Mitochondrial cholesterol: mechanisms of import and effects on mitochondrial function
Abstract
Mitochondria require cholesterol for biogenesis and membrane maintenance, and for the synthesis of steroids, oxysterols and hepatic bile acids. Multiple pathways mediate the transport of cholesterol from different subcellular pools to mitochondria. In steroidogenic cells, the steroidogenic acute regulatory protein (StAR) interacts with a mitochondrial protein complex to mediate cholesterol delivery to the inner mitochondrial membrane for conversion to pregnenolone. In non-steroidogenic cells, several members of a protein family defined by the presence of a StAR-related lipid transfer (START) domain play key roles in the delivery of cholesterol to mitochondrial membranes. Subdomains of the endoplasmic reticulum (ER), termed mitochondria-associated ER membranes (MAM), form membrane contact sites with mitochondria and may contribute to the transport of ER cholesterol to mitochondria, either independently or in conjunction with lipid-transfer proteins. Model systems of mitochondria enriched with cholesterol in vitro and mitochondria isolated from cells with (patho)physiological mitochondrial cholesterol accumulation clearly demonstrate that mitochondrial cholesterol levels affect mitochondrial function. Increased mitochondrial cholesterol levels have been observed in several diseases, including cancer, ischemia, steatohepatitis and neurodegenerative diseases, and influence disease pathology. Hence, a deeper understanding of the mechanisms maintaining mitochondrial cholesterol homeostasis may reveal additional targets for therapeutic intervention. Here we give a brief overview of mitochondrial cholesterol import in steroidogenic cells, and then focus on cholesterol trafficking pathways that deliver cholesterol to mitochondrial membranes in non-steroidogenic cells. We also briefly discuss the consequences of increased mitochondrial cholesterol levels on mitochondrial function and their potential role in disease pathology.
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The ER is the site of action of numerous steroidogenic CYP and HSD/KSR enzymes and has attracted interest as a possible source of cholesterol for mitochondrial cholesterol metabolism.
“The ER is well known in steroidogenic research as the site of action of numerous steroidogenic CYP and HSD/KSR enzymes (3), but recently, the ER has attracted recent interest in mitochondrial cholesterol metabolism as a possible source of cholesterol (147).”
From Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies (2016) · cites this paper as [147]
Cites
Regulation of cancer cell metabolism
Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744 · see citing works
Otto Warburg's contributions to current concepts of cancer metabolism
Koppenol, W. H., Bounds, P. L., & Dang, C. V. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3038 · Cited by 3,427 · see citing works
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works
Cellular cholesterol trafficking and compartmentalization
Ikonen, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2336 · Cited by 1,455 · see citing works
Links between metabolism and cancerPreprint
Dang, C. V. (2012) · Genes & Development · doi:10.1101/gad.189365.112 · Cited by 991 · see citing works
Mitochondrial Glutathione, a Key Survival Antioxidant
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works
Horvath, S. E., & Daum, G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.07.002 · Cited by 906 · see citing works
MAM: more than just a housekeeper
Hayashi, T., Rizzuto, R., Hajnoczky, G., & Su, T.-P. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.002 · Cited by 787 · see citing works
McEnery, M. W., Snowman, A. M., Trifiletti, R. R., & Snyder, S. H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.8.3170 · Cited by 708 · see citing works
Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G. (2008) · Science · doi:10.1126/science.1161302 · Cited by 667 · see citing works
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 665 · see citing works
Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease
Area‐Gomez, E., del Carmen Lara Castillo, M., Tambini, M. D., Guardia‐Laguarta, C., de Groof, A. J. C., Madra, M., Ikenouchi, J., Umeda, M., Bird, T. D., Sturley, S. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.202 · Cited by 638 · see citing works
Bravo, R., Vicencio, J. M., Parra, V., Troncoso, R., Muñoz, J. P., Bui, M., Quiroga, C., Rodriguez, A. E., Verdejo, H., Ferreira, J., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.080762 · Cited by 607 · see citing works
Mitochondrial free cholesterol loading sensitizes to TNF- and Fas-mediated steatohepatitis
Marı́, M., Caballero, F. G., Colell, A., Morales, A., Caballería, J., Fernandez, A., Enrich, C., Fernández-Checa, J. C., & García‐Ruiz, C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.07.006 · Cited by 605 · see citing works
Structure of the human voltage-dependent anion channel
Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., & Zeth, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808115105 · Cited by 588 · see citing works
Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · see citing works
Early steps in steroidogenesis: intracellular cholesterol trafficking
Miller, W. L., & Bose, H. S. (2011) · Journal of Lipid Research · doi:10.1194/jlr.r016675 · Cited by 563 · see citing works
Structure and lipid transport mechanism of a StAR-related domain
Tsujishita (2000) · Nature Structural Biology · doi:10.1038/75192 · Cited by 535 · see citing works
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 502 · see citing works
A Role for Caveolin in Transport of Cholesterol from Endoplasmic Reticulum to Plasma Membrane
Smart, E. J., Ying, Y., Donzell, W. C., & Anderson, R. G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.29427 · Cited by 501 · see citing works
Rusiñol, A. E., Cui, Z., Chen, M. H., & Vance, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47012-3 · Cited by 469 · see citing works
Organization and Function of Membrane Contact Sites
Helle, S. C. J., Kanfer, G., Kolar, K., Lang, A., Michel, A. H., & Kornmann, B. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.028 · Cited by 453 · see citing works
Raturi, A., & Simmen, T. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.013 · Cited by 448 · see citing works
Rone, M. B., Fan, J., & Papadopoulos, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.03.001 · Cited by 399 · see citing works
START: a lipid-binding domain in StAR, HD-ZIP and signalling proteins
Ponting, C. P., & Aravind, L. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01362-6 · Cited by 398 · see citing works
Arakane, F., King, S. R., Du, Y., Kallen, C. B., Walsh, L. P., Watari, H., Stocco, D. M., & Strauss, J. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32656 · Cited by 391 · see citing works
Regulation of hexokinase binding to VDAC
Pastorino, J. G., & Hoek, J. B. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9148-8 · Cited by 388 · see citing works
Give lipids a START: the StAR-related lipid transfer (START) domain in mammals
Alpy, F., & Tomasetto, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.02485 · Cited by 384 · see citing works
Enhanced free cholesterol, SREBP-2 and StAR expression in human NASH
Caballero, F., Fernández, A., De Lacy, A. M., Fernández-Checa, J. C., Caballería, J., & García-Ruiz, C. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2008.12.016 · Cited by 368 · see citing works
Understanding metabolic regulation and its influence on cell physiology
Metallo, C. M., & Vander Heiden, M. G. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.018 · Cited by 367 · see citing works
New functions of mitochondria associated membranes in cellular signaling
van Vliet, A. R., Verfaillie, T., & Agostinis, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.009 · Cited by 353 · see citing works
Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works
Non-vesicular lipid transport by lipid-transfer proteins and beyond
Lev, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2971 · Cited by 347 · see citing works
Lacapère, J.-J., & Papadopoulos, V. (2003) · Steroids · doi:10.1016/s0039-128x(03)00101-6 · Cited by 342 · see citing works
Porter, F. D., Scherrer, D. E., Lanier, M. H., Langmade, S. J., Molugu, V., Gale, S. E., Olzeski, D., Sidhu, R., Dietzen, D. J., Fu, R., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001417 · Cited by 340 · see citing works
Murphy, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 338 · see citing works
Steroidogenic acute regulatory protein (StAR), a novel mitochondrial cholesterol transporter
Miller, W. L. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.02.012 · Cited by 332 · see citing works
Li, 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 · see citing works
Manna, P. R., Dyson, M. T., & Stocco, D. M. (2009) · Molecular Human Reproduction · doi:10.1093/molehr/gap025 · Cited by 315 · see citing works
Unearthing the secrets of mitochondrial ROS and glutathione in bioenergetics
