The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Peripheral-Type Benzodiazepine Receptor Function in Cholesterol Transport. Identification of a Putative Cholesterol Recognition/Interaction Amino Acid Sequence and Consensus Pattern1
Abstract
In steroid-synthesizing cells, like the MA-10 mouse tumor Leydig cells, the peripheral-type benzodiazepine receptor (PBR) is an outer mitochondrial membrane protein involved in the regulation of cholesterol transport from the outer to the inner mitochondrial membrane, the rate-determining step in steroid biosynthesis. Expression of PBR in Escherichia coli DE3 cells, which have no PBR, no cholesterol, and do not make steroids, induced the ability to take up cholesterol in a time-dependent, temperature-sensitive, and energy- independent manner. These cells took up no other steroids tested. Addition of the high affinity PBR ligand PK 11195 to cholesterol-loaded membranes, obtained from cells transfected with PBR, resulted in the release of the uptaken cholesterol. Expression in DE3 cells of mutant PBRs demonstrated that deletions in the cytoplasmic carboxy-terminus dramatically reduced the cholesterol uptake function of PBR, although it retained full capacity to bind PK 11195. Site-directed mutagenesis in the carboxy-terminal region of PBR demonstrated that bacteria expressing the mutant PBR proteins PBR(Y153S) and PBR(R156L) do not accumulate cholesterol, suggesting that amino acids Y153 and R156 are involved in the interaction of the receptor with cholesterol. Considering these results, we postulate the existence of a common cholesterol recognition/interaction amino acid consensus pattern (–L/V-(X)1–5-Y-(X)1–5-R/K-). Indeed, we found this amino acid consensus pattern in all proteins shown to interact with cholesterol. In conclusion, these data suggest that the expression of PBR confers the ability to take up and release, upon ligand activation, cholesterol. Considering the widespread occurrence of this protein and its tissue and cell specific subcellular localization, these results suggest a more general role of PBR in intracellular cholesterol transport and compartmentalization.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
TSPO contains an evolutionarily conserved C-terminal CRAC motif that facilitates cholesterol binding through a conserved tyrosine residue.
“TSPO does contain an evolutionarily conserved C-terminal cholesterol recognition amino acid concensus (CRAC) motif (117, 118), which has been shown to facilitate cholesterol binding through a conserved tyrosine residue (119).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [117]
Citations
Cites
The publisher hasn’t deposited this paper’s reference list.
Cited by
Sorted by citations
Rupprecht, R., Papadopoulos, V., Rammes, G., Baghai, T. C., Fan, J., Akula, N., Groyer, G., Adams, D., & Schumacher, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3295 · Cited by 930
Self-citationEnigma of the peripheral benzodiazepine receptor
Gavish, M., Bachman, I., Shoukrun, R., Katz, Y., Veenman, L., Weisinger, G., & Weizman, A. (1999) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01424-8 · Cited by 512
Compositional, technological and nutritional aspects of dromedary camel milk
haj, O. A. A., & Alkanhal, H. A. (2010) · International Dairy Journal · doi:10.1016/j.idairyj.2010.04.003 · Cited by 487
Lacapère, J.-J., & Papadopoulos, V. (2003) · Steroids · doi:10.1016/s0039-128x(03)00101-6 · Cited by 342
Self-citationLi, H., Yao, Z.-X., Degenhardt, B., Teper, G., & Papadopoulos, V. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1267 · Cited by 317
Self-citationCholesterol and the interaction of proteins with membrane domains
Epand, R. M. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2006.02.001 · Cited by 317
Hauet, T., Yao, Z.-X., Bose, H. S., Wall, C. T., Han, Z., Li, W., Hales, D. B., Miller, W. L., Culty, M., & Papadopoulos, V. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0307 · Cited by 252
