthesis
    • Morohaku K., et al. Translocator protein/peripheral benzodiazepine receptor is not required for steroid hormone biosynthesis. Endocrinology 2014, 155:89-97.
    • (2014) Endocrinology , vol.155 , pp. 89-97
    • Morohaku, K.1
  • 30
    • 84923870787 scopus 로고    scopus 로고
    • PK11195 effect on steroidogenesis is not mediated through the translocator protein (TSPO)
    • Tu L.N., et al. PK11195 effect on steroidogenesis is not mediated through the translocator protein (TSPO). Endocrinology 2014, 156:1033-1039.
    • (2014) Endocrinology , vol.156 , pp. 1033-1039
    • Tu, L.N.1
  • 31
    • 0024408795 scopus 로고
    • Molecular cloning and expression of cDNA encoding a peripheral-type benzodiazepine receptor
    • Sprengel R., et al. Molecular cloning and expression of cDNA encoding a peripheral-type benzodiazepine receptor. J. Biol. Chem. 1989, 264:20415-20421.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20415-20421
    • Sprengel, R.1
  • 32
    • 0031893596 scopus 로고    scopus 로고
    • Topological analysis of the peripheral benzodiazepine receptor in yeast mitochondrial membranes supports a five-transmembrane structure
    • Joseph-Liauzun E., et al. Topological analysis of the peripheral benzodiazepine receptor in yeast mitochondrial membranes supports a five-transmembrane structure. J. Biol. Chem. 1998, 273:2146-2152.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2146-2152
    • Joseph-Liauzun, E.1
  • 33
    • 43849100475 scopus 로고    scopus 로고
    • 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
    • Murail S., 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 2008, 1778:1375-1381.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1375-1381
    • Murail, S.1
  • 34
    • 84872841358 scopus 로고    scopus 로고
    • Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein
    • Galvagnion C., et al. Production and initial structural characterization of the TM4TM5 helix-loop-helix domain of the translocator protein. J. Pept. Sci. 2013, 19:102-109.
    • (2013) J. Pept. Sci. , vol.19 , pp. 102-109
    • Galvagnion, C.1
  • 35
    • 77953560009 scopus 로고    scopus 로고
    • Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals
    • Korkhov V.M., et al. Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals. Structure 2010, 18:677-687.
    • (2010) Structure , vol.18 , pp. 677-687
    • Korkhov, V.M.1
  • 36
    • 84883234112 scopus 로고    scopus 로고
    • Characterization and modeling of the oligomeric state and ligand binding behavior of purified translocator protein 18kDa from Rhodobacter sphaeroides
    • Li F., et al. Characterization and modeling of the oligomeric state and ligand binding behavior of purified translocator protein 18kDa from Rhodobacter sphaeroides. Biochemistry 2013, 52:5884-5899.
    • (2013) Biochemistry , vol.52 , pp. 5884-5899
    • Li, F.1
  • 37
    • 84896998596 scopus 로고    scopus 로고
    • Structure of the mitochondrial translocator protein in complex with a diagnostic ligand
    • Jaremko L., et al. Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science 2014, 343:1363-1366.
    • (2014) Science , vol.343 , pp. 1363-1366
    • Jaremko, L.1
  • 38
    • 84921829870 scopus 로고    scopus 로고
    • Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism
    • Li F., et al. Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism. Science 2015, 347:555-558.
    • (2015) Science , vol.347 , pp. 555-558
    • Li, F.1
  • 39
    • 79851473610 scopus 로고    scopus 로고
    • Mixed-affinity binding in humans with 18-kDa translocator protein ligands
    • Owen D.R., et al. Mixed-affinity binding in humans with 18-kDa translocator protein ligands. J. Nucl. Med. 2011, 52:24-32.
    • (2011) J. Nucl. Med. , vol.52 , pp. 24-32
    • Owen, D.R.1
  • 40
    • 84921931701 scopus 로고    scopus 로고
    • Protein structure. Structure and activity of tryptophan-rich TSPO proteins
    • Guo Y., et al. Protein structure. Structure and activity of tryptophan-rich TSPO proteins. Science 2015, 347:551-555.