Mailloux, R. J., McBride, S., & Harper, M. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.09.001 · Cited by 302 · see citing works
Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
Lash, L. H. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.03.001 · Cited by 280 · see citing works
Abu-Hamad, S., Zaid, H., Israelson, A., Nahon, E., & Shoshan-Barmatz, V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708216200 · Cited by 278 · see citing works
Mitochondrial Cholesterol Contributes to Chemotherapy Resistance in Hepatocellular Carcinoma
Montero, J., Morales, A., Llacuna, L., Lluis, J. M., Terrones, O., Basáñez, G., Antonsson, B. E., Prìeto, J., García‐Ruiz, C., Colell, A., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6161 · Cited by 276 · see citing works
VDAC structure, selectivity, and dynamics
Colombini, M. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.026 · Cited by 274 · see citing works
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works
Lipid droplet-organelle interactions; sharing the fats
Murphy, S., Martin, S., & Parton, R. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.07.004 · Cited by 265 · see citing works
Jamin, N., Neumann, J., Ostuni, M. A., Vu, T. K. N., Yao, Z., Murail, S., Robert, J., Giatzakis, C., Papadopoulos, V., & Lacapère, J.-J. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0308 · Cited by 254 · see citing works
Rone, M. B., Midzak, A. S., Issop, L., Rammouz, G., Jagannathan, S., Fan, J., Ye, X., Blonder, J., Veenstra, T., & Papadopoulos, V. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1159 · Cited by 247 · see citing works
Watari, H., Arakane, F., Moog-Lutz, C., Kallen, C. B., Tomasetto, C., Gerton, G. L., Rio, M.-C., Baker, M. E., & Strauss, J. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8462 · Cited by 247 · see citing works
Tomasetto, C., Régnier, C. H., Moog‐Lutz, C., Mattéi, M., Chenard, M., Lidereau, R., Basset, P., & Rio, M. (1995) · Genomics · doi:10.1006/geno.1995.1163 · Cited by 246 · see citing works
Sun, Y., Vashisht, A. A., Tchieu, J. H., Wohlschlegel, J. A., & Dreier, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419721 · Cited by 244 · see citing works
Mesmin, B., & Maxfield, F. R. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.03.002 · Cited by 243 · see citing works
Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis
Liu, J., Rone, M. B., & Papadopoulos, V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608820200 · Cited by 241 · see citing works
Niemann‐Pick type C disease: molecular mechanisms and potential therapeutic approaches
Rosenbaum, A. I., & Maxfield, F. R. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06976.x · Cited by 232 · see citing works
STARD3/STARD3NL and VAP make a novel molecular tether between late endosomes and the ER
Alpy, F., Rousseau, A., Schwab, Y., Legueux, F., Stoll, I., Wendling, C., Spiegelhalter, C., Kessler, P., Mathelin, C., Rio, M., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.139295 · Cited by 226 · see citing works
VDAC regulation: role of cytosolic proteins and mitochondrial lipids
Rostovtseva, T. K., & Bezrukov, S. M. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9145-y · Cited by 220 · see citing works
Hayashi, T., & Fujimoto, M. (2010) · Molecular Pharmacology · doi:10.1124/mol.109.062539 · Cited by 219 · see citing works
Bosch, M., Marı́, M., Herms, A., Fernández, A. M. C., Fajardo, A., Kassan, A., Giralt, A., Colell, A., Balgoma, D., Barbero, E., et al. (2011) · Current Biology · doi:10.1016/j.cub.2011.03.030 · Cited by 211 · see citing works
Altered Cholesterol Metabolism in Niemann-Pick Type C1 Mouse Brains Affects Mitochondrial Function
Yu, W., Gong, J.-S., Ko, M.-H., Garver, W. S., Yanagisawa, K., & Michikawa, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412898200 · Cited by 207 · see citing works
Mitochondrial glutathione: Features, regulation and role in disease
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.018 · Cited by 205 · see citing works
Charman, M., Kennedy, B. E., Osborne, N., & Karten, B. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m002345 · Cited by 201 · see citing works
Self-citationThe Mechanism of Action of Steroidogenic Acute Regulatory Protein (StAR)
Arakane, F., Kallen, C. B., Watari, H., Foster, J. A., Sepuri, N. B. V., Pain, D., Stayrook, S. E., Lewis, M., Gerton, G. L., & Strauss, J. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16339 · Cited by 200 · see citing works
Soccio, R. E., Adams, R. M., Romanowski, M. J., Sehayek, E., Burley, S. K., & Breslow, J. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052143799 · Cited by 188 · see citing works
Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
Arbel, N., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345918 · Cited by 179 · see citing works
Alpy, F., Stoeckel, M. E., Dierich, A., Escola, J.-M., Wendling, C., Chenard, M., Vanier, M. T., Gruenberg, J. E., Tomasetto, C., & Rio, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006279200 · Cited by 176 · see citing works
Lluis, J. M., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2003) · Gastroenterology · doi:10.1053/gast.2003.50089 · Cited by 172 · see citing works
Gilquin, B., Taillebourg, E., Cherradi, N., Hubstenberger, A., Gay, O., Merle, N., Assard, N., Fauvarque, M.-O., Tomohiro, S., Kuge, O., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00007-10 · Cited by 171 · see citing works
Mitochondria: gatekeepers of response to chemotherapy
Sarosiek, K. A., Chonghaile, T. N., & Letai, A. G. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.003 · Cited by 170 · see citing works
MLN64 Mediates Mobilization of Lysosomal Cholesterol to Steroidogenic Mitochondria
Zhang, M., Liu, P., Dwyer, N. K., Christenson, L. K., Fujimoto, T., Martı́nez, F., Comly, M., Hanover, J. A., Blanchette‐Mackie, E. J., & Strauss, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200003200 · Cited by 169 · see citing works
Colell, A., García‐Ruiz, C., Morales, A., Ballesta, A. M., Ookhtens, M., Rodés, J., Kaplowitz, N., & Fernández-Checa, J. C. (1997) · Hepatology · doi:10.1002/hep.510260323 · Cited by 165 · see citing works
The mammalian START domain protein family in lipid transport in health and disease
Clark, B. J. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0313 · Cited by 163 · see citing works
Coll, O., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2003) · Hepatology · doi:10.1053/jhep.2003.50351 · Cited by 151 · see citing works
Fernández, A., Llacuna, L., Fernández-Checa, J. C., & Colell, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4909-08.2009 · Cited by 150 · see citing works
START domain proteins and the intracellular trafficking of cholesterol in steroidogenic cells
Strauss, J. F., Kishida, T., Christenson, L. K., Fujimoto, T., & Hiroi, H. (2003) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(03)00063-7 · Cited by 150 · see citing works
Mitochondrial fusion is essential for steroid biosynthesis
Duarte, A., Poderoso, C., Cooke, M., Soria, G., Cornejo Maciel, F., Gottifredi, V., & Podestá, E. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045829 · Cited by 149 · see citing works
Bose, M., Whittal, R. M., Miller, W. L., & Bose, H. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709221200 · Cited by 143 · see citing works
Acyl-coenzyme A binding domain containing 3 (ACBD3; PAP7; GCP60): An emerging signaling molecule
Fan, J., Liu, J., Culty, M., & Papadopoulos, V. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.12.003 · Cited by 142 · see citing works
The role of cholesterol in the association of endoplasmic reticulum membranes with mitochondria
Fujimoto, M., Hayashi, T., & Su, T.-P. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.12.022 · Cited by 140 · see citing works
Parlo, R. A., & Coleman, P. S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90917-8 · Cited by 139 · see citing works
Mitochondrial VDAC1: Function in Cell Life and Death and a Target for Cancer Therapy
Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 139 · see citing works
The 3D structures of VDAC represent a native conformation
Hiller, S., Abramson, J., Mannella, C. A., Wagner, G., & Zeth, K. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.03.005 · Cited by 137 · see citing works
Colell, A., García‐Ruiz, C., Lluis, J. M., Coll, O., Marı́, M., & Fernández-Checa, J. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210943200 · Cited by 136 · see citing works
Lucken‐Ardjomande, S., Montessuit, S., & Martinou, J. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402280 · Cited by 134 · see citing works
STARD4 abundance regulates sterol transport and sensing
Mesmin, B., Pipalia, N. H., Lund, F. W., Ramlall, T. F., Sokolov, A., Eliezer, D., & Maxfield, F. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0372 · Cited by 132 · see citing works
Karten, B., Peake, K. B., & Vance, J. (2009) · Biochimica et Biophysica Acta · doi:10.1016/j.bbalip.2009.01.025 · Cited by 129 · see citing works
Self-citationIs there a mitochondrial signaling complex facilitating cholesterol import?
