Loss of prohibitin membrane scaffolds impairs mitochondrial architecture and leads to tau hyperphosphorylation and neurodegeneration
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Fusion and fission of mitochondria maintain the functional integrity of mitochondria and protect against neurodegeneration, but how mitochondrial dysfunctions trigger neuronal loss remains ill-defined. Prohibitins form large ring complexes in the inner membrane that are composed of PHB1 and PHB2 subunits and are thought to function as membrane scaffolds. In Caenorhabditis elegans, prohibitin genes affect aging by moderating fat metabolism and energy production. Knockdown experiments in mammalian cells link the function of prohibitins to membrane fusion, as they were found to stabilize the dynamin-like GTPase OPA1 (optic atrophy 1), which mediates mitochondrial inner membrane fusion and cristae morphogenesis. Mutations in OPA1 are associated with dominant optic atrophy characterized by the progressive loss of retinal ganglion cells, highlighting the importance of OPA1 function in neurons. Here, we show that neuron-specific inactivation of Phb2 in the mouse forebrain causes extensive neurodegeneration associated with behavioral impairments and cognitive deficiencies. We observe early onset tau hyperphosphorylation and filament formation in the hippocampus, demonstrating a direct link between mitochondrial defects and tau pathology. Loss of PHB2 impairs the stability of OPA1, affects mitochondrial ultrastructure, and induces the perinuclear clustering of mitochondria in hippocampal neurons. A destabilization of the mitochondrial genome and respiratory deficiencies manifest in aged neurons only, while the appearance of mitochondrial morphology defects correlates with tau hyperphosphorylation in the absence of PHB2. These results establish an essential role of prohibitin complexes for neuronal survival in vivo and demonstrate that OPA1 stability, mitochondrial fusion, and the maintenance of the mitochondrial genome in neurons depend on these scaffolding proteins. Moreover, our findings establish prohibitin-deficient mice as a novel genetic model for tau pathologies caused by a dysfunction of mitochondria and raise the possibility that tau pathologies are associated with other neurodegenerative disorders caused by deficiencies in mitochondrial dynamics.
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Inactivation of PHB-2 in mice brain affects mitochondrial structure and activity resulting in neurodegeneration by hyperphosphorylation of Tau.
“inactivation of PHB-2 in mice brain affects mitochondrial structure and activity resulting in neurodegeneration by hyperphosphorylation of Tau (Merkwirth et al., 2012)”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Merkwirth et al., 2012
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Cites
Generalized lacZ expression with the ROSA26 Cre reporter strain
Soriano, P. (1999) · Nature Genetics · doi:10.1038/5007 · Cited by 5,237 · see citing works
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734 · see citing works
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066 · see citing works
Mitochondrial fragmentation in neurodegeneration.
Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002 · see citing works
Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 839 · see citing works
Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826 · see citing works
Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 818 · see citing works
Essential Role for TrkB Receptors in Hippocampus-Mediated Learning
Minichiello, L., Korte, M., Wolfer, D., Kühn, R., Unsicker, K., Cestari, V., Rossi-Arnaud, C., Lipp, H.-P., Bonhoeffer, T., & Klein, R. (1999) · Neuron · doi:10.1016/s0896-6273(00)80853-3 · Cited by 799 · see citing works
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works
Regulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1
Ehses, S., Lauria, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., Martinou, J., Westermann, B., Rugarli, E. I., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906084 · Cited by 570 · see citing works
Self-citationMitochondria: The Next (Neurode)Generation
Schon, E. A., & Przedborski, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.003 · Cited by 568 · see citing works