Self-citationTu, L. N., Morohaku, K., Manna, P. R., Pelton, S. H., Butler, W. R., Stocco, D. M., & Selvaraj, V. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.578286 · Cited by 239
Papadopoulos, V., Lecanu, L., Brown, R. C., Han, Z., & Yao, Z. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.05.063 · Cited by 235
Self-citationTSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality control
Gatliff, J., East, D., Crosby, J., Abeti, R., Harvey, R., Craigen, W., Parker, P., & Campanella, M. (2014) · Autophagy · doi:10.4161/15548627.2014.991665 · Cited by 215
Wang, M., Wang, X., Zhao, L., Ma, W., Rodríguez, I. R., Fariss, R. N., & Wong, W. T. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3153-13.2014 · Cited by 211
Membrane Cholesterol in the Function and Organization of G-Protein Coupled Receptors
Paila, Y. D., & Chattopadhyay, A. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-8622-8_16 · Cited by 195
Specificity of Intramembrane Protein-Lipid InteractionsPreprint
Contreras, F. ‐., Ernst, A. M., Wieland, F., & Brügger, B. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004705 · Cited by 167
Lipids and membrane microdomains in HIV-1 replication
Waheed, A. A., & Freed, E. O. (2009) · Virus Research · doi:10.1016/j.virusres.2009.04.007 · Cited by 173
Caveolin Scaffolding Region and Cholesterol-rich Domains in Membranes
Epand, R. M., Sayer, B. G., & Epand, R. F. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.064 · Cited by 161
Assanasen, C., Mineo, C., Seetharam, D., Yuhanna, I. S., Marcel, Y. L., Connelly, M. A., Williams, D. L., de la Llera-Moya, M., Shaul, P. W., & Silver, D. L. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23858 · Cited by 158
G-protein-coupled receptors, cholesterol and palmitoylation: facts about fats
Chini, B., & Parenti, M. D. (2009) · Journal of Molecular Endocrinology · doi:10.1677/jme-08-0114 · Cited by 146
In vitro studies on the role of the peripheral-type benzodiazepine receptor in steroidogenesis
Culty, M., Li, H., Boujrad, N., Amri, H., Vidic, B., Bernassau, J. M., Reversat, J. L., & Papadopoulos, V (1999) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(99)00056-4 · Cited by 122
Self-citationCurrent knowledge on the acute regulation of steroidogenesis
Selvaraj, V., Stocco, D. M., & Clark, B. J. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy102 · Cited by 118
Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies
Midzak, A., & Papadopoulos, V. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00106 · Cited by 114
Self-citationStructural basis for catalysis and substrate specificity of human ACAT1
Qian, H., Zhao, X., Yan, R., Yao, X., Gao, S., Sun, X., Du, X., Yang, H., Wong, C. C. L., & Yan, N. (2020) · Nature · doi:10.1038/s41586-020-2290-0 · Cited by 108
Scuron, M. D., Boesze‐Battaglia, K., Dlakić, M., & Shenker, B. J. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00168 · Cited by 93
Chapter 4 The Biology of Caveolae
Parat, M. (2009) · International review of cytology · doi:10.1016/s1937-6448(08)01804-2 · Cited by 87
Liu, J., Li, H., & Papadopoulos, V. (2003) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(03)00213-9 · Cited by 79
Self-citationLuo, C., Wang, K., Liu, D., Li, Y., & Zhao, Q.-S. (2008) · Cellular and Molecular Immunology · doi:10.1038/cmi.2008.1 · Cited by 70
Midzak, A., Akula, N., Lecanu, L., & Papadopoulos, V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203216 · Cited by 69
Self-citationCosta, B., Pini, S., Gabelloni, P., Da Pozzo, E., Abelli, M., Lari, L., Preve, M., Lucacchini, A., Cassano, G. B., & Martini, C. (2009) · Endocrinology · doi:10.1210/en.2009-0752 · Cited by 68
Allosteric modulation of the adenosine A2A receptor by cholesterol
Huang, S. K., Almurad, O., Pejana, R. J., Morrison, Z. A., Pandey, A. N., Picard, L.-P., Nitz, M., Sljoka, A., & Prosser, R. S. (2021) · eLife · doi:10.7554/elife.73901 · Cited by 60