Papadopoulos, V., Liu, J., & Culty, M. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.004 · Cited by 125 · see citing works
Rispoli, L. A., Horvat, R. D., Roess, D. A., Barisas, B. G., Juengel, J. L., & NISWENDER, G. D. (2001) · Endocrinology · doi:10.1210/endo.142.1.8052 · Cited by 124 · see citing works
Differential gene regulation of StarD4 and StarD5 cholesterol transfer proteins
Soccio, R. E., Adams, R. M., Maxwell, K. N., & Breslow, J. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501778200 · Cited by 118 · see citing works
Oxidative stress in Niemann–Pick disease, type C
Fu, R., Yanjanin, N. M., Bianconi, S. E., Pavan, W. J., & Porter, F. D. (2010) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2010.06.018 · Cited by 117 · see citing works
Disruption and therapeutic rescue of autophagy in a human neuronal model of Niemann Pick type C1
Ordonez, M. P., Roberts, E. A., Kidwell, C. U., Yuan, S. H., Plaisted, W. C., & Goldstein, L. S. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds090 · Cited by 117 · see citing works
Barbero-Camps, E., Fernández, A., Martínez, L., Fernández-Checa, J., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 113 · see citing works
Montero, J., Marı́, M., Colell, A., Morales, A., Basáñez, G., García‐Ruiz, C., & Fernández-Checa, J. C. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.010 · Cited by 112 · see citing works
Maldonado, E. N., & Lemasters, J. J. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192153 · Cited by 112 · see citing works
Paradies, G., & Ruggiero, F. M. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90060-h · Cited by 111 · see citing works
Modeling the structure of the StART domains of MLN64 and StAR proteins in complex with cholesterol
Murcia, M., Faráldo-Gómez, J. D., Maxfield, F. R., & Roux, B. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600232-jlr200 · Cited by 111 · see citing works
Mitochondria‐localized caveolin in adaptation to cellular stress and injury
Fridolfsson, H. N., Kawaraguchi, Y., Ali, S. S., Panneerselvam, M., Niesman, I. R., Finley, J. C., Kellerhals, S. E., Migita, M. Y., Okada, H., Moreno, A. L., et al. (2012) · The FASEB Journal · doi:10.1096/fj.12-215798 · Cited by 108 · see citing works
Katz, Y. S., Ben‐Baruch, G., Kloog, Y., Menczer, J., & Gavish, M. (1990) · Clinical Science · doi:10.1042/cs0780155 · Cited by 106 · see citing works
ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells
Fang, H., Chang, C.-L., Hsu, S., Huang, K. C., Chiang, S., Chiou, S.-H., Huang, C.-H., Hsiao, Y.-T., Lin, T., Chiang, I., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.062034 · Cited by 106 · see citing works
Barbero‐Camps, E., Fernández, A., Baulies, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.03.014 · Cited by 105 · see citing works
Where Killers Meet--Permeabilization of the Outer Mitochondrial Membrane during ApoptosisPreprint
Bender, T., & Martinou, J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011106 · Cited by 105 · see citing works
Geula, S., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Biochemical Journal · doi:10.1042/bj20112079 · Cited by 105 · see citing works
Fernandez, A., Matías, N., Fucho, R., Ribas, V., von Montfort, C., Nuño‐Lámbarri, N., Baulies, A., Martínez-Gili, L., Tarrats, N., Marı́, M., et al. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.05.023 · Cited by 103 · see citing works
START ships lipids across interorganelle space
Alpy, F., & Tomasetto, C. (2013) · Biochimie · doi:10.1016/j.biochi.2013.09.015 · Cited by 102 · see citing works
Bose, H. S., Whittal, R. M., Huang, M.-C., Baldwin, M. A., & Miller, W. L. (2000) · Biochemistry · doi:10.1021/bi000911l · Cited by 101 · see citing works
Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1
Choudhary, O. P., Paz, A., Adelman, J. L., Colletier, J., Abramson, J., & Grabe, M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2841 · Cited by 100 · see citing works
Organelle plasticity and interactions in cholesterol transport and steroid biosynthesis
Issop, L., Rone, M. B., & Papadopoulos, V. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.12.003 · Cited by 99 · see citing works
Kishida, T., Kostetskii, I., Zhang, Z., Martı́nez, F., Liu, P., Walkley, S. U., Dwyer, N. K., Blanchette‐Mackie, E. J., Radice, G. L., & Strauss, J. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400717200 · Cited by 93 · see citing works
Cluzeau, C. V. M., Watkins‐Chow, D. E., Fu, R., Borate, B. R., Yanjanin, N. M., Dail, M. K., Davidson, C. D., Walkley, S. U., Ory, D. S., Wassif, C. A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds193 · Cited by 93 · see citing works
Rodríguez‐Agudo, D., Ren, S., Wong, E., Marques, D., Redford, K. S., Gil, G., Hylemon, P. B., & Pandak, W. M. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m700537-jlr200 · Cited by 92 · see citing works
Carmel, I., Fares, F., Leschiner, S., Scherübl, H., Weisinger, G., & Gavish, M. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00093-3 · Cited by 90 · see citing works
Oxidative Stress: A Pathogenic Mechanism for Niemann-Pick Type C Disease
Vázquez, M. C., Balboa, E., Alvarez, A. R., & Zanlungo, S. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/205713 · Cited by 90 · see citing works
Paradies, G., & Ruggiero, F. M. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90304-2 · Cited by 88 · see citing works
Kennedy, B. E., Madreiter‐Sokolowski, C. T., Vishnu, N., Malli, R., Graier, W. F., & Karten, B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.559914 · Cited by 87 · see citing works
Self-citationParadies, G., Petrosillo, G., Gadaleta, M. N., & Ruggiero, F. M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00809-1 · Cited by 84 · see citing works
The Niemann-Pick Disease Genes Regulators of Cellular Cholesterol Homeostasis
Ory, D. (2004) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2003.12.003 · Cited by 83 · see citing works
Endosome–mitochondria juxtaposition during apoptosis induced by H. pylori VacA
Calore, F., Genisset, C., Casellato, A., Rossato, M., Codolo, G., Esposti, M. D., Scorrano, L., & de Bernard, M. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.42 · Cited by 82 · see citing works
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 · see citing works
Cholesterol ester droplets and steroidogenesis
Kraemer, F. B., Khor, V. K., Shen, W., & Azhar, S. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.10.012 · Cited by 79 · see citing works
MLN64 Is Involved in Actin-mediated Dynamics of Late Endocytic Organelles
Hölttä‐Vuori, M., Alpy, F., Tanhuanpää, K., Jokitalo, E., Mutka, A., & Ikonen, E. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-12-1105 · Cited by 76 · see citing works
StAR-like activity and molten globule behavior of StARD6, a male germ-line protein
Bose, H. S., Whittal, R. M., Ran, Y., Bose, M., Baker, B. Y., & Miller, W. L. (2008) · Biochemistry · doi:10.1021/bi701966a · Cited by 74 · see citing works
Functional characterization of the MENTAL domain
Alpy, F., Latchumanan, V. K., Kedinger, V., Janoshazi, A., Thiele, C., Wendling, C., Rio, M.-C., & Tomasetto, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500723200 · Cited by 71 · see citing works
Rostovtseva, T. K., Gurnev, P. A., Chen, M.-Y., & Bezrukov, S. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.378778 · Cited by 70 · see citing works
Detection of the steroidogenic acute regulatory protein, StAR, in human liver cells