    • (2015) Science , vol.347 , pp. 551-555
    • Guo, Y.1
  • 41
    • 0034815369 scopus 로고    scopus 로고
    • Structural and functional study of reconstituted peripheral benzodiazepine receptor
    • Lacapere J.J., et al. Structural and functional study of reconstituted peripheral benzodiazepine receptor. Biochem. Biophys. Res. Commun. 2001, 284:536-541.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 536-541
    • Lacapere, J.J.1
  • 42
    • 0035970108 scopus 로고    scopus 로고
    • 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
    • Li H., 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. U.S.A. 2001, 98:1267-1272.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1267-1272
    • Li, H.1
  • 43
    • 20044376658 scopus 로고    scopus 로고
    • Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor
    • Jamin N., et al. Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor. Mol. Endocrinol. 2005, 19:588-594.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 588-594
    • Jamin, N.1
  • 44
    • 84906890554 scopus 로고    scopus 로고
    • Toward the functional oligomerization state of tryptophan-rich sensory proteins
    • Jaremko L., et al. Toward the functional oligomerization state of tryptophan-rich sensory proteins. Protein Sci. 2014, 23:1154-1160.
    • (2014) Protein Sci. , vol.23 , pp. 1154-1160
    • Jaremko, L.1
  • 45
    • 84914689510 scopus 로고    scopus 로고
    • Construction and validation of an atomic model for bacterial TSPO from electron microscopy density, evolutionary constraints, and biochemical and biophysical data
    • Hinsen K., et al. Construction and validation of an atomic model for bacterial TSPO from electron microscopy density, evolutionary constraints, and biochemical and biophysical data. Biochim. Biophys. Acta 2015, 1848:568-580.
    • (2015) Biochim. Biophys. Acta , vol.1848 , pp. 568-580
    • Hinsen, K.1
  • 46
    • 0037461325 scopus 로고    scopus 로고
    • In vivo and in vitro peripheral-type benzodiazepine receptor polymerization: functional significance in drug ligand and cholesterol binding
    • Delavoie F., et al. In vivo and in vitro peripheral-type benzodiazepine receptor polymerization: functional significance in drug ligand and cholesterol binding. Biochemistry 2003, 42:4506-4519.
    • (2003) Biochemistry , vol.42 , pp. 4506-4519
    • Delavoie, F.1
  • 47
    • 84937524245 scopus 로고    scopus 로고
    • The changing landscape in translocator protein (TSPO) function
    • Selvaraj V., Stocco D.M. The changing landscape in translocator protein (TSPO) function. Trends Endocrinol. Metab. 2015, 26:341-348.
    • (2015) Trends Endocrinol. Metab. , vol.26 , pp. 341-348
    • Selvaraj, V.1    Stocco, D.M.2
  • 48
    • 78651385379 scopus 로고    scopus 로고
    • Regulation of the inner membrane mitochondrial permeability transition by the outer membrane translocator protein (peripheral benzodiazepine receptor)
    • Sileikyte J., et al. Regulation of the inner membrane mitochondrial permeability transition by the outer membrane translocator protein (peripheral benzodiazepine receptor). J. Biol. Chem. 2011, 286:1046-1053.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1046-1053
    • Sileikyte, J.1
  • 49
    • 0024853180 scopus 로고
    • Mitochondrial benzodiazepine receptors regulate steroid biosynthesis
    • Mukhin A.G., et al. Mitochondrial benzodiazepine receptors regulate steroid biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 1989, 86:9813-9816.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9813-9816
    • Mukhin, A.G.1
  • 50
    • 0024503813 scopus 로고
    • Testicular interstitial cells as targets for peripheral benzodiazepines
    • Ritta M.N., Calandra R.S. Testicular interstitial cells as targets for peripheral benzodiazepines. Neuroendocrinology 1989, 49:262-266.
    • (1989) Neuroendocrinology , vol.49 , pp. 262-266
    • Ritta, M.N.1    Calandra, R.S.2
  • 51
    • 84891469290 scopus 로고    scopus 로고
    • On the role of the translocator protein (18-kDa) TSPO in steroid hormone biosynthesis
    • Papadopoulos V. On the role of the translocator protein (18-kDa) TSPO in steroid hormone biosynthesis. Endocrinology 2014, 155:15-20.