Song, W., Chen, J., Petrilli, A. M., Liot, G., Klinglmayr, E., Zhou, Y., Poquiz, P., Tjong, J., Pouladi, M. A., Hayden, M. R., et al. (2011) · Nature Medicine · doi:10.1038/nm.2313 · Cited by 556 · see citing works
Merkwirth, C., Dargazanli, S., Tatsuta, T., Geimer, S., Löwer, B., Wunderlich, F. T., von Kleist-Retzow, J., Waisman, A., Westermann, B., & Langer, T. (2008) · Genes & Development · doi:10.1101/gad.460708 · Cited by 519 · see citing works
Self-citationRegulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 467 · see citing works
Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459 · see citing works
Zhu, X.-W., Raina, A., Rottkamp, C., Aliev, G., Perry, G., Boux, H., & Smith, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00046.x · Cited by 440 · see citing works
Duvezin‐Caubet, S., Jagasia, R., Wagener, J., Hofmann, S., Trifunović, A., Hansson, A., Chomyn, A., Bauer, M. F., Attardi, G. M., Larsson, N., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606059200 · Cited by 431 · see citing works
The Layered Structure of Human Mitochondrial DNA Nucleoids
Bogenhagen, D. F., Rousseau, D. L., & Burke, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708444200 · Cited by 426 · see citing works
Mitochondrial quality control: a matter of life and death for neurons
Rugarli, E. I., & Langer, T. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.38 · Cited by 419 · see citing works
Self-citationThe SPFH domain-containing proteins: more than lipid raft markers
Browman, D., Hoegg, M. B., & Robbins, S. M. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.06.005 · Cited by 403 · see citing works
Prohibitins Regulate Membrane Protein Degradation by the m -AAA Protease in Mitochondria
Steglich, G., Neupert, W., & Langer, T. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3435 · Cited by 357 · see citing works
Self-citationFormation of Membrane-bound Ring Complexes by Prohibitins in Mitochondria
Tatsuta, T., Model, K., & Langer, T. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-09-0807 · Cited by 345 · see citing works
Self-citationProhibitins and the functional compartmentalization of mitochondrial membranes
Osman, C., Merkwirth, C., & Langer, T. (2009) · Journal of Cell Science · doi:10.1242/jcs.037655 · Cited by 309 · see citing works
Self-citationReddy, P. H. (2011) · Brain Research · doi:10.1016/j.brainres.2011.07.052 · Cited by 300 · see citing works
An intimate liaison: spatial organization of the endoplasmic reticulum–mitochondria relationship
de Brito, O. M., & Scorrano, L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.177 · Cited by 297 · see citing works
Tiveron, M.-C., Hirsch, M., & Brunet, J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-23-07649.1996 · Cited by 295 · see citing works
Osman, C., Haag, M., Potting, C., Rodenfels, J., Dip, P. V., Wieland, F., Brügger, B., Westermann, B., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810189 · Cited by 295 · see citing works
Self-citationAbnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 289 · see citing works
Prohibitin and mitochondrial biology
Artal‐Sanz, M., & Tavernarakis, N. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.04.004 · Cited by 285 · see citing works
Microtubule-Associated Protein Tau
Yen, S.-H. C., Nacharaju, P., Ko, L., Kenessey, Á., & Liu, W.-K. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50012-9 · Cited by 284 · see citing works
Tavernarakis, N., Driscoll, M., & Kyrpides, N. C. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01467-x · Cited by 260 · see citing works
Pierson, T. M., Adams, D. R., Bonn, F., Martinelli, P., Cherukuri, P. F., Teer, J. K., Hansen, N. F., Cruz, P., Mullikin, J. C., Blakesley, R. W., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002325 · Cited by 226 · see citing works
Self-citationPhysiological functions of mitochondrial fusion
Chen, H., & Chan, D. C. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05615.x · Cited by 221 · see citing works
Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
Ittner, L. M., Fath, T., Ke, Y. D., Bi, M., van Eersel, J., Li, K. M., Gunning, P. W., & Götz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808084105 · Cited by 219 · see citing works
Artal‐Sanz, M., Tsang, W. Y., Willems, E., Grivell, L. A., Lemire, B. D., van der Spek, H., & Nijtmans, L. G. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304877200 · Cited by 219 · see citing works