Hall, E. A., Ren, S., Hylemon, P. B., Rodríguez‐Agudo, D., Redford, K. S., Marques, D., Kang, D., Gil, G., & Pandak, W. M. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2005.01.004 · Cited by 65 · see citing works
Ren, S., Hylemon, P. B., Marques, D., Hall, E., Redford, K. S., Gil, G., & Pandak, W. M. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m400233-jlr200 · Cited by 65 · see citing works
Molten Globule Structure and Steroidogenic Activity of N-218 MLN64 in Human Placental Mitochondria
Tuckey, R. C., Bose, H. S., Czerwionka, I., & Miller, W. L. (2004) · Endocrinology · doi:10.1210/en.2003-1034 · Cited by 64 · see citing works
Hsa-miR-34c suppresses growth and invasion of human laryngeal carcinoma cells via targeting c-Met
Cai (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000378 · Cited by 63 · see citing works
Kennedy, B. E., Charman, M., & Karten, B. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m029942 · Cited by 63 · see citing works
Self-citationLlacuna, L., Fernández, A., von Montfort, C., Matías, N., Martínez-Gili, L., Caballero, F., Rimola, A., Elena, M., Morales, A., Fernández-Checa, J. C., et al. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.08.031 · Cited by 61 · see citing works
Modulation of Plant Mitochondrial VDAC by Phytosterols
Mlayeh, L., Chatkaew, S., Léonetti, M., & Homblé, F. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.067 · Cited by 60 · see citing works
Lavigne, P., Najmanivich, R., & Lehoux, J. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-8622-8_15 · Cited by 59 · see citing works
MENTHO, a MLN64 homologue devoid of the START domain
Alpy, F., Wendling, C., Rio, M.-C., & Tomasetto, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208290200 · Cited by 58 · cited 4× · see citing works
“…Stard3-Nterminal domain, when present above certain threshold levels, sequesters cholesterol in the endosomal perimeter membrane, possibly due to its oligomerization (Alpy et al. 2005; Alpy et al. 2002; Alpy and Tomasetto 2006), and can inhibit the import of endosomal cholesterol into mitochondria.”
BackgroundInfluentialMitochondrial Cholesterol: A Connection Between Caveolin, Metabolism, and Disease
Bosch, M., Marı́, M., Gross, S. P., Fernández-Checa, J. C., & Pol, A. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01259.x · Cited by 58 · see citing works
Baggetto, L. G., Clottes, E., & Vial, C. (1992) · PubMed · Cited by 57 · see citing works
ATAD3, a vital membrane bound mitochondrial ATPase involved in tumor progression
Li, S., & Rousseau, D. L. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9424-5 · Cited by 56 · see citing works
THE STEROIDOGENIC ACUTE REGULATORY PROTEIN, StAR, WORKS ONLY AT THE OUTER MITOCHONDRIAL MEMBRANE
Bose, H. S., Lingappa, V. R., & Miller, W. L. (2002) · Endocrine Research · doi:10.1081/erc-120016800 · Cited by 56 · see citing works
Paradis, S., Leoni, V., Caccia, C., Berdeaux, A., & Morin, D. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt079 · Cited by 56 · see citing works
Ziółkowski, W., Szkatuła, M., Nurczyk, A., Wakabayashi, T., Kaczor, J. J., Olek, R. A., Knap, N., Antosiewicz, J., Wieckowski, M. R., & Woźniak, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.10.023 · Cited by 55 · see citing works
Eckmann, J., Clemens, L. E., Eckert, S. H., Hagl, S., Yu-Taeger, L., Bordet, T., Pruss, R. M., Muller, W. E., Leuner, K., Nguyen, H. P., et al. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8663-3 · Cited by 53 · see citing works
MLN64 and MENTHO, two mediators of endosomal cholesterol transport
Alpy, F., & Tomasetto, C. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340343 · Cited by 53 · see citing works
Campbell, A. M., & Chan, S. H. P. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9138-x · Cited by 52 · see citing works
Kennedy, B. E., Leblanc, V., Mailman, T. M., Fice, D., Burton, I. W., Karakach, T. K., & Karten, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082685 · Cited by 52 · see citing works
Self-citationReitz, J., Gehrig‐Burger, K., Strauss, J. F., & Gimpl, G. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06337.x · Cited by 52 · see citing works
Riegelhaupt, J. J., Waase, M. P., Garbarino, J., Cruz, D. E., & Breslow, J. L. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m003095 · Cited by 52 · see citing works
Popp, B., Schmid, A., & Benz, R. (1995) · Biochemistry · doi:10.1021/bi00010a026 · Cited by 52 · see citing works
The voltage dependent anion channel affects mitochondrial cholesterol distribution and function
Campbell, A. M., & Chan, S. H. P. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.06.012 · Cited by 47 · see citing works
Lange, Y., Steck, T. L., Ye, J., Lanier, M. H., Molugu, V., & Ory, D. S. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m900116-jlr200 · Cited by 46 · see citing works
Overexpression of STARD3 in human monocyte/macrophages induces an anti-atherogenic lipid phenotype
Borthwick, F., Allen, A.-M., Taylor, J. M. W., & Graham, A. (2010) · Clinical Science · doi:10.1042/cs20100266 · Cited by 45 · see citing works
Expression of the Putative Sterol Binding Protein Stard6 Gene Is Male Germ Cell Specific1
Gomes, C., Oh, S., Kim, J.-W., Chun, S., Lee, K., Kwon, H.-B., & Soh, J. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.104.032672 · Cited by 44 · see citing works
Echegoyen, S., Oliva, E. B., Sepúlveda, J., Díaz-Zagoya, J. C., Espinosa-García, M. T., Pardo, J. P., & Martı́nez, F. (1993) · Biochemical Journal · doi:10.1042/bj2890703 · Cited by 44 · see citing works
Garbarino, J., Pan, M., Chin, H. F., Lund, F. W., Maxfield, F. R., & Breslow, J. L. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m032227 · Cited by 43 · see citing works
Stigliano, A., Gandini, O., Cerquetti, L., Gazzaniga, P., Misiti, S., Monti, S., Gradilone, A., Falasca, P., Poggi, M., Brunetti, E., et al. (2007) · Journal of Endocrinology · doi:10.1677/joe-07-0131 · Cited by 43 · see citing works
Translocator Protein Blockade Reduces Prostate Tumor Growth
Fafalios, A., Akhavan, A., Parwani, A. V., Bies, R. R., McHugh, K. J., & Pflug, B. R. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-0844 · Cited by 43 · see citing works
Mitochondrial cholesterol content and membrane properties in porcine myocardial ischemia
ROUSLIN, W., MacGee, J., Gupte, S. S., Wesselman, A., & Epps, D. E. V. (1982) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1982.242.2.h254 · Cited by 43 · see citing works
Mohamed, A., Saavedra, L., Pardo, A. D., Sipione, S., & Chaves, E. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0630-12.2012 · Cited by 41 · see citing works
The Human Cytomegalovirus Protein UL37 Exon 1 Associates with Internal Lipid Rafts
Williamson, C. D., Zhang, A., & Colberg‐Poley, A. M. (2010) · Journal of Virology · doi:10.1128/jvi.01830-10 · Cited by 38 · see citing works
StAR-related lipid transfer domain protein 5 binds primary bile acids
Létourneau, D., Lorin, A., Lefèbvre, A., Frappier, V., Gaudreault, F., Najmanovich, R., Lavigne, P., & Lehoux, J. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m031245 · Cited by 38 · see citing works
Expression analysis of ATAD3 isoforms in rodent and human cell lines and tissues
Li, S., Lamarche, F., Charton, R., Delphin, C., Gires, O., Hubstenberger, A., Schlattner, U., & Rousseau, D. L. (2013) · Gene · doi:10.1016/j.gene.2013.10.062 · Cited by 37 · see citing works
Madden, T. D., Vigo, C., Bruckdorfer, K. R., & Chapman, D. (1980) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(80)90197-2 · Cited by 35 · see citing works