    • (2014) Endocrinology , vol.155 , pp. 15-20
    • Papadopoulos, V.1
  • 52
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • Hirschey M.D., et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 2010, 464:121-125.
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1
  • 53
    • 84898012702 scopus 로고    scopus 로고
    • Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases
    • Wagner G.R., Hirschey M.D. Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases. Mol. Cell 2014, 54:5-16.
    • (2014) Mol. Cell , vol.54 , pp. 5-16
    • Wagner, G.R.1    Hirschey, M.D.2
  • 54
    • 84865421953 scopus 로고    scopus 로고
    • Mitochondrial sirtuins: regulators of protein acylation and metabolism
    • He W., et al. Mitochondrial sirtuins: regulators of protein acylation and metabolism. Trends Endocrinol. Metab. 2012, 23:467-476.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 467-476
    • He, W.1
  • 55
    • 84901639801 scopus 로고    scopus 로고
    • Parkin and PINK1: much more than mitophagy
    • Scarffe L.A., et al. Parkin and PINK1: much more than mitophagy. Trends Neurosci. 2014, 37:315-324.
    • (2014) Trends Neurosci. , vol.37 , pp. 315-324
    • Scarffe, L.A.1
  • 56
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier C.A., et al. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:11364-11369.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11364-11369
    • Gautier, C.A.1
  • 57
    • 84895904175 scopus 로고    scopus 로고
    • Enhancing nucleotide metabolism protects against mitochondrial dysfunction and neurodegeneration in a PINK1 model of Parkinson's disease
    • Tufi R., et al. Enhancing nucleotide metabolism protects against mitochondrial dysfunction and neurodegeneration in a PINK1 model of Parkinson's disease. Nat. Cell Biol. 2014, 16:157-166.
    • (2014) Nat. Cell Biol. , vol.16 , pp. 157-166
    • Tufi, R.1
  • 58
    • 77953666105 scopus 로고    scopus 로고
    • Genetic animal models of Parkinson's disease
    • Dawson T.M., et al. Genetic animal models of Parkinson's disease. Neuron 2010, 66:646-661.
    • (2010) Neuron , vol.66 , pp. 646-661
    • Dawson, T.M.1
  • 59
    • 84883492814 scopus 로고    scopus 로고
    • Parkin- and PINK1-dependent mitophagy in neurons: will the real pathway please stand up?
    • Grenier K., et al. Parkin- and PINK1-dependent mitophagy in neurons: will the real pathway please stand up?. Front. Neurol. 2013, 4:100.
    • (2013) Front. Neurol. , vol.4 , pp. 100
    • Grenier, K.1
  • 60
    • 84922177703 scopus 로고    scopus 로고
    • TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control
    • Gatliff J., et al. TSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control. Autophagy 2014, 10:2279-2296.
    • (2014) Autophagy , vol.10 , pp. 2279-2296
    • Gatliff, J.1
  • 61
    • 84869051280 scopus 로고    scopus 로고
    • Mitochondrial disorders as windows into an ancient organelle
    • Vafai S.B., Mootha V.K. Mitochondrial disorders as windows into an ancient organelle. Nature 2012, 491:374-383.
    • (2012) Nature , vol.491 , pp. 374-383
    • Vafai, S.B.1    Mootha, V.K.2
  • 62
    • 0024497217 scopus 로고
    • Mitochondrial benzodiazepine receptors mediate inhibition of mitochondrial respiratory control
    • Hirsch J.D., et al. Mitochondrial benzodiazepine receptors mediate inhibition of mitochondrial respiratory control. Mol. Pharmacol. 1989, 35:157-163.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 157-163
    • Hirsch, J.D.1
  • 63
    • 33847035458 scopus 로고    scopus 로고
    • 0-ATPase by ligands of the peripheral benzodiazepine receptor
    • 0-ATPase by ligands of the peripheral benzodiazepine receptor. Bioorg. Med. Chem. Lett. 2007, 17:1667-1670.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1667-1670
    • Cleary, J.1
  • 64
    • 84860303350 scopus 로고    scopus 로고
    • 0-ATP synthase in Bcl-2 knock-down cells
    • 0-ATP synthase in Bcl-2 knock-down cells. Curr. Mol. Med. 2012, 12:476-482.