Kasashima, K., Ohta, E., Kagawa, Y., & Endo, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605260200 · Cited by 208 · see citing works
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206 · see citing works
Schleicher, M., Shepherd, B. R., Suárez, Y., Fernandez-Hernando, C. F., Yu, J. Q., Pan, Y., Acevedo, L. M., Shadel, G. S., & Sessa, W. C. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200706072 · Cited by 204 · see citing works
Prohibitin couples diapause signalling to mitochondrial metabolism during ageing in C. elegans
Artal-Sanz, M., & Tavernarakis, N. (2009) · Nature · doi:10.1038/nature08466 · Cited by 196 · see citing works
Ferreira, A., Lu, Q., Orecchio, L., & Kosik, K. S. (1997) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1997.0615 · Cited by 178 · see citing works
Human prohibitin 1 maintains the organization and stability of the mitochondrial nucleoids
Kasashima, K., Sumitani, M., Satoh, M., & Endo, H. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.01.005 · Cited by 141 · see citing works
Marine Natural Product Aurilide Activates the OPA1-Mediated Apoptosis by Binding to Prohibitin
Sato, S., Murata, A., Orihara, T., Shirakawa, T., Suenaga, K., Kigoshi, H., & Uesugi, M. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.10.017 · Cited by 125 · see citing works
Characterization of OPA1 isoforms isolated from mouse tissues
Akepati, V. R., Müller, E., Otto, A., Strauss, H. M., Portwich, M., & Alexander, C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05401.x · Cited by 114 · see citing works
Park, S.-E., Xu, J., Frolova, A. I., Liao, L., O’Malley, B. W., & Katzenellenbogen, B. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1989-1999.2005 · Cited by 99 · see citing works
Birner‐Gruenberger, R., Nebauer, R., Schneiter, R., & Daum, G. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-05-0263 · Cited by 96 · see citing works
Zhou, P., Qian, L., D’Aurelio, M., Cho, S., Wang, G., Manfredi, G., Pickel, V. M., & Iadecola, C. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2849-11.2012 · Cited by 79 · see citing works
Piechota, J., Kołodziejczak, M., Juszczak, I., Sakamoto, W., & Jańska, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063644 · Cited by 72 · see citing works
George, S. K., Jiao, Y., Bishop, C. E., & Lu, B. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00686.x · Cited by 66 · see citing works
Martinelli, P., Mattina, V. L., Bernacchia, A., Magnoni, R., Cerri, F., Cox, G. A., Quattrini, A., Casari, G., & Rugarli, E. I. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp124 · Cited by 65 · see citing works
Self-citationOpposing function of mitochondrial prohibitin in aging
Artal‐Sanz, M., & Tavernarakis, N. (2010) · Aging · doi:10.18632/aging.100246 · Cited by 25 · see citing works
Atypical tauopathy with massive involvement of the white matter
Giaccone, G., Marcon, G., Mangieri, M., Morbin, M., Rossi, G., Fetoni, V., Patriarca, C., Catania, M., Fede, G. D., & Tagliavini, F. (2008) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2007.00927.x · Cited by 24 · see citing works
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Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor
Wei, Y., Chiang, W., Sumpter, R., Mishra, P., & Levine, B. (2016) · Cell · doi:10.1016/j.cell.2016.11.042 · Cited by 853 · see citing works
Role of Cardiolipin in Mitochondrial Signaling Pathways
Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 433 · see citing works
OPA1 processing in cell death and disease – the long and short of it
MacVicar, T., & Langer, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.159186 · Cited by 420 · see citing works
Self-citationA cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death
Wang, X., & Chen, X. J. (2015) · Nature · doi:10.1038/nature14859 · Cited by 366 · see citing works
Mechanisms and roles of mitophagy in neurodegenerative diseases
Wang, Y., Liu, N., & Lu, B. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13140 · Cited by 214 · see citing works
Prohibitin Ligands in Cell Death and Survival: Mode of Action and Therapeutic Potential
Thuaud, F., Ribeiro, N., Nebigil, C. G., & Désaubry, L. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.02.006 · Cited by 209 · see citing works
Prohibitins: A Critical Role in Mitochondrial Functions and Implication in Diseases
Signorile, A., Sgaramella, G., Bellomo, F., & Rasmo, D. D. (2019) · Cells · doi:10.3390/cells8010071 · Cited by 209 · see citing works