Lai, C.-K., Chen, Y., Lin, C., Lin, H., Kao, M.-C., Huang, M.-Z., Lin, Y.-H., Chiang-Ni, C., Chen, C., Lo, U., et al. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00009 · Cited by 59
Colasanti, A., Owen, D. R., Grozeva, D., Rabiner, E. A., Matthews, P. M., Craddock, N., & Young, A. H. (2013) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2013.07.007 · Cited by 55
Role of Mitochondria in Steroidogenesis
Miller, W. L. (2011) · Endocrine Development · doi:10.1159/000321204 · Cited by 57
Structural insights into GIRK2 channel modulation by cholesterol and PIP2
Mathiharan, Y. K., Glaaser, I. W., Zhao, Y., Robertson, M. J., Skiniotis, G., & Slesinger, P. A. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109619 · Cited by 52
Role of the peripheral-type benzodiazepine receptor in adrenal and brain steroidogenesis
Brown, R. C., & Papadopoulos, V. (2001) · International review of neurobiology · doi:10.1016/s0074-7742(01)46061-2 · Cited by 51
Self-citationCorver, J., Broer, R., van Kasteren, P. B., & Spaan, W. J. M. (2009) · Virology Journal · doi:10.1186/1743-422x-6-230 · Cited by 50
Fan, J., & Papadopoulos, V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076701 · Cited by 48
Self-citationBalsemão-Pires, E., Jaillais, Y., Olson, B. J. S. C., de Andrade, L. R., Umen, J., Chory, J., & Sachetto‐Martins, G. (2011) · BMC Plant Biology · doi:10.1186/1471-2229-11-108 · Cited by 48
Auriac, A., Willemetz, A., & Canonne‐Hergaux, F. (2010) · Haematologica · doi:10.3324/haematol.2009.019992 · Cited by 47
Current status and future perspectives: TSPO in steroid neuroendocrinology
Selvaraj, V., & Tu, L. N. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0241 · Cited by 41
Vianello, R., Domene, C., & Mavri, J. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00327 · Cited by 39
Sphingolipid-Binding Domain in the Serotonin1A Receptor
Chattopadhyay, A., Paila, Y. D., Shrivastava, S. K., Tiwari, S., Singh, P., & Fantini, J. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3381-1_19 · Cited by 39
Alhaj, O. A., Kanekanian, A. D., Peters, A. C., & Tatham, A. S. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.04.061 · Cited by 39
Peripheral-Type Benzodiazepine Receptor
Cascio, C., Guarneri, P., Li, H., Brown, R. C., Amri, H., Boujrad, N., Kotoula, M. G., Vidić, B., Drieu, K., & Papadopoulos, V. (1999) · Humana Press eBooks · doi:10.1007/978-1-59259-693-5_5 · Cited by 39
Self-citationMidzak, A., & Papadopoulos, V. (2014) · Traffic · doi:10.1111/tra.12177 · Cited by 38
Self-citationA Journey of Cytolethal Distending Toxins through Cell Membranes
Boesze‐Battaglia, K., Alexander, D., Dlakić, M., & Shenker, B. J. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00081 · Cited by 36
Bélanger, M., Desjardins, P., Chatauret, N., Rose, C. F., & Butterworth, R. F. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2004.12.029 · Cited by 36
Cannarozzo, C., Fred, S. M., Girych, M., Biojone, C., Enkavi, G., Róg, T., Vattulainen, I., Casarotto, P. C., & Ċastrén, E. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15218 · Cited by 33
Jaipuria, G., Ukmar, T., & Zweckstetter, M. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2789-9 · Cited by 31
Interaction(s) of rotavirus non-structural protein 4 (NSP4) C-terminal peptides with model membranes
Huang, H., Schroeder, F., Estes, M. K., McPherson, T., & Ball, J. M. (2004) · Biochemical Journal · doi:10.1042/bj20031789 · Cited by 29
Gazouli, M., Han, Z. J., & Papadopoulos, V. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.039388 · Cited by 28
Self-citationSensitivity of cholecystokinin receptors to membrane cholesterol content
Desai, A. J., & Miller, L. J. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00123 · Cited by 25
Chong, H. S., Campbell, L. T., Padula, M. P., Hill, C. J., Harry, E. J., Li, S. S., Wilkins, M. R., Herbert, B. R., & Carter, D. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042835 · Cited by 25
Giatzakis, C., Batarseh, A., Dettin, L., & Papadopoulos, V. (2007) · Biochemistry · doi:10.1021/bi062208o · Cited by 24