Evidence That Star and MLN64 act on the Outer Mitochondrial Membrane as Molten Globules
Bose, H. S., Baldwin, M. A., & Miller, W. L. (2000) · Endocrine Research · doi:10.3109/07435800009048583 · Cited by 35 · see citing works
Ha, S.-D., Park, S., Han, C. Y., Nguyen, M. L., & Kim, S. O. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00494-12 · Cited by 33 · see citing works
Sangeetha, T., & Quine, S. D. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0066-9 · Cited by 33 · see citing works
Paradies, G., Ruggiero, F. M., Petrosillo, G., Gadaleta, M. N., & Quagliariello, E. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb12093.x · Cited by 32 · see citing works
Liapis, A., Chen, F. W., Davies, J. P., Wang, R., & Ioannou, Y. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034424 · Cited by 30 · see citing works
Paradies, G., Ruggiero, F. M., & Dinoi, P. (1992) · International Journal of Biochemistry · doi:10.1016/0020-711x(92)90012-p · Cited by 29 · see citing works
[4] Lipid enrichment and fusion of mitochondrial inner membranes
Hackenbrock, C. R., & Chazotte, B. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)25006-5 · Cited by 29 · see citing works
Changes in specific lipids regulate BAX‐induced mitochondrial permeability transition
Abundis, E. M., Garcı́a, N., Correa, F., Franco, M., & Zazueta, C. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06166.x · Cited by 28 · see citing works
Calderón‐Domínguez, M., Gil, G., Medina, M. Á., Pandak, W. M., & Rodríguez‐Agudo, D. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.01.002 · Cited by 27 · see citing works
Cholesterol increase in mitochondria: a new method of cholesterol incorporation.
Martı́nez, F., Eschegoyen, S., Briones, R., & Cuellar, A. (1988) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38465-0 · Cited by 27 · see citing works
Rodríguez‐Agudo, D., Calderón‐Domínguez, M., Medina, M. Á., Ren, S., Gil, G., & Pandak, W. M. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m031997 · Cited by 26 · see citing works
Villoutreix, B. O., Dahlb�ck, B., Borgel, D., Gandrille, S., & Muller, Y. A. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010501)43:2 · Cited by 26 · see citing works
Létourneau, D., Lorin, A., Lefèbvre, A., Cabana, J., Lavigne, P., & Lehoux, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.07.005 · Cited by 24 · see citing works
Mei, S., Gu, H., Yang, X., Guo, H., Liu, Z., & Cao, W. (2012) · Endocrinology · doi:10.1210/en.2011-2119 · Cited by 22 · see citing works
Regulation of human STARD4 gene expression under endoplasmic reticulum stress
Yamada, S. D., Yamaguchi, T., Hosoda, A., Iwawaki, T., & Kohno, K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.051 · Cited by 22 · see citing works
Prabhu, A. V., Krycer, J. R., & Brown, A. J. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.02.040 · Cited by 21 · see citing works
Les protéines à domaine START, des trafiquants intracellulaires de lipides
Alpy, F., Legueux, F., Bianchetti, L., & Tomasetto, C. (2009) · médecine/sciences · doi:10.1051/medsci/2009252181 · Cited by 20 · see citing works
Dietzen, D. J., & Davis, E. J. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1122 · Cited by 19 · see citing works
STARD5 specific ligand binding: Comparison with STARD1 and STARD4 subfamilies
Létourneau, D., Lefèbvre, A., Lavigne, P., & Lehoux, J. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.004 · Cited by 19 · see citing works
STARD6 is expressed in steroidogenic cells of the ovary and can enhance de novo steroidogenesis
LaVoie, H. A., Whitfield, N. E., Shi, B., King, S. R., Bose, H. S., & Hui, Y. Y. (2014) · Experimental Biology and Medicine · doi:10.1177/1535370213517616 · Cited by 18 · see citing works
Jiang, W. G. (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000379 · Cited by 18 · see citing works
Characterization of peripheral benzodiazepine receptors in rat prostatic adenocarcinoma
Batra, S. C., & Alenfall, J. (1994) · The Prostate · doi:10.1002/pros.2990240509 · Cited by 17 · see citing works
Ziółkowski, W., Vadhana, D., Kaczor, J. J., Olek, R. A., Flis, D. J., Hałoń, M., Woźniak, M., Fedeli, D., Carloni, M., Antosiewicz, J., et al. (2013) · Experimental Physiology · doi:10.1113/expphysiol.2013.073007 · Cited by 11 · see citing works
On a fully closed state of native human type-1 VDAC enriched in Nonidet P40
THINNES, F. P., & Burckhardt, G. (2012) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2012.08.015 · Cited by 9 · see citing works
The influence of sterols on the conformation of recombinant mitochondrial porin in detergent
Bay, D. C., O’Neil, J. D., & Court, D. A. (2008) · Biochemistry and Cell Biology · doi:10.1139/o08-132 · Cited by 8 · see citing works
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Mitochondria at the crossroads of health and disease
Suomalainen, A., & Nunnari, J. M. (2024) · Cell · doi:10.1016/j.cell.2024.04.037 · Cited by 512 · see citing works
Molecular mechanisms of mitochondrial dynamics
Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 431 · see citing works
Oxysterol Restraint of Cholesterol Synthesis Prevents AIM2 Inflammasome Activation
Dang, E. V., McDonald, J. G., Russell, D. W., & Cyster, J. G. (2017) · Cell · doi:10.1016/j.cell.2017.09.029 · Cited by 348 · see citing works
Li, X., Xin, Y., Mo, Y., Marozik, P. M., He, T., & Guo, H. (2022) · Molecules · doi:10.3390/molecules27020523 · Cited by 189 · see citing works
Mitochondrial cholesterol import
Elustondo, P. A., Martin, L. A., & Karten, B. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.012 · Cited by 160 · see citing works
Self-citationCellular cholesterol homeostasis and Alzheimer’s disease
Chang, T.-Y., Yamauchi, Y., Hasan, M. T., & Chang, C. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075630 · Cited by 155 · see citing works
Cardiac metabolism in HFpEF: from fuel to signalling
Capone, F., Sotomayor-Flores, C., Bode, D., Wang, R., Rodolico, D., Strocchi, S., & Schiattarella, G. G. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac166 · Cited by 141 · see citing works
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 · see citing works
Mitochondria Quality Control and Male Fertility
Costa, J. L., Braga, P. C., Rebelo, I., Oliveira, P. F., & Alves, M. G. (2023) · Biology · doi:10.3390/biology12060827 · Cited by 115 · see citing works
Lipids, inflammasomes, metabolism, and disease
Anand, P. (2020) · Immunological Reviews · doi:10.1111/imr.12891 · Cited by 104 · see citing works
Routes and mechanisms of post‐endosomal cholesterol trafficking: A story that never ends
Luo, J., Jiang, L., Yang, H., & Song, B. (2017) · Traffic · doi:10.1111/tra.12471 · Cited by 102 · see citing works
Cholesterol homeostasis: Researching a dialogue between the brain and peripheral tissues
Gliozzi, M., Musolino, V., Bosco, F., Scicchitano, M., Scarano, F., Nucera, S., Zito, M. C., Ruga, S., Carresi, C., Macrì, R., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105215 · Cited by 92 · see citing works
Expression and putative role of mitochondrial transport proteins in cancer
Lytovchenko, O., & Kunji, E. R. S. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.03.006 · Cited by 78 · see citing works
Zhong, S., Li, L., Liang, N., Zhang, L., Xu, X., Chen, S., & Yin, H. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101919 · Cited by 76 · see citing works
Lipotoxicity: a driver of heart failure with preserved ejection fraction?