Richter‐Dennerlein, R., Korwitz, A., Haag, M., Tatsuta, T., Dargazanli, S., Baker, M., Decker, T., Lamkemeyer, T., Rugarli, E. I., & Langer, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.016 · Cited by 200 · see citing works
Self-citationMultifaceted role of prohibitin in cell survival and apoptosis
Peng, Y., Chen, P., Ouyang, R., & Song, L. (2015) · APOPTOSIS · doi:10.1007/s10495-015-1143-z · Cited by 195 · see citing works
Prohibitin 2: At a communications crossroads
Bavelloni, A., Piazzi, M., Raffini, M., Faenza, I., & Blalock, W. L. (2015) · IUBMB Life · doi:10.1002/iub.1366 · Cited by 167 · see citing works
Signaling networks determining life span
Riera, C. E., Merkwirth, C., De Magalhaes Filho, C. D., & Dillin, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014451 · Cited by 161 · see citing works
Self-citationThe Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160 · see citing works
Molecular mechanisms underlying genotype‐dependent responses to dietary restriction
Schleit, J., Johnson, S. C., Bennett, C. F., Simko, M., Trongtham, N., Castanza, A., Hsieh, E. J., Moller, R. M., Wasko, B. M., Delaney, J. R., et al. (2013) · Aging Cell · doi:10.1111/acel.12130 · Cited by 159 · see citing works
TDP-43 interacts with mitochondrial proteins critical for mitophagy and mitochondrial dynamics
Davis, S. A., Itaman, S., Janney, C., Sherard, J. A., Dowell, J. A., Cairns, N. J., & Gitcho, M. A. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.04.053 · Cited by 159 · see citing works
Shaping the mitochondrial inner membrane in health and disease
Colina-Tenorio, L., Horten, P., Pfanner, N., & Rampelt, H. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13031 · Cited by 151 · see citing works
Cannabidiol (CBD) Is a Novel Inhibitor for Exosome and Microvesicle (EMV) Release in Cancer
Kosgodage, U. S., Mould, R. R., Henley, A. B., Nunn, A. V. W., Guy, G. W., Thomas, E. L., Inal, J. M., Bell, J. D., & Lange, S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00889 · Cited by 144 · see citing works
Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria
Korwitz, A., Merkwirth, C., Richter‐Dennerlein, R., Tröder, S. E., Sprenger, H., Quirós, P. M., López-Otı́n, C., Rugarli, E. I., & Langer, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201507022 · Cited by 138 · see citing works
Self-citationMolecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease
Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135 · see citing works
Briston, T., & Hicks, A. R. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180025 · Cited by 129 · see citing works
Barbero‐Camps, E., Fernández, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 127 · see citing works
Ma, H., Jiang, T., Tang, W., Ma, Z., Pu, K., Xu, F., Chang, H., Zhao, G., Gao, W., Li, Y., et al. (2020) · Clinical Science · doi:10.1042/cs20200530 · Cited by 111 · see citing works
Respiratory supercomplexes: structure, function and assembly
Vartak, R. S., Porras, C. A.-M., & Bai, Y. (2013) · Protein & Cell · doi:10.1007/s13238-013-3032-y · Cited by 104 · see citing works
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103 · see citing works
“Moreover, inactivation of PHB-2 in mice brain affects mitochondrial structure and activity resulting in neurodegeneration by hyperphosphorylation of Tau (Merkwirth et al., 2012) or alters beta-cell function in pancreas producing diabetes (Supale et al., 2013).”
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Chowdhury, I., Thompson, W. E., & Thomas, K. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24531 · Cited by 97 · see citing works
Yoshinaka, T., Kosako, H., Yoshizumi, T., Furukawa, R., Hirano, Y., Kuge, O., Tamada, T., & Koshiba, T. (2019) · iScience · doi:10.1016/j.isci.2019.08.056 · Cited by 96 · see citing works
Lachén‐Montes, M., González-Morales, A., Zelaya, M. V., Pérez‐Valderrama, E., Ausín, K., Ferrer, I., Fernández‐Irigoyen, J., & Santamaría, E. (2017) · Scientific Reports · doi:10.1038/s41598-017-09481-x · Cited by 95 · see citing works
Yang, J., Li, B., & He, Q. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0661-3 · Cited by 95 · see citing works
Supale, S., Thorel, F., Merkwirth, C., Gjinovci, A., Herrera, P. L., Scorrano, L., Meda, P., Langer, T., & Maechler, P. (2013) · Diabetes · doi:10.2337/db13-0152 · Cited by 94 · see citing works
Self-citationOPA1 functionally interacts with MIC60 but is dispensable for crista junction formation