    • (2012) Curr. Mol. Med. , vol.12 , pp. 476-482
    • Seneviratne, M.S.1
  • 65
    • 84901463419 scopus 로고    scopus 로고
    • Genetic analysis of dTSPO, an outer mitochondrial membrane protein, reveals its functions in apoptosis, longevity, and Ab42-induced neurodegeneration
    • Lin R., et al. Genetic analysis of dTSPO, an outer mitochondrial membrane protein, reveals its functions in apoptosis, longevity, and Ab42-induced neurodegeneration. Aging Cell 2014, 13:507-518.
    • (2014) Aging Cell , vol.13 , pp. 507-518
    • Lin, R.1
  • 66
    • 84865169609 scopus 로고    scopus 로고
    • Metabolic pathway alterations that support cell proliferation
    • Vander Heiden M.G., et al. Metabolic pathway alterations that support cell proliferation. Cold Spring Harb. Symp. Quant. Biol. 2011, 76:325-334.
    • (2011) Cold Spring Harb. Symp. Quant. Biol. , vol.76 , pp. 325-334
    • Vander Heiden, M.G.1
  • 67
    • 84856442945 scopus 로고    scopus 로고
    • A guide to analysis of mouse energy metabolism
    • Tschop M.H., et al. A guide to analysis of mouse energy metabolism. Nat. Methods 2012, 9:57-63.
    • (2012) Nat. Methods , vol.9 , pp. 57-63
    • Tschop, M.H.1
  • 68
    • 72749091047 scopus 로고    scopus 로고
    • Translocator protein (18kDa) is involved in primitive erythropoiesis in zebrafish
    • Rampon C., et al. Translocator protein (18kDa) is involved in primitive erythropoiesis in zebrafish. FASEB J. 2009, 23:4181-4192.
    • (2009) FASEB J. , vol.23 , pp. 4181-4192
    • Rampon, C.1
  • 69
    • 84878322623 scopus 로고    scopus 로고
    • Chemical catalysis by the translocator protein (18kDa)
    • Ginter C., et al. Chemical catalysis by the translocator protein (18kDa). Biochemistry 2013, 52:3609-3611.
    • (2013) Biochemistry , vol.52 , pp. 3609-3611
    • Ginter, C.1
  • 70
    • 56449113261 scopus 로고    scopus 로고
    • An ancient evolutionary origin of genes associated with human genetic diseases
    • Domazet-Loso T., Tautz D. An ancient evolutionary origin of genes associated with human genetic diseases. Mol. Biol. Evol. 2008, 25:2699-2707.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2699-2707
    • Domazet-Loso, T.1    Tautz, D.2
  • 71
    • 80855134313 scopus 로고    scopus 로고
    • Defining the role of essential genes in human disease
    • Dickerson J.E., et al. Defining the role of essential genes in human disease. PLoS ONE 2011, 6:e27368.
    • (2011) PLoS ONE , vol.6 , pp. e27368
    • Dickerson, J.E.1
  • 72
    • 32144444135 scopus 로고    scopus 로고
    • Highly consistent patterns for inherited human diseases at the molecular level
    • Lopez-Bigas N., et al. Highly consistent patterns for inherited human diseases at the molecular level. Bioinformatics 2006, 22:269-277.
    • (2006) Bioinformatics , vol.22 , pp. 269-277
    • Lopez-Bigas, N.1
  • 73
    • 84886294241 scopus 로고    scopus 로고
    • How old is my gene?
    • Capra J.A., et al. How old is my gene?. Trends Genet. 2013, 29:659-668.
    • (2013) Trends Genet. , vol.29 , pp. 659-668
    • Capra, J.A.1
  • 74
    • 84855340957 scopus 로고    scopus 로고
    • An 18-kDa translocator protein (TSPO) polymorphism explains differences in binding affinity of the PET radioligand PBR28
    • Owen D.R., et al. An 18-kDa translocator protein (TSPO) polymorphism explains differences in binding affinity of the PET radioligand PBR28. J. Cereb. Blood Flow Metab. 2012, 32:1-5.
