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Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
Open accessAbstract
Parkinson's disease (PD) is a common neurodegenerative disorder characterized by loss of dopaminergic neurons in the substantia nigra. Several lines of evidence strongly implicate mitochondrial dysfunction as a major causative factor in PD, although the molecular mechanisms responsible for mitochondrial dysfunction are poorly understood. Recently, loss-of-function mutations in the parkin gene, which encodes a ubiquitin-protein ligase, were found to underlie a familial form of PD known as autosomal recessive juvenile parkinsonism (AR-JP). To gain insight into the molecular mechanism responsible for selective cell death in AR-JP, we have created a Drosophila model of this disorder. Drosophila parkin null mutants exhibit reduced lifespan, locomotor defects, and male sterility. The locomotor defects derive from apoptotic cell death of muscle subsets, whereas the male sterile phenotype derives from a spermatid individualization defect at a late stage of spermatogenesis. Mitochondrial pathology is the earliest manifestation of muscle degeneration and a prominent characteristic of individualizing spermatids in parkin mutants. These results indicate that the tissue-specific phenotypes observed in Drosophila parkin mutants result from mitochondrial dysfunction and raise the possibility that similar mitochondrial impairment triggers the selective cell loss observed in AR-JP.
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“Conversely, reduction of mitophagy caused by the ablation of PINK and Parkin induces mitochondrial dysfunction and increased sensitivity to oxidative stress followed by muscle degeneration [225–228].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [225]
In the citing paper
“Both excessive autophagy [140, 186] and the deficient degradation of cytosolic components [225, 226] contribute to muscle atrophy.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [225]
In the citing paper
“whereas Parkin loss-of-function in Drosophila resulted in a decreased lifespan and increased locomotor defects [157,158].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [157]
In the citing paper
“Although there are conflicting data regarding the specific effects of these proteins on mitochondrial morphology in mammalian cells, extensive studies in Drosophila revealed that knocking out either gene caused muscle degeneration that was associated with enlarged mitochondria (Clark et al., 2006; Greene et al., 2003).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Greene et al., 2003
Citations
Cites
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Mitochondrial Complex I Deficiency in Parkinson's Disease
Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283
A Drosophila model of Parkinson's disease
Feany, M. Β., & Bender, W. W. (2000) · Nature · doi:10.1038/35006074 · Cited by 2,156
Self-citationFamilial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024
MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE
Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757
Nicklas, W. J., Vyas, I. L., & Heikkila, R. E. (1985) · Life Sciences · doi:10.1016/0024-3205(85)90146-8 · Cited by 1,273
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Shimura, H., Schlossmacher, M. G., Hattori, N., Frosch, M. P., Trockenbacher, A., Schneider, R., Mizuno, Y., Kosik, K. S., & Selkoe, D. J. (2001) · Science · doi:10.1126/science.1060627 · Cited by 1,053
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Woodall, B. P., Orogo, A. M., Najor, R. H., Cortez, M. Q., Moreno, E. R., Wang, H., Divakaruni, A. S., Murphy, A. N., & Gustafsson, Å. B. (2019) · JCI Insight · doi:10.1172/jci.insight.127713 · Cited by 55
Battaglia, G., Farrace, M. G., Mastroberardino, P. G., Viti, I., Fimia, G. M., BEEUMEN, J. V., Devreese, B. V., Melino, G., Molinaro, G., Busceti, C. L., et al. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04140.x · Cited by 59
Vincow, E. S., Thomas, R. E., Merrihew, G. E., Shulman, N. J., Bammler, T. K., MacDonald, J. W., MacCoss, M. J., & Pallanck, L. J. (2019) · Autophagy · doi:10.1080/15548627.2019.1586258 · Cited by 54