Barrera, M., Koob, S., Dikov, D., Vogel, F., & Reichert, A. S. (2016) · FEBS Letters · doi:10.1002/1873-3468.12384 · Cited by 94 · see citing works
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Valdés‐Tovar, M., Rodríguez‐Ramírez, A. M., Rodríguez-Cárdenas, L., Sotelo-Ramírez, C. E., Camarena, B., Sanabrais‐Jiménez, M. A., Solís‐Chagoyán, H., Argueta, J., & López-Riquelme, G. O. (2022) · World Journal of Psychiatry · doi:10.5498/wjp.v12.i2.264 · Cited by 93 · see citing works
Chicco, A. J., Le, C. H., Gnaiger, E., Dreyer, H. C., Muyskens, J. B., D’Alessandro, A., Nemkov, T. G., Hocker, A. D., Prenni, J. E., Wolfe, L. M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000470 · Cited by 88 · see citing works
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Campello, S., Strappazzon, F., & Cecconi, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.11.010 · Cited by 83 · see citing works
Mitochondrial Quality Control Mechanisms and the PHB (Prohibitin) Complex
Hernando‐Rodríguez, B., & Artal‐Sanz, M. (2018) · Cells · doi:10.3390/cells7120238 · Cited by 83 · see citing works
Inhibition of insulin/IGF‐1 receptor signaling protects from mitochondria‐mediated kidney failure
Ising, C., Koehler, S., Brähler, S., Merkwirth, C., Höhne, M., Baris, O. R., Hagmann, H., Kann, M., Fabretti, F., Dafinger, C., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404916 · Cited by 81 · see citing works
Self-citationKondadi, A. K., Wang, S., Montagner, S., Kladt, N., Korwitz, A., Martinelli, P., Herholz, D., Baker, M. J., Schauss, A. C., Langer, T., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201387009 · Cited by 81 · see citing works
Self-citationGenetic evidence for common pathways in human age‐related diseases
Johnson, S. C., Dong, X., Vijg, J., & Suh, Y. (2015) · Aging Cell · doi:10.1111/acel.12362 · Cited by 78 · see citing works
In situ architecture of Opa1-dependent mitochondrial cristae remodeling
Fry, M. Y., Navarro, P. P., Hakim, P., Ananda, V. Y., Qin, X., Landoni, J. C., Rath, S. P., Inde, Z., Lugo, C. M., Luce, B. E., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00027-2 · Cited by 72 · see citing works
Prohibitin 2 deficiency impairs cardiac fatty acid oxidation and causes heart failure
Wu, D., Jian, C., Peng, Q., Hou, T., Wu, K., Shang, B., Zhao, M., Wang, Y., Zheng, W. L., Ma, Q., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2374-7 · Cited by 68 · see citing works
Prohibitin levels regulate OMA1 activity and turnover in neurons
Anderson, C. J., Kahl, A., Fruitman, H., Qian, L., Zhou, P., Manfredi, G., & Iadecola, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0469-4 · Cited by 62 · see citing works
Non-classical ferroptosis inhibition by a small molecule targeting PHB2
Yang, W. P., Mu, B., You, J., Tian, C., Bin, H., Xu, Z., Zhang, L., Ma, R., Wu, M., Zhang, G., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35294-2 · Cited by 62 · see citing works
Gureev, A. P., Sadovnikova, I. S., Starkov, N. N., Starkov, A. A., & Popov, V. N. (2020) · Brain Sciences · doi:10.3390/brainsci10110847 · Cited by 61 · see citing works
Control of mitochondrial integrity in ageing and disease
Szklarczyk, R., Nooteboom, M., & Osiewacz, H. D. (2014) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2013.0439 · Cited by 61 · see citing works
Lachén‐Montes, M., González-Morales, A., de Morentin, X. M., Pérez‐Valderrama, E., Ausín, K., Zelaya, M. V., Serna, A., Aso, E., Ferrer, I., Fernández‐Irigoyen, J., et al. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.07.032 · Cited by 61 · see citing works
Mitophagy in aging and longevity
Guo, J., & Chiang, W. (2021) · IUBMB Life · doi:10.1002/iub.2585 · Cited by 58 · see citing works
Mitochondrial Chaperones in the Brain: Safeguarding Brain Health and Metabolism?
Castro, J. P., Wardelmann, K., Grune, T., & Kleinridders, A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00196 · Cited by 53 · see citing works
Mitochondrial Membrane Remodeling
Yang, Z., Wang, L., Yang, C., Pu, S., Guo, Z., Wu, Q., Zhou, Z., & Zhao, H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.786806 · Cited by 51 · see citing works
Zheng, J., Akbari, M., Schirmer, C., Reynaert, M., Loyens, A., Lefebvre, B., Buée, L., Croteau, D. L., Galas, M., & Bohr, V. A. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00896-8 · Cited by 51 · see citing works