    • (2012) J. Cereb. Blood Flow Metab. , vol.32 , pp. 1-5
    • Owen, D.R.1
  • 75
    • 84886102268 scopus 로고    scopus 로고
    • Bipolar disorder is associated with the rs6971 polymorphism in the gene encoding 18kDa translocator protein (TSPO)
    • Colasanti A., et al. Bipolar disorder is associated with the rs6971 polymorphism in the gene encoding 18kDa translocator protein (TSPO). Psychoneuroendocrinology 2013, 38:2826-2829.
    • (2013) Psychoneuroendocrinology , vol.38 , pp. 2826-2829
    • Colasanti, A.1
  • 76
    • 84912001146 scopus 로고    scopus 로고
    • Emergent properties of microglia
    • Svahn A.J., et al. Emergent properties of microglia. Brain Pathol. 2014, 24:665-670.
    • (2014) Brain Pathol. , vol.24 , pp. 665-670
    • Svahn, A.J.1
  • 77
    • 84912029813 scopus 로고    scopus 로고
    • Neuroinflammation: no rose by any other name
    • Graeber M.B. Neuroinflammation: no rose by any other name. Brain Pathol. 2014, 24:620-622.
    • (2014) Brain Pathol. , vol.24 , pp. 620-622
    • Graeber, M.B.1
  • 78
    • 0027333450 scopus 로고
    • A 3D model of the peripheral benzodiazepine receptor and its implication in intra mitochondrial cholesterol transport
    • 235
    • Bernassau J.M., et al. A 3D model of the peripheral benzodiazepine receptor and its implication in intra mitochondrial cholesterol transport. J. Mol. Graph. 1993, 11:236-244. 235.
    • (1993) J. Mol. Graph. , vol.11 , pp. 236-244
    • Bernassau, J.M.1
  • 79
    • 84886812954 scopus 로고    scopus 로고
    • The nexus of chromatin regulation and intermediary metabolism
    • Gut P., Verdin E. The nexus of chromatin regulation and intermediary metabolism. Nature 2013, 502:489-498.
    • (2013) Nature , vol.502 , pp. 489-498
    • Gut, P.1    Verdin, E.2
  • 80
    • 70349142240 scopus 로고    scopus 로고
    • Negative feedback maintenance of heme homeostasis by its receptor, Rev-erbα
    • Wu N., et al. Negative feedback maintenance of heme homeostasis by its receptor, Rev-erbα. Genes Dev. 2009, 23:2201-2209.
    • (2009) Genes Dev. , vol.23 , pp. 2201-2209
    • Wu, N.1
  • 81
    • 37249086610 scopus 로고    scopus 로고
    • Rev-erbα, a heme sensor that coordinates metabolic and circadian pathways
    • Yin L., et al. Rev-erbα, a heme sensor that coordinates metabolic and circadian pathways. Science 2007, 318:1786-1789.
    • (2007) Science , vol.318 , pp. 1786-1789
    • Yin, L.1
  • 82
    • 23944476164 scopus 로고    scopus 로고
    • Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α
    • Handschin C., et al. Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α. Cell 2005, 122:505-515.
    • (2005) Cell , vol.122 , pp. 505-515
    • Handschin, C.1
  • 83
    • 76049093949 scopus 로고    scopus 로고
    • PGC-1α negatively regulates hepatic FGF21 expression by modulating the heme/Rev-Erbα axis
    • Estall J.L., et al. PGC-1α negatively regulates hepatic FGF21 expression by modulating the heme/Rev-Erbα axis. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:22510-22515.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 22510-22515
    • Estall, J.L.1
  • 84
    • 0035906835 scopus 로고    scopus 로고
    • Bcl-2 resistant mitochondrial toxicity mediated by the isoquinoline carboxamide PK11195 involves de novo generation of reactive oxygen species
    • Fennell D.A., et al. Bcl-2 resistant mitochondrial toxicity mediated by the isoquinoline carboxamide PK11195 involves de novo generation of reactive oxygen species. Br. J. Cancer 2001, 84:1397-1404.
    • (2001) Br. J. Cancer , vol.84 , pp. 1397-1404
    • Fennell, D.A.1


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