Self-citationKim, G. J., Mo, H., Liu, H., Wu, Z., Chen, S., Zheng, J., Zhao, X., Nucum, D., Shortland, J., Peng, L., et al. (2021) · eLife · doi:10.7554/elife.69795 · Cited by 49
Parkinson’s Disease: Exploring Different Animal Model Systems
Khan, E., Hasan, I., & Haque, M. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24109088 · Cited by 57
de Castro, I. P., Costa, A. C. O., Celardo, I., Tufi, R., Dinsdale, D. D., Loh, S. H. Y., & Martins, L. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.394 · Cited by 57
Yun, J.-W., Ahn, J.-B., & Kang, B.-C. (2015) · Laboratory Animal Research · doi:10.5625/lar.2015.31.4.155 · Cited by 53
Twenty years since the discovery of the parkin gene
Hattori, N., & Mizuno, Y. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1742-7 · Cited by 55
Potential Future Neuroprotective Therapies for Neurodegenerative Disorders and Stroke
Tarawneh, R. M., & Galvin, J. E. (2010) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2009.12.003 · Cited by 54
Martinez, A., Sánchez-Martínez, Á., Pickering, J. T., Twyning, M. J., Terriente-Félix, A., Chen, P., Chen, C., & Whitworth, A. J. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00701-3 · Cited by 54
Self-citationShim, J. H., Yoon, S. H., Kim, K., Han, J., Ha, J., Hyun, D. H., Paek, S. H., Kang, U. J., Zhuang, X., & Son, J. H. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.05.013 · Cited by 55
Mitochondrial Dynamics: An Emerging Paradigm in Ischemia-Reperfusion Injury
Calo, L., Dong, Y., Kumar, R., Przyklenk, K., & Sanderson, T. H. (2013) · Current Pharmaceutical Design · doi:10.2174/138161281939131127110701 · Cited by 53
Edens, B. M., Miller, N., & Ma, Y. C. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00044 · Cited by 52
Gurubaran, I. S., Viiri, J., Koskela, A. K. J., Hyttinen, J. M. T., Paterno, J. J., Kis, G. N., Antal, M., Urtti, A. O., Kauppinen, A., Felszeghy, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061976 · Cited by 52
Mitophagy and neurodegeneration
Wager, K., & Russell, C. (2013) · Autophagy · doi:10.4161/auto.25082 · Cited by 51
Slabbaert, J. R., Kuenen, S., Swerts, J., Maes, I., Uytterhoeven, V., Kasprowicz, J., Fernandes, A. C., Blust, R., & Verstreken, P. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3432-15.2016 · Cited by 50
Hwang, C. J., Kim, Y., Son, D. J., Park, M. H., Choi, D., Park, P., Hellström, M., Han, S., Oh, K., Park, E., et al. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.008 · Cited by 50
Aggarwal, A., Reichert, H., & VijayRaghavan, K. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1807456116 · Cited by 51
Value of genetic models in understanding the cause and mechanisms of Parkinson’s disease
Moore, D. J., & Dawson, T. M. (2008) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-008-0045-7 · Cited by 50
Protein stability and aggregation in Parkinson's disease
Robinson, P. A. (2008) · Biochemical Journal · doi:10.1042/bj20080295 · Cited by 50
Klein, R. L., Dayton, R. D., Henderson, K. M., & Petrucelli, L. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.03.001 · Cited by 50
Saini, N., Georgiev, O., & Schaffner, W. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05207-11 · Cited by 49
Yasuda, T., & Mochizuki, H. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0486-8 · Cited by 51
Vincent, A. J., Briggs, L., Chatwin, G. F. J., Emery, E., Tomlins, R., Oswald, M. C. W., Middleton, C. A., Evans, G. J., Sweeney, S. T., & Elliott, C. J. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr609 · Cited by 51
Eswari, S., & Naik, S. (2019) · Materials Science for Energy Technologies · doi:10.1016/j.mset.2019.10.011 · Cited by 49
Neurogenetics: Advancing the “Next-Generation” of Brain Research
Zoghbi, H. Y., & Warren, S. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.015 · Cited by 48
Andreazza, S., Samstag, C. L., Sánchez-Martínez, Á., Fernández‐Vizarra, E., Gómez-Durán, A., Lee, J. J., Tufi, R., Hipp, M. J., Schmidt, E. K., Nicholls, T. J. J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10857-y · Cited by 48
Self-citationKim, M., Semple, I. A., Kim, B. Y., Kiers, A., Nam, S., Park, H., Park, H., Ro, S., Kim, J.-S., Juhász, G., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1063766 · Cited by 48