mPOS is a novel mitochondrial trigger of cell death – implications for neurodegeneration
Coyne, L. P., & Chen, X. J. (2017) · FEBS Letters · doi:10.1002/1873-3468.12894 · Cited by 50 · see citing works
Mitochondrial Dynamics Imbalance: A Strategy for Promoting Viral Infection
Ren, Z., Zhang, X., Ding, T., Zhong, Z., Hu, H., Xu, Z., & Deng, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01992 · Cited by 50 · see citing works
Mitochondrial dysfunction in Alzheimer’s disease - a proteomics perspective
Abyadeh, M., Gupta, V., Chitranshi, N., Gupta, V., Wu, Y., Saks, D., Wall, R. V., Fitzhenry, M. J., Basavarajappa, D. K., You, Y., et al. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1918550 · Cited by 50 · see citing works
Liu, X., Ye, M., & Ma, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1022821 · Cited by 48 · see citing works
Li, L., Martin-Levilain, J., Jiménez‐Sánchez, C., Karaca, M., Foti, M., Martinou, J., & Maechler, P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007601 · Cited by 48 · see citing works
Mitochondrial protein dysfunction in pathogenesis of neurological diseases
Wang, L., Yang, Z., He, X., Pu, S., Yang, C., Wu, Q., Zhou, Z., Cen, X., & Zhao, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.974480 · Cited by 46 · see citing works
Schweingruber, C., Nijssen, J., Mechtersheimer, J., Reber, S., Lebœuf, M., O’Brien, N. L., Mei, I., Hedges, E. C., Keuper, M., Benitez, J. A., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59679-1 · Cited by 43 · see citing works
Therapeutic Targeting of Casein Kinase 1δ/ε in an Alzheimer’s Disease Mouse Model
Adler, P., Mayne, J., Walker, K., Ning, Z., & Figeys, D. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00312 · Cited by 43 · see citing works
Samluk, Ł., Ostapczuk, P., & Dziembowska, M. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-11-0553 · Cited by 41 · see citing works
Moncunill‐Massaguer, C., Saura‐Esteller, J., Pérez‐Perarnau, A., Palmeri, C. M., Núñez‐Vázquez, S., Cosialls, A. M., González‐Gironès, D. M., Pomares, H., Korwitz, A., Preciado, S., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6154 · Cited by 38 · see citing works
Self-citationGamberi, T., Massai, L., Magherini, F., Landini, I., Fiaschi, T., Scaletti, F., Gabbiani, C., Bianchi, L., Bini, L., Nobili, S., et al. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.03.032 · Cited by 37 · see citing works
RNA-Binding Proteins Implicated in Mitochondrial Damage and Mitophagy
Ravanidis, S., & Doxakis, E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00372 · Cited by 36 · see citing works
Jia, Y., Wang, M., Mao, C., Yu, F., Wang, Y., Xiao, R., Jiang, C., Zheng, L., Xu, Q., Zheng, M., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0703-x · Cited by 35 · see citing works
Consequences of inner mitochondrial membrane protein misfolding
Coyne, L. P., & Chen, X. J. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.001 · Cited by 34 · see citing works
Curcumin: Novel Treatment in Neonatal Hypoxic-Ischemic Brain Injury
Rocha‐Ferreira, E., Sisa, C., Bright, S., Fautz, T., Harris, M., Ingrid, C. R., Agwu, C., Tugce, K., Mistry, B., Hill, D., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01351 · Cited by 34 · see citing works
Essential Protein PHB2 and Its Regulatory Mechanisms in Cancer
Qi, A., Lamont, L., Liu, E., Murray, S., Meng, X., & Yang, S. (2023) · Cells · doi:10.3390/cells12081211 · Cited by 32 · see citing works
Prohibitin in Adipose and Immune Functions
Ande, S. R., Nguyen, K. H., Nyomba, B. L. G., & Mishra, S. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.05.003 · Cited by 32 · see citing works
Guyot, A.-C., Leuxe, C., Disdier, C., Oumata, N., Costa, N., Roux, G. L., Varela, P. F., Duchon, A., Charbonnier, J., Hérault, Y., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-57560-3 · Cited by 32 · see citing works
Stress vulnerability shapes disruption of motor cortical neuroplasticity
Gellner, A., Sitter, A., Rackiewicz, M., Sylvester, M., Philipsen, A., Zimmer, A., & Stein, V. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-01855-8 · Cited by 32 · see citing works
Kurinami, H., Shimamura, M., Ma, T., Qian, L., Koizumi, K., Park, L., Klann, E., Manfredi, G., Iadecola, C., & Zhou, P. (2014) · Stroke · doi:10.1161/strokeaha.113.003577 · Cited by 31 · see citing works
Human Rights Here and Now: Celebrating the Universal Declaration of Human Rights.