Self-citationEvidence for a Mitochondrial Impact of Trimetazidine during Cold Ischemia and Reperfusion
Baumert, H., Faure, J., Zhang, K., Petit, I., Goujon, J. M., Dutheil, D., Favreau, F. D., Barrière, M., Tillement, J. P., Mauco, G., et al. (2004) · Pharmacology · doi:10.1159/000076259 · Cited by 23
Self-citationHachen, A., Jewgenow, K., & Braun, B. C. (2011) · Theriogenology · doi:10.1016/j.theriogenology.2011.08.029 · Cited by 22
Midzak, A. S., Akula, N., Rone, M. B., & Papadopoulos, V. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.023 · Cited by 20
Self-citationYu, W., Wang, E., Voll, R. J., Miller, A. H., & Goodman, M. M. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.04.046 · Cited by 21
Effects of peripheral-type benzodiazepine receptor ligands on Ehrlich tumor cell proliferation
Sakai, M., Fonseca, E. S. M., Oloris, S. C. S., Matsuzaki, P., Otake, A. H., Leite, K. R. M., Massoco, C. D. O., Dagli, M. L., & Palermo‐Neto, J. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.07.057 · Cited by 19
The peripheral-type benzodiazepine receptor and adrenal steroidogenesis
Amri, H., Li, H., Culty, M., Gaillard, J. L., Teper, G., & Papadopoulos, V. (1999) · Current Opinion in Endocrinology & Diabetes · doi:10.1097/00060793-199906000-00002 · Cited by 17
Self-citationMorgan, J., Oseroff, A. R., & Cheney, R. T. (2004) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2004.06198.x · Cited by 19
Bélanger, M., Ahboucha, S., Desjardins, P., & Butterworth, R. F. (2003) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(03)31044-6 · Cited by 14
NMR spectroscopy of basic/aromatic amino acid clusters in membrane proteins
Zhang, W., Sato, T., & Smith, S. O. (2006) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2006.04.002 · Cited by 15
Kiaa1024L/Minar2 is essential for hearing by regulating cholesterol distribution in hair bundles
Gao, G., Guo, S., Zhang, Q., Zhang, H., Zhang, C., & Peng, G. (2022) · eLife · doi:10.7554/elife.80865 · Cited by 13
Sędzik, J., & Jastrzebski, J. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22612 · Cited by 15
Dong, Q. G., & Hardy, M. P. (2004) · Humana Press eBooks · doi:10.1007/978-1-59259-727-7_2 · Cited by 14
Thornton, S. J., Wong, E. M., Lee, S. D., & Wasan, K. M. (2008) · Lipids in Health and Disease · doi:10.1186/1476-511x-7-21 · Cited by 12
Chen, Y., Hagopian, B., & Tan, S. (2025) · PLOS Pathogens · doi:10.1371/journal.ppat.1013207 · Cited by 11
Controlling the mitochondrial gatekeeper for effective chemotherapy
Fennell, D. A., & Cotter, F. E. (2000) · British Journal of Haematology · doi:10.1046/j.1365-2141.2000.02271.x · Cited by 11
Depletion of membrane cholesterol modifies structure, dynamic and activation of Nav1.7
Albani, S., Eswaran, V. S. B., Piergentili, A., Souza, P. C. T., Lampert, A., & Rossetti, G. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134219 · Cited by 10
Bacterial Overexpressed Membrane Proteins: An Example: The TSPO
Robert, J., & Lacapère, J.-J. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-762-4_3 · Cited by 8
Chetverikov, N., Randáková, A., Nelic, D., & Jakubík, J. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117296 · Cited by 7
Leneveu‐Jenvrin, C., Bouffartigues, E., Maillot, O., Cornélis, P., Feuilloley, M. G. J., Connil, N., & Chevalier, S. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01023 · Cited by 9
Welter, B. H., Walters, H. A., & Temesvari, L. A. (2020) · PLoS ONE · doi:10.1371/journal.pone.0219870 · Cited by 7
Interaction of RTX toxins with the host cell plasma membrane
Chacko, F. M., & Schmitt, L. (2023) · Biological Chemistry · doi:10.1515/hsz-2022-0336 · Cited by 5
Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity
Dergunov, A. D. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1619-5 · Cited by 5
Valdés, V. J., Athie, A., Salinas, L. S., Navarro, R. E., & Vaca, L. A. (2012) · PLoS ONE · doi:10.1371/annotation/5a203055-6c15-43b0-96ad-0fbd5eb9b810 · Cited by 5
Schroeder, C., & Lin, T.-I. (2007) · Springer eBooks · doi:10.1007/0-387-28146-0_9 · Cited by 4