Aβ43 is neurotoxic and primes aggregation of Aβ40 in vivo
Burnouf, S., Gorsky, M. K., Dols, J., Grönke, S., & Partridge, L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1419-y · Cited by 51
Haylett, W. L., Swart, C., van der Westhuizen, F. H., Dyk, H. C. V., van der Merwe, L., van der Merwe, C., Loos, B., Carr, J. A., Kinnear, C. J., & Bardien, S. (2016) · Parkinson s Disease · doi:10.1155/2016/1819209 · Cited by 49
Mitochondrial clearance: mechanisms and roles in cellular fitness
Onishi, M., & Okamoto, K. (2021) · FEBS Letters · doi:10.1002/1873-3468.14060 · Cited by 49
Schurr, E., Alcaïs, A., de Léséleuc, L., & Abel, L. (2006) · Seminars in Immunology · doi:10.1016/j.smim.2006.07.005 · Cited by 48
Zhu, J., Vereshchagina, N., Sreekumar, V., Burbulla, L. F., Costa, A. C., Daub, K. J., Woitalla, D., Martins, L. M., Krüger, R., & Rasse, T. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083714 · Cited by 49
Zinc supplement greatly improves the condition of parkin mutant Drosophila
Saini, N., & Schaffner, W. (2010) · Biological Chemistry · doi:10.1515/bc.2010.052 · Cited by 48
Bug22 influences cilium morphology and the post-translational modification of ciliary microtubules
Mendes Maia, T., Gogendeau, D., Pennetier, C., Janke, C., & Basto, R. (2014) · Biology Open · doi:10.1242/bio.20146577 · Cited by 47
Chib, S., & Singh, S. (2022) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2022.107124 · Cited by 47
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Hung, Y.-C., Huang, K.-L., Chen, P., Li, J., Lu, S. H.-A., Chang, J., Lin, H., Lo, W.-C., Huang, S., Lee, T., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109729 · Cited by 46
Adedara, A. O., Babalola, A. D., Stephano, F., Awogbindin, I. O., Olopade, J. O., da Rocha, J. B. T., Whitworth, A. J., & Abolaji, A. O. (2022) · Scientific Reports · doi:10.1038/s41598-022-07909-7 · Cited by 46
Self-citationAboud, A. A., Tidball, A. M., Kumar, K. K., Neely, M. D., Ess, K. C., Erikson, K. M., & Bowman, A. B. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.10.009 · Cited by 46
Integrin-mediated adhesion maintains sarcomeric integrity
Perkins, A., Ellis, S. J., Asghari, P., Shamsian, A., Moore, E. D. W., & Tanentzapf, G. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2009.10.034 · Cited by 51
Long, M., Sánchez-Martínez, Á., Longo, M., Suomi, F., Stenlund, H. C., Johansson, A. I., Ehsan, H., Salo, V. T., Montava‐Garriga, L., Naddafi, S., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021109390 · Cited by 48
Self-citationGenetic Mouse Models of Neurodegenerative Diseases
Trancikova, A. K., Ramonet, D., & Moore, D. J. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-384878-9.00012-1 · Cited by 47
Umeda‐Kameyama, Y., Tsuda, M., Ohkura, C., Matsuo, T., Namba, Y., Ohuchi, Y., & Aigaki, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700937200 · Cited by 46
Palin, E., Paetau, A. E., & Suomalainen, A. (2013) · Brain · doi:10.1093/brain/awt160 · Cited by 46
A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit
Rebelo‐Guiomar, P., Pellegrino, S., Dent, K. C., Sas‐Chen, A., Miller‐Fleming, L., Garone, C., Haute, L. V., Rogan, J. F., Dinan, A. M., Firth, A. E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28503-5 · Cited by 45
Self-citationSen, A., Kalvakuri, S., Bodmer, R., & Cox, R. T. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.019208 · Cited by 51
Deletion of endogenous Tau proteins is not detrimental in Drosophila
Burnouf, S., Grönke, S., Augustin, H., Dols, J., Gorsky, M. K., Werner, J. A., Kerr, F., Alic, N., Martinez, P., & Partridge, L. (2016) · Scientific Reports · doi:10.1038/srep23102 · Cited by 45
Autophagy in Mitochondrial Quality Control
Wang, R., & Wang, G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-0602-4_19 · Cited by 46
Serviddio, G., Romano, A. D., Cassano, T., Bellanti, F., Altomare, E., & Vendemiale, G. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796904740 · Cited by 45
Bonilla-Ramírez, L., Jiménez-Del-Río, M., & Velez‐Pardo, C. (2012) · Gene · doi:10.1016/j.gene.2012.09.120 · Cited by 45
Balance is the challenge – The impact of mitochondrial dynamics in Parkinson’s disease