Flowers, N. B. (1998) · Cited by 31 · see citing works
Gao, H., Chen, Z., Fu, Y., Yang, X., Weng, R., Wang, R., Lu, J., Pan, M., Jin, K., McElroy, C., et al. (2016) · Scientific Reports · doi:10.1038/srep34403 · Cited by 30 · see citing works
Cardiolipin remodeling in Barth syndrome and other hereditary cardiomyopathies
Bertero, E., Kutschka, I., Maack, C., & Dudek, J. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165803 · Cited by 30 · see citing works
Rossi, L., Bonuccelli, L., Iacopetti, P., Evangelista, M., Ghezzani, C., Tana, L., & Salvetti, A. (2014) · Stem Cell Reviews and Reports · doi:10.1007/s12015-014-9540-1 · Cited by 30 · see citing works
Tortelli, T. C., de Godoy, L. M. F., de Souza, G. A., Bonatto, D., Otake, A. H., Saito, R. D. F., Rosa, J. C., Greene, L. J., & Chammas, R. J. (2017) · Oncotarget · doi:10.18632/oncotarget.17810 · Cited by 29 · see citing works
CHCHD10 and SLP2 control the stability of the PHB complex: a key factor for motor neuron viability
Genin, E. C., Bannwarth, S., Ropert, B., Lespinasse, F., Mauri-Crouzet, A., Augé, G., Fragaki, K., Cochaud, C., Donnarumma, E., Lacas‐Gervais, S., et al. (2022) · Brain · doi:10.1093/brain/awac197 · Cited by 28 · see citing works
Prohibitin – At the crossroads of obesity-linked diabetes and cancer
Mishra, S., & Nyomba, B. L. G. (2017) · Experimental Biology and Medicine · doi:10.1177/1535370217703976 · Cited by 28 · see citing works
An Unusual Prohibitin Regulates Malaria Parasite Mitochondrial Membrane Potential
Matz, J. M., Goosmann, C., Matuschewski, K., & Kooij, T. W. A. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.088 · Cited by 28 · see citing works
Agrawal, S., & Fox, J. H. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.03.004 · Cited by 28 · see citing works
Inner mitochondrial membrane protein Prohibitin 1 mediates Nix-induced, Parkin-independent mitophagy
Alula, K. M., Delgado‐Deida, Y., Callahan, R. C., Till, A., Underwood, L., Thompson, W. E., Souza, R. F., Dassopoulos, T., Onyiah, J. C., Venuprasad, K., et al. (2023) · Scientific Reports · doi:10.1038/s41598-022-26775-x · Cited by 27 · see citing works
Role of Prohibitins in Aging and Therapeutic Potential Against Age-Related Diseases
Belser, M., & Walker, D. W. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.714228 · Cited by 26 · see citing works
Hernando‐Rodríguez, B., Erinjeri, A. P., Rodríguez‐Palero, M. J., Millar, V., González-Hernández, S., Olmedo, M., Schulze, B., Baumeister, R., Muñoz, M. J., Askjaer, P., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0496-5 · Cited by 26 · see citing works
Iommarini, L., Peralta, S., Torraco, A., & Díaz, F. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.01.008 · Cited by 25 · see citing works
Hernando‐Rodríguez, B., Hernando‐Rodríguez, B., Rodríguez-Palero, M., Pla, A., Martínez‐Bueno, M. D., Pla, A., Gatsi, R., & Artal‐Sanz, M. (2021) · Aging Cell · doi:10.1111/acel.13359 · Cited by 25 · see citing works
Mechanism of progression of diabetic kidney disease mediated by podocyte mitochondrial injury
Su, J., Ye, D., Gao, C., Huang, Q., & Gui, D. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05749-0 · Cited by 24 · see citing works
Qu, Y., Konràd, C., Anderson, C. J., Qian, L., Yin, T., Manfredi, G., Iadecola, C., & Zhou, P. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1804-19.2020 · Cited by 23 · see citing works
OMA1—An integral membrane protease?