The Role of Proteins in the Formation of Domains in Membranes
Epand, R. M. (2006) · Springer eBooks · doi:10.1007/3-540-28435-4_4 · Cited by 4
Peripheral benzodiazepine receptors
Guilarte, T. (2002) · CRC Press eBooks · doi:10.1201/9781420032208.ch28 · Cited by 3
Membrane-mediated ligand unbinding of the PK-11195 ligand from TSPOPreprint
Dixon, T., Uyar, A., Ferguson-Miller, S. M., & Dickson, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.21.914127 · Cited by 4
Cholesterol-Binding Peptides and Phagocytosis
Dunina-Barkovskaya, A. Y. (2012) · InTech eBooks · doi:10.5772/38255 · Cited by 2
Bombalska, A., & Graczyk, A. (2008) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2008.11.001 · Cited by 2
Chan, R. H. Y. (2014) · Journal of Addiction Research & Therapy · doi:10.4172/2155-6105.1000198 · Cited by 1
Mechanisms by Which Pathogens Hijack and Utilize Membrane Domains to Mediate Cytotoxicity
Krummenacher, C., Brown, A. C., Edrington, T. C., Shenker, B. J., & Boesze‐Battaglia, K. (2011) · CRC Press eBooks · doi:10.1201/b11018-9 · Cited by 2
Amuategi, J., Alonso, R., & Ostolaza, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.26.470122 · Cited by 2
Structure and dynamics of cholesterol-mediated aquaporin-0 arrays and implications for lipid raftsPreprint
Chiu, P., Orjuela, J. D., de Groot, B. L., Aponte-Santamaria, C. A., & Walz, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.16.540959 · Cited by 2
Perrot, N., Isvoran, A., Nédelec, P., Jamin, N., & Beswick, V. (2023) · Analele Universităţii "Ovidius" Constanţa. Seria Chimie/"Ovidius" University Annals of Chemistry · doi:10.2478/auoc-2023-0016 · Cited by 1
Cell Junctions as Membrane Raft Domains
Resnik, N., & Veranič, P. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-396533-2.00004-5 · Cited by 1
Membrane environment and endocannabinoid signaling
Maccarrone, M. (2010) · Frontiers in Physiology · doi:10.3389/fphys.2010.00140 · Cited by 1
Functional Consequencesof the Lateral Organizationof Biological Membranes
Epand, R. M., & Epand, R. F. (2011) · CRC Press eBooks · doi:10.1201/b11018-8 · Cited by 1
Natile, G., & Denora, N. (2018) · MDPI eBooks · doi:10.3390/books978-3-03842-758-2 · Cited by 1
Amuategi, J., Alonso, R., de la Arada, I., & Ostolaza, H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.18.537300 · Cited by 1
Mecanismo de acción de la toxina alfa hemolisina de Escherichia coli
Vázquez, R. F. (2015) · doi:10.35537/10915/45707
Caveolin and cholesterol in lipid transport and signaling
Fielding, C. J. (2004) · International Congress Series · doi:10.1016/j.ics.2003.12.023
Mohideen, A. K. S., Sheriff, M. A., & Altaff, K. (2015) · American journal of biochemistry & biotechnology/American journal of biochemistry and biotechnology · doi:10.3844/ajbbsp.2015.200.213 · Cited by 1
Novak, A., & Lingwood, C. A. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/137612
Avaliação dos efeitos dos ligantes de TSPO (translocator protein 18 KDa) na ativação dos neutrófilos
Kupa, L. D. V. K. (2015) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.9.2015.tde-19102015-101109
Metadata
- Authors
- Li, H., & Papadopoulos, V.
- Affiliations
- Georgetown University Medical Center (US)
- Corresponding author
- Li, Hua
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1998-12
- Volume
- 139
- Issue
- 12
- Pages
- 4991-4997
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W4239702608
- Cited by
- 94
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 1 · 2023: 6 · 2022: 4 · 2021: 6 · 2020: 3 · 2018: 2 · 2017: 1 · 2016: 6 · 2015: 5 · 2014: 2 · 2013: 3 · 2012: 6
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrinology (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Keywords
- translocator protein (TSPO), cholesterol transport, steroidogenesis, mitochondrial outer membrane, MA-10 Leydig cells, PK11195, heterologous expression in Escherichia coli
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