Leggat, J., Bidault, G., & Vidal‐Puig, A. (2021) · Clinical Science · doi:10.1042/cs20210127 · Cited by 74 · see citing works
Mitochondrial matrix proteases: quality control and beyond
Szczepanowska, K., & Trifunović, A. (2021) · FEBS Journal · doi:10.1111/febs.15964 · Cited by 76 · see citing works
Mitochondrial DNA signals driving immune responses: Why, How, Where?
Giordano, L., Ware, S. A., Lagranha, C. J., & Kaufman, B. A. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02042-0 · Cited by 77 · see citing works
Thoughts on interactions between PGRMC1 and diverse attested and potential hydrophobic ligands
Cahill, M. A., & Medlock, A. E. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2016.12.020 · Cited by 68 · see citing works
Castillo, A. F., Orlando, U. D., Helfenberger, K. E., Poderoso, C., & Podesta, E. J. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.12.011 · Cited by 67 · see citing works
Cholesterol Metabolism: A Double-Edged Sword in Hepatocellular Carcinoma
Zhou, F., & Sun, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.762828 · Cited by 66 · see citing works
Multiple functions of syncytiotrophoblast mitochondria
Martı́nez, F., Olvera-Sánchez, S., Esparza-Perusquía, M., Gómez-Chang, E., & Flores-Herrera, Ó. (2015) · Steroids · doi:10.1016/j.steroids.2015.09.006 · Cited by 61 · see citing works
Tsui, H. S., Pham, N. B., Amer, B. R., Bradley, M. C., Gosschalk, J. E., Gallagher-Jones, M., Ibarra, H., Clubb, R., Blaby, C., & Clarke, C. F. (2019) · Journal of Lipid Research · doi:10.1194/jlr.m093534 · Cited by 57 · see citing works
Hepatic alterations during the development and progression of cancer cachexia
Rosa‐Caldwell, M. E., Brown, J. L., Lee, D. E., Wiggs, M. P., Perry, R. A., Haynie, W. S., Caldwell, A. R., Washington, T. A., Lo, W.-J., & Greene, N. P. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0407 · Cited by 57 · see citing works
Li, L., Liu, Y., Liu, X., Zheng, N., Gu, Y., Song, Y., & Wang, X. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.902 · Cited by 56 · see citing works
Mitochondrial regulation of macrophage cholesterol homeostasis
Graham, A. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.010 · Cited by 54 · see citing works
Development of a neurotoxicity assay that is tuned to detect mitochondrial toxicants
Delp, J., Funke, M., Rudolf, F., Cediel-Ulloa, A., Bennekou, S. H., van der Stel, W., Carta, G., Jennings, P., Toma, C., Gardner, I. B., et al. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02473-y · Cited by 53 · see citing works
Lysosome-Mitochondrial Crosstalk in Cellular Stress and Disease
Kiraly, S., Stanley, J., & Eden, E. R. (2025) · Antioxidants · doi:10.3390/antiox14020125 · Cited by 52 · see citing works
Imidacloprid disrupts the endocrine system by interacting with androgen receptor in male mice
Yuan, X., Shen, J., Zhang, X., Tu, W., Fu, Z., & Jin, Y. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.135163 · Cited by 52 · see citing works
The role of mitochondrial dynamics in mtDNA maintenance
Sabouny, R., & Shutt, T. E. (2021) · Journal of Cell Science · doi:10.1242/jcs.258944 · Cited by 51 · see citing works
Mitochondrial Dysfunction and Diabetes: Is Mitochondrial Transfer a Friend or Foe?
Montgomery, M. K. (2019) · Biology · doi:10.3390/biology8020033 · Cited by 52 · see citing works
Cholesterol—The Devil You Know; Ceramide—The Devil You Don’t
Tippetts, T. S., Holland, W., & Summers, S. (2021) · TIPS - Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.10.001 · Cited by 47 · see citing works
Mitochondrial dysfunction and pancreatic islet β‑cell failure (Review)
Sha, W., Hu, F., & Bu, S. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9396 · Cited by 51 · see citing works
ER‐mitochondria contacts and cholesterol metabolism are disrupted by disease‐associated tau protein
Szabo, L., Cummins, N., Paganetti, P., Odermatt, A., Papassotiropoulos, A., Karch, C. M. M., Götz, J., Eckert, A., & Grimm, A. (2023) · EMBO Reports · doi:10.15252/embr.202357499 · Cited by 48 · see citing works
Yanagisawa, R., He, C., Asai, A., Hellwig, M., Henle, T., & Toda, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012236 · Cited by 47 · see citing works
Pathological Crosstalk Between Oxidized LDL and ER Stress in Human Diseases: A Comprehensive Review
Varghese, D. S., & Ali, B. R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.674103 · Cited by 48 · see citing works
Vrijsen, S., Vrancx, C., Vecchio, M. D., Swinnen, J. V., Agostinis, P., Winderickx, J., Vangheluwe, P., & Annaert, W. G. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.900338 · Cited by 52 · see citing works
Tian, S., Ohta, A., Horiuchi, H., & Fukuda, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000596 · Cited by 43 · see citing works
Aster-B coordinates with Arf1 to regulate mitochondrial cholesterol transport
Andersen, J.-P., Zhang, J., Sun, H., Liu, X., Liu, J., Nie, J., & Shi, Y. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101055 · Cited by 39 · see citing works
Mitochondrial Proteolysis and Metabolic Control
Ahola, S., Langer, T., & MacVicar, T. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033936 · Cited by 37 · see citing works
Dombach, J. L., Quintana, J. L. J., Nagy, T. A., Wan, C., Crooks, A. L., Yu, H., Su, C., Yu, E. W., Shen, J., & Detweiler, C. S. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1009119 · Cited by 34 · see citing works
Setting the curve: the biophysical properties of lipids in mitochondrial form and function
Venkatraman, K., Lee, C. T., & Budin, I. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100643 · Cited by 32 · see citing works
Mareninova, O. A., Végh, E. T., Shalbuyeva, N., Wightman, C. J. M., Dillon, D. L., Malla, S. R., Xie, Y., Takahashi, T., Rakonczay, Z., French, S. W., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci146870 · Cited by 33 · see citing works
Myocardial Metabolism in Heart Failure with Preserved Ejection Fraction
Henry, J. A., Couch, L. S., & Rider, O. J. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13051195 · Cited by 30 · see citing works
Mitochondrial Disorders in Alzheimer’s Disease
Sukhorukov, V. S., Mudzhiri, N. M., Voronkova, A. S., Baranich, T. I., Glinkina, V. V., & Illarioshkin, S. N. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921060055 · Cited by 30 · see citing works
Batissaco, L., de Arruda, R. P., Alves, M. B. R., Torres, M. A., Lemes, K. M., Prado-Filho, R. R., Almeida, T. G. D., de Andrade, A. F. C., & Celeghini, E. C. C. (2020) · Reproductive Biology · doi:10.1016/j.repbio.2020.01.002 · Cited by 29 · see citing works