Alavi, M. V. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140558 · Cited by 22 · see citing works
Chang, C., Chang, Y., Chuang, P., Nguyen, T. N. A., Wu, K.-C., Chou, F.-Y., Cheng, S., Chen, H., Jin, L., Carvalho, K., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01213-7 · Cited by 22 · see citing works
Chen, Y., Qin, Q., Zhao, W., Luo, D., Huang, Y., Liu, G., Kuang, Y., Cao, Y., & Chen, Y. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c02665 · Cited by 22 · see citing works
Mitophagy and iron: two actors sharing the stage in age-associated neuronal pathologies
Schiavi, A., Strappazzon, F., & Ventura, N. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111252 · Cited by 21 · see citing works
Han, B., Chen, H., Yao, Y., Liu, X., Nie, C., Min, J., Zeng, Y., & Lutz, M. W. (2020) · Scientific Reports · doi:10.1038/s41598-020-75446-2 · Cited by 21 · see citing works
Structures of human organellar SPFH protein complexes
Gao, J., Sherpa, D., Kupko, N., Chino, H., Zeng, J., & Shao, S. (2025) · Nature Communications · doi:10.1038/s41467-025-65078-3 · Cited by 20 · see citing works
Targeting Mitochondrial Protein Expression as a Future Approach for Cancer Therapy
Criscuolo, D., Avolio, R., Matassa, D. S., & Esposito, F. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.797265 · Cited by 20 · see citing works
Guedouari, H., Amer, Y. O., Pichaud, N., & Hébert-Chatelain, É. (2021) · Mitochondrion · doi:10.1016/j.mito.2020.12.012 · Cited by 19 · see citing works
Mitochondrial prohibitin and its ubiquitination during crayfish Procambarus clarkii spermiogenesis
Dong, W., Hou, C.-C., & Yang, W. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-2044-0 · Cited by 18 · see citing works
Kong, B., Han, C. Y., Kim, S. I., Patten, D. A., Han, Y., Carmona, E., Shieh, D., Cheung, A. C., Mes‐Masson, A., Harper, M., et al. (2022) · Journal of Ovarian Research · doi:10.1186/s13048-022-00999-x · Cited by 17 · see citing works
Cantor, R. M., Navarro, L., Won, H., Walker, R. L., Lowe, J. K., & Geschwind, D. H. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.114 · Cited by 17 · see citing works
Guo, S.-D., Yan, S., Li, W., Zhou, H., Yang, J., Yao, Y., Shen, M.-J., Zhang, L., Zhang, H., & Sun, L.-C. (2020) · Aging · doi:10.18632/aging.102964 · Cited by 17 · see citing works
Brekk, O. R., Makridakis, M., Mavroeidi, P., Vlahou, A., Xilouri, M., & Stefanis, L. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.12.006 · Cited by 16 · see citing works
van Gastel, J., Leysen, H., Santos‐Otte, P., Hendrickx, J. O., Azmi, A., Martin, B., & Maudsley, S. R. (2019) · Aging · doi:10.18632/aging.102528 · Cited by 16 · see citing works
Prohibitin‐1 Is a Dynamically Regulated Blood Protein With Cardioprotective Effects in Sepsis
Mattox, T. A., Psaltis, C. E., Weihbrecht, K., Robidoux, J., Kilburg-Basnyat, B. J., Murphy, M. P., Gowdy, K. M., & Anderson, E. J. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.120.019877 · Cited by 16 · see citing works
Dynamic regulation of mitochondrial genome maintenance in germ cells
Kasashima, K., Nagao, Y., & Endo, H. (2013) · Reproductive Medicine and Biology · doi:10.1007/s12522-013-0162-0 · Cited by 16 · see citing works
The Mitochondrial Prohibitin (PHB) Complex in C. elegans Metabolism and Ageing Regulation
Lourenço, A. B., & Artal‐Sanz, M. (2021) · Metabolites · doi:10.3390/metabo11090636 · Cited by 15 · see citing works
- Authors
- Merkwirth, C., Martinelli, P., Korwitz, A., Morbin, M., Brönneke, H. S., Jordan, S. D., Rugarli, E. I., & Langer, T.
- Affiliations
- University of Cologne (DE)
- Fondazione IRCCS Istituto Neurologico Carlo Besta (IT)
- Corresponding author
- Langer, Thomas
- ORCID
- Venue
- PLoS Genetics
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-11-08
- Volume
- 8
- Issue
- 11
- Pages
- e1003021
- ISSN
- 1553-7390 (ISSN-L)
- 1553-7404
- PMC
- PMC3493444
- OpenAlex
- W2005255392
- Cited by
- 162
- References
- 59
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 8 · 2023: 13 · 2022: 20 · 2021: 16 · 2020: 18 · 2019: 15 · 2018: 11 · 2017: 12 · 2016: 12 · 2015: 9 · 2014: 9 · 2013: 8
- FWCI
- 3.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Genetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Deutsche Forschungsgemeinschaft (SFB635, C4, 233078, SFB 635)
- FP7 Ideas: European Research Council (233078)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- prohibitin, PHB2, prohibitin 1, OPA1, mitochondrial fusion, mitochondrial fission, mitochondrial dynamics, tau hyperphosphorylation, neurodegeneration, hippocampal neurons, mitochondrial ultrastructure, mitochondrial genome stability, respiratory deficiency, neuronal aging, cognitive impairment, autosomal dominant optic atrophy
- MeSH terms
- Prohibitins, Animals, Membrane Fusion, Mitochondria, Morphogenesis, Neurons, Phosphorylation, Repressor Proteins, tau Proteins, Apoptosis, Neurodegenerative Diseases, Optic Atrophy, Autosomal Dominant, Caenorhabditis elegans Proteins, Mitochondrial Membranes, Mice, Genome, Mitochondrial
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