Burbulla, L. F., Krebiehl, G., & Krüger, R. (2010) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2010.02354.x · Cited by 46
Knuppertz, L., & Osiewacz, H. D. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.01.003 · Cited by 44
Edenharter, O., Schneuwly, S., & Navarro, J. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00038 · Cited by 44
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Pacelli, C., Rotundo, G., Lecce, L., Menga, M., Bidollari, E., Scrima, R., Cela, O., Piccoli, C., Cocco, T., Vescovi, A. L., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112772 · Cited by 44
Edmunds, L. R., Xie, B., Mills, A. M., Huckestein, B. R., Undamatla, R., Murali, A., Pangburn, M. M., Martin, J. L., SIPULA, I. J., Kaufman, B. A., et al. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101051 · Cited by 45
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Jetto, C. T., Nambiar, A., & Manjithaya, R. R. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.837337 · Cited by 44
Decreasing pdzd8-mediated mito–ER contacts improves organismal fitness and mitigates Aβ 42 toxicity
Hewitt, V. L., Miller‐Fleming, L., Twyning, M. J., Andreazza, S., Mattedi, F., Prudent, J., Polleux, F., Vagnoni, A., & Whitworth, A. J. (2022) · Life Science Alliance · doi:10.26508/lsa.202201531 · Cited by 45
Self-citationDrosophila melanogaster: a fly through its history and current use
Stephenson, R. E., & Metcalfe, N. H. (2013) · The Journal of the Royal College of Physicians of Edinburgh · doi:10.4997/jrcpe.2013.116 · Cited by 44
Wang, Z.-H., Clark, C. P., & Geisbrecht, E. R. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw067 · Cited by 49
Mitophagy in Neurons: Mechanisms Regulating Mitochondrial Turnover and Neuronal Homeostasis
Basak, B., & Holzbaur, E. L. F. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169161 · Cited by 44
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Guo, M. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)84001-4 · Cited by 44
Yumnamcha, T., Roy, D., Devi, M. D., & Nongthomba, U. (2015) · Toxicological & Environmental Chemistry Reviews · doi:10.1080/02772248.2015.1093750 · Cited by 43
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Chen, Y., Deng, J., Wang, P., Yang, M., Chen, X., Zhu, L., Liu, J., Lu, B., Shen, Y., Fushimi, K., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw310 · Cited by 46
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Rita, A. D., Maiorino, T., Bruqi, K., Volpicelli, F., Bellenchi, G. C., & Strappazzon, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21010355 · Cited by 43
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Lee, F. J. S., & Liu, F. (2008) · Brain Research Reviews · doi:10.1016/j.brainresrev.2008.02.001 · Cited by 43
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Lavara-Culebras, E., Muñoz, V. F. L., Gómez‐Pastor, R., Matallana, E., & Paricio, N. (2010) · Gene · doi:10.1016/j.gene.2010.04.009 · Cited by 43
Pokrzywa, M., Dacklin, I., Hultmark, D., & Lundgren, E. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05728.x · Cited by 43
Pareek, G., Thomas, R. E., & Pallanck, L. J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0365-8 · Cited by 42
Self-citationShimura, T., & Kunugita, N. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1170271 · Cited by 42
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Zhang, Q., Chen, W.-L., Tan, S., & Lin, T. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.116 · Cited by 44
Thomas, R. E., Vincow, E. S., Merrihew, G. E., MacCoss, M. J., Davis, M. Y., & Pallanck, L. J. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007694 · Cited by 42
Self-citationMast, J. D., Tomalty, K. M. H., Vogel, H. S., & Clandinin, T. R. (2008) · Development · doi:10.1242/dev.020644 · Cited by 43
Włodarczyk, A., Sonakowska, L., Kamińska, K. Z., Marchewka, A., Wilczek, G., Wilczek, P., Student, S., & Rost-Roszkowska, M. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173563 · Cited by 41
Ali, Y., McCormack, R., Darr, A. J., & Zhai, R. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.219295 · Cited by 41
Parkin affects mitochondrial function and apoptosis in neuronal and myogenic cells