Fundamentals of CNS energy metabolism and alterations in lysosomal storage diseases
McKenna, M. C., Schuck, P. F., & Ferreira, G. C. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14577 · Cited by 29 · see citing works
The ER-mitochondria Ca2+ signaling in cancer progression: Fueling the monster
Bustos, G., Ahumada-Castro, U., Silva-Pavez, E., Puebla, A., Lovy, A., & Cárdenas, C. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.03.006 · Cited by 28 · see citing works
Shan, A., Li, M., Li, X., Li, Y., Yan, M., Xian, P., Chang, Y., Chen, X., & Tang, N. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00312 · Cited by 27 · see citing works
MitoQ Is Able to Modulate Apoptosis and Inflammation
Piscianz, E., Tesser, A., Rimondi, E., Melloni, E., Celeghini, C., & Marcuzzi, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094753 · Cited by 26 · see citing works
Zhuang, Y., Chai, J., Abdelsattar, M. M., Fu, Y., & Zhang, N. (2023) · Animal nutrition · doi:10.1016/j.aninu.2023.02.012 · Cited by 26 · see citing works
Gou, Y., Wang, L., Zhao, J., Xu, X., Xu, H., Xie, F. X., Wang, Y., Feng, Y., Zhang, J., & Zhang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119681 · Cited by 25 · see citing works
Mitochondrial respiratory chain dysfunction alters ER sterol sensing and mevalonate pathway activity
Wall, C. T., Lefebvre, G. C., Métairon, S., Descombes, P., Wiederkehr, A., & Domingo, J. S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101652 · Cited by 24 · see citing works
Targeting mitochondria: how intravacuolar bacterial pathogens manipulate mitochondria
Fielden, L. F., Kang, Y., Newton, H. J., & Stojanovski, D. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2475-x · Cited by 24 · see citing works
Kim, J. E., Park, S., Kwak, C. S., Lee, Y., Song, D., Jung, J. W., Lee, H., Shin, E., Pinanga, Y. D., Pyo, K., et al. (2023) · 癌症:英文版 · doi:10.1002/cac2.12510 · Cited by 22 · see citing works
Mitochondrially-Targeted Therapeutic Strategies for Alzheimer’s Disease
Onyango, I. G., Bennett, J. P., & Stokin, G. B. (2021) · Current Alzheimer Research · doi:10.2174/1567205018666211208125855 · Cited by 21 · see citing works
The heat shock protein 60 promotes progesterone synthesis in mitochondria of JEG-3 cells
Monreal‐Flores, J., Espinosa-García, M. T., García-Regalado, A., Arechavaleta-Velasco, F., & Martı́nez, F. (2017) · Reproductive Biology · doi:10.1016/j.repbio.2017.04.001 · Cited by 22 · see citing works
Petricca, S., Celenza, G., Luzi, C., Cinque, B., Lizzi, A. R., Franceschini, N., Festuccia, C., & Iorio, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105429 · Cited by 21 · see citing works
Cardiomyocyte-specific PCSK9 deficiency compromises mitochondrial bioenergetics and heart function
Laudette, M., Lindbom, M., Arif, M., Cinato, M., Ruiz, M., Doran, S., Miljanovic, A., Rutberg, M., Andersson, L. K., Klevstig, M., et al. (2023) · Cardiovascular Research · doi:10.1093/cvr/cvad041 · Cited by 21 · see citing works
Plasma membrane cholesterol trafficking in steroidogenesis
Deng, B., Shen, W., Dong, D., Azhar, S., & Kraemer, F. B. (2018) · The FASEB Journal · doi:10.1096/fj.201800697rrr · Cited by 21 · see citing works
Jiang, Z., Teng, L., Zhang, S., & Ding, Y. (2020) · Mitochondrial DNA Part A · doi:10.1080/24701394.2020.1856101 · Cited by 21 · see citing works
Mollinedo, F., & Gajate, C. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13050763 · Cited by 21 · see citing works
Delahunty, I. M., Li, J., Jiang, W., Lee, C., Yang, X., Kumar, A., Liu, Z., Zhang, W., & Xie, J. (2022) · Small · doi:10.1002/smll.202200710 · Cited by 20 · see citing works
The central role of mitochondrial metabolism in hepatic steatosis
Win, S., Than, T. A., Kaplowitz, N., Wong, N., Arya, A., Win, Z. T., Win, S. H., Phyu, E., Kuemerle, C., Suh, J., et al. (2024) · Exploration of Digestive Diseases · doi:10.37349/edd.2024.00039 · Cited by 18 · see citing works
Chiu, Y.-C., Chu, P.-W., Lin, H.-C., & Chen, S.-K. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101166 · Cited by 18 · see citing works
Moreira, B. P., Monteiro, M. P., Sousa, M., Oliveira, P. F., & Alves, M. G. (2018) · Biochemical Journal · doi:10.1042/bcj20180631 · Cited by 17 · see citing works
Eckert, G. P., Eckert, S. H., Eckmann, J., Hagl, S., Muller, W. E., & Friedland, K. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113286 · Cited by 17 · see citing works
Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases
Bogorodskiy, A. O., Okhrimenko, I. S., Burkatovskii, D., Jakobs, P., Maslov, I., Gordeliy, V., Dencher, N. A., Gensch, T., Voos, W., Altschmied, J., et al. (2021) · Cells · doi:10.3390/cells10123528 · Cited by 17 · see citing works
Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form
Cao, S., Yang, Y., He, L., Hang, Y., Yan, X., Shi, H., Wu, J., & Ouyang, Z. (2023) · Nature Communications · doi:10.1038/s41467-023-37851-9 · Cited by 16 · see citing works
Reproductive effects of pubertal exposure to neonicotinoid thiacloprid in immature male mice
Zou, Y., Zhang, L., Yue, M., Zou, Z., Wu, X., Zhang, Q., Huang, Y., Zeng, S., Chen, C., & Gao, J. (2023) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2023.116629 · Cited by 16 · see citing works
Qu, S., Lin, H., Pfeiffer, N., & Grus, F. H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031624 · Cited by 16 · see citing works
Zhou, H., Huang, Y., Chen, C., Song, M., & Hylemon, P. B. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100120 · Cited by 15 · see citing works
Caveolin‐1 influences mitochondrial plasticity and function in hepatic stellate cell activation
Ilha, M., Martins, L. A. M., Moraes, K. D. S., Dias, C. K., Thomé, M. P. M., Petry, F. D. S., Rohden, F., Borojević, R., Trindade, V. M. T., Klamt, F., et al. (2022) · Cell Biology International · doi:10.1002/cbin.11876 · Cited by 14 · see citing works
Chewing the Fat with Microbes: Lipid Crosstalk in the Gut
Lemons, J. M. S., & Liu, L. (2022) · Nutrients · doi:10.3390/nu14030573 · Cited by 14 · see citing works
Refining a steroidogenic model: an analysis of RNA-seq datasets from insect prothoracic glands
Moulos, P., Αλεξανδράτος, Α., Nellas, I., & Dedos, S. (2018) · BMC Genomics · doi:10.1186/s12864-018-4896-2 · Cited by 14 · see citing works
Coleman, P. S., & Parlo, R. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.626316 · Cited by 14 · see citing works