Kuroda, Y., Mitsui, T., Kunishige, M., & Matsumoto, T. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.201 · Cited by 41
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Koh, H., & Chung, J. (2012) · Molecules and Cells · doi:10.1007/s10059-012-0100-8 · Cited by 40
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Johnstone, K. L., Wells, R. E., Strutt, D. I., & Zeidler, M. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065076 · Cited by 40
Samstag, C. L., Hoekstra, J. G., Huang, C.-H., Chaisson, M., Youle, R. J., Kennedy, S. R., & Pallanck, L. J. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007805 · Cited by 42
Self-citationZhao, Y., Chen, F., Chen, S., Liu, X., Cui, M., & Dong, Q. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12340 · Cited by 39
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Ke, M., Chong, C., Zhu, Q., Zhang, K., Cai, C.-Z., Lu, J., Qin, D., & Su, H. (2021) · Aging and Disease · doi:10.14336/ad.2020.0331 · Cited by 41
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Xu, Z., Tito, A. J., Rui, Y., & Zhang, S. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.002 · Cited by 41
Kubo, S., Hattori, N., & Mizuno, Y. (2006) · Movement Disorders · doi:10.1002/mds.20841 · Cited by 39
Proteasome function is required to maintain muscle cellular architecture.
Haas, K. F., Woodruff, E., & Broadie, K. (2007) · Biology of the Cell · doi:10.1042/bc20070019 · Cited by 38
Zhu, M., Li, X., Tian, X., & Wu, C. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv081 · Cited by 39
Clausen, L., Okarmus, J., Voutsinos, V., Meyer, M., Lindorff‐Larsen, K., & Hartmann‐Petersen, R. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05262-8 · Cited by 43
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Valadas, J. S., Vos, M. H., & Verstreken, P. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12577 · Cited by 44
Rompuy, A. V., Lobbestael, E., der Perren, A. V., den Haute, C. V., & Baekelandt, V. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000039 · Cited by 38
Hwang, R., Wiemerslage, L., LaBreck, C. J., Khan, M. H., Kannan, K., Wang, X., Zhu, X., Lee, D., & Fridell, Y.-W. C. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.032 · Cited by 38
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Grenier, K., Kontogiannea, M., & Fon, E. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.607150 · Cited by 39
Holmbeck, M. A., Donner, J. R., Villa-Cuesta, E., & Rand, D. M. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.019323 · Cited by 39
Cortese, G. P., Zhu, M. J., Williams, D. J., Heath, S. L., & Waites, C. L. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1473-16.2016 · Cited by 38
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Metadata
- Authors
- Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J.
- Affiliations
- Brigham and Women's Hospital (US)
- Department of Genome Sciences, University of Washington, P.O. Box 357730, Seattle, WA 98195; and Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2003-03-17
- Volume
- 100
- Issue
- 7
- Pages
- 4078-4083
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC153051
- OpenAlex
- W2055124287
- Cited by
- 1,203
- References
- 34
- Citations by year
- 2026: 17 · 2025: 29 · 2024: 34 · 2023: 38 · 2022: 49 · 2021: 64 · 2020: 68 · 2019: 50 · 2018: 64 · 2017: 54 · 2016: 69 · 2015: 56 · 2014: 55 · 2013: 64 · 2012: 67
- FWCI
- 27.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01NS041780, 1R01NS41780-01, 1R01NS41536-01, R01NS041536)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- Parkin, Parkinson's disease, autosomal recessive juvenile parkinsonism, mitochondrial dysfunction, muscle degeneration, apoptosis, Drosophila model, ubiquitin-protein ligase, spermatid individualization, male sterility, locomotion defects, lifespan, selective cell death
- MeSH terms
- Amino Acid Sequence, Animals, Cloning, Molecular, Drosophila, Ligases, Longevity, Male, Mitochondria, Molecular Sequence Data, Nerve Degeneration, Parkinson Disease, Recombinant Proteins, Spermatids, Mutagenesis, Sequence Alignment, Apoptosis, Sequence Homology, Amino Acid, Muscle, Skeletal, Ubiquitin-Protein Ligases
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