PCSK9 Regulates Cardiac Mitochondrial Cholesterol by Promoting TSPO Degradation
Laudette, M., Lindbom, M., Cinato, M., Bergh, P., Skålén, K., Arif, M., Miljanovic, A., Czuba, T., Perkins, R., Smith, J. G., et al. (2025) · Circulation Research · doi:10.1161/circresaha.124.325629 · Cited by 12 · see citing works
Flis, D. J., Olek, R. A., Kaczor, J. J., Rodziewicz-Flis, E. A., Hałoń, M., Antosiewicz, J., Woźniak, M., Gabbianelli, R., & Ziółkowski, W. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3620929 · Cited by 12 · see citing works
Hepatic Mitochondrial Dysfunction and Risk of Liver Disease in an Ovine Model of “PCOS Males”
Siemienowicz, K. J., Filis, P., Thomas, J. L., Fowler, P., Duncan, W. C., & Rae, M. T. (2022) · Biomedicines · doi:10.3390/biomedicines10061291 · Cited by 12 · see citing works
Nanoparticle-Mediated Routing of Antibiotics into Mitochondria in Cancer Cells
Bajpai, A., Desai, N. N., Pandey, S., Shukla, C., Datta, B., & Basu, S. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c00527 · Cited by 11 · see citing works
Prokaryotic and Mitochondrial Lipids: A Survey of Evolutionary Origins
Rappocciolo, E., & Stiban, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-21162-2_2 · Cited by 10 · see citing works
Mitochondrial Diabetes Is Associated with the ND4 G11696A Mutation
Ding, Y., Zhang, S., Guo, Q., & Leng, J. (2023) · Biomolecules · doi:10.3390/biom13060907 · Cited by 10 · see citing works
Crockett, A. M., Colόn, M. C. V., Kébir, H., Smith, F. M., Iascone, D. M., Ciesielski, B., Кошкин, С. А., Patterson, A. D., Rossano, A. J., Sehgal, A., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.ads2116 · Cited by 10 · see citing works
Specific cellular microenvironments for spatiotemporal regulation of StAR and steroid synthesis
Castillo, A. F., Poderoso, C., Maloberti, P. M., Maciel, F. C., Garcia, M. M. M. S., Orlando, U. D., Mele, P. G., Benzo, Y., Dattilo, M. A., Prada, J. G., et al. (2024) · Journal of Endocrinology · doi:10.1530/joe-23-0391 · Cited by 9 · see citing works
Hsu, J., Leu, W., Zhong, N., & Guh, J. (2021) · Molecules · doi:10.3390/molecules26195967 · Cited by 9 · see citing works
Quo vadis PGRMC? Grand-Scale Biology in Human Health and Disease
Cahill, M. A. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2711318 · Cited by 8 · see citing works
SQLE drives bladder cancer progression by boosting mitochondrial oxidative phosphorylation
Dong, Y., Jiang, X., Yang, X., Zhang, J., Fu, Q., Zhou, Y., Xun, Y., Fu, Y., Hou, Y., Li, M., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03626-3 · Cited by 7 · see citing works
Bezerra, A. F., Alves, J. P. M., Fernandes, C. C. L., Cavalcanti, C. M., Silva, M. R. L., Conde, A. J. H., Tetaping, G. M., Ferreira, A. C. A., Melo, L. M., Rodrigues, A. P. R., et al. (2022) · Veterinary Research Communications · doi:10.1007/s11259-022-09995-4 · Cited by 6 · see citing works
Mycobacterial infection alters host mitochondrial activity
Mohareer, K., & Banerjee, S. (2023) · International review of cytology · doi:10.1016/bs.ircmb.2023.01.007 · Cited by 7 · see citing works
Advances in understanding of the oxysterol-binding protein homologous in yeast and filamentous fungi
Qiu, S., & Zeng, B. (2019) · International Microbiology · doi:10.1007/s10123-019-00056-6 · Cited by 6 · see citing works
Panee, J., Pomozi, V., Franke, A. A., Saux, O. L., & Gerschenson, M. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.03.006 · Cited by 6 · see citing works
Yang, N. V., Rogers, S. W., Guerra, R. M., Pagliarini, D. J., Theusch, E., & Krauss, R. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.24.546411 · Cited by 6 · see citing works
Cholesterol metabolism and its role in type 2 diabetes mellitus development
Luo, G., Niu, M., Li, Y., Cui, N., Huang, S., & Yang, X. (2025) · Food, Nutrition and Health. · doi:10.1007/s44403-025-00025-0 · Cited by 5 · see citing works
Zhang, W., Jiang, Z., & Mi, K. (2025) · Cells · doi:10.3390/cells14120867 · Cited by 6 · see citing works
Garg, S., Swaminathan, V., Dhavala, S., Kiebish, M. A., Sarangarajan, R., & Narain, N. R. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.03.021 · Cited by 5 · see citing works
Profiling subcellular localization of nuclear-encoded mitochondrial gene products in zebrafish
Uszczyńska-Ratajczak, B., Sugunan, S., Kwiatkowska, M., Migdał, M., Sala, S. C., Sokòl, A. M., Winata, C. L., & Chacińska, A. (2022) · Life Science Alliance · doi:10.26508/lsa.202201514 · Cited by 5 · see citing works
A lipid in transit – the journey of cholesterol into the heart of mitochondrial research
Simmen, T., & Pellegrini, L. (2025) · Journal of Cell Science · doi:10.1242/jcs.263907 · Cited by 4 · see citing works
Li, L., & Wang, X. (2022) · Clinical and Translational Discovery · doi:10.1002/ctd2.121 · Cited by 4 · see citing works
Exploration of Digestive Diseases
(2022) · Exploration of Digestive Diseases · doi:10.37349/edd · Cited by 4 · see citing works
Kawatani, K., Baker, S. K., Yaeger, J. D. W., Anderson, R. H., Ren, Y., Li, Z., Bao, H., Han, X., Francis, K. R., & Kanekiyo, T. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf159 · Cited by 3 · see citing works
Chen, J., Chen, M., Hu, J., Wu, Z., Li, H., Li, W., He, F., Peng, C., Xu, Y., Huang, W., et al. (2025) · Journal of the American Heart Association · doi:10.1161/jaha.125.045554 · Cited by 3 · see citing works
- Authors
- Martin, L. A., Kennedy, B. E., & Karten, B.
- Affiliations
- Dalhousie University (CA)
- Corresponding author
- Karten, Barbara
- ORCID
- Karten, Barbara
- Venue
- Journal of Bioenergetics and Biomembranes
- Published
- 2014-11-26
- Volume
- 48
- Issue
- 2
- Pages
- 137-151
- ISSN
- 0145-479X (ISSN-L)
- 1573-6881
- OpenAlex
- W1993948951
- Cited by
- 128
- References
- 186
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 10 · 2023: 13 · 2022: 21 · 2021: 20 · 2020: 9 · 2019: 10 · 2018: 5 · 2017: 8 · 2016: 4 · 2015: 3 · 2014: 1
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Bioenergetics and Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- mitochondrial cholesterol, steroidogenic acute regulatory protein, mitochondria-associated ER membranes, lipid transfer proteins, mitochondrial function, oxysterols, bile acids, mitochondrial membrane
- MeSH terms
- Steroidogenic Acute Regulatory Protein, Animals, Biological Transport, Active, Cholesterol, Endoplasmic Reticulum, Humans, Mitochondria, Phosphoproteins, Mitochondrial Membranes
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