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Mitochondrial dysfunction in Parkinson's disease
Open accessAbstract
Mitochondria are highly dynamic organelles which fulfill a plethora of functions. In addition to their prominent role in energy metabolism, mitochondria are intimately involved in various key cellular processes, such as the regulation of calcium homeostasis, stress response and cell death pathways. Thus, it is not surprising that an impairment of mitochondrial function results in cellular damage and is linked to aging and neurodegeneration. Many lines of evidence suggest that mitochondrial dysfunction plays a central role in the pathogenesis of Parkinson's disease (PD), starting in the early 1980s with the observation that an inhibitor of complex I of the electron transport chain can induce parkinsonism. Remarkably, recent research indicated that several PD-associated genes interface with pathways regulating mitochondrial function, morphology, and dynamics. In fact, sporadic and familial PD seem to converge at the level of mitochondrial integrity.
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“Recessively inherited loss-of-function mutations in PTEN-induced kinase 1 (PINK1) and the E3 ubiquitin ligase PRKN are the most common genetic causes for early-onset PD, which occurs in about 5%–10% of cases [1, 2].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [2]
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“Loss-of-function mutations in the genes encoding PINK1 and PRKN result in early-onset Parkinson disease (EOPD).”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [2]
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“α-Synuclein has been reported to cause dysfunction of mitochondrial complex I in PD which in turn increases levels of ROS and consequently ROS-induced oxidative stress (Winklhofer and Haass 2010).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Winklhofer and Haass 2010
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Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
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 Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis
Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914
α-Synuclein Locus Triplication Causes Parkinson's Disease
Singleton, A. B., Farrer, M., Johnson, J., Singleton, A., Hague, S., Kachergus, J., Hulihan, M., Peuralinna, T., Dutra, A., Nussbaum, R., et al. (2003) · Science · doi:10.1126/science.1090278 · Cited by 4,383
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
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Items 101–200 of 690
Wang, H., Chou, A.-H., Wu, A.-S., Chen, S.-Y., Weng, Y.-H., Kao, Y.-C., Yeh, T., Chu, P., & Lu, C.-S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.03.007 · Cited by 122
Mitochondrial defect and PGC-1α dysfunction in parkin-associated familial Parkinson's disease
Pacelli, C., Rasmo, D. D., Signorile, A., Grattagliano, I., Tullio, G. D., D’Orazio, A., Nico, B., Comi, G. P., Ronchi, D., Ferranini, E., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.022 · Cited by 119
GDNF–Ret signaling in midbrain dopaminergic neurons and its implication for Parkinson disease
Kramer, E. R., & Liss, B. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.11.006 · Cited by 121
Molecular Pathology of Lewy Body Diseases
Beyer, K., Domingo-Sàbat, M., & Ariza, A. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10030724 · Cited by 127
Bolaños, J. P., Moro, M. Á., Lizasoaín, I., & Almeida, Á. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.009 · Cited by 120
Cellular senescence in aging and age-related diseases: Implications for neurodegenerative diseases
(2020) · International Review of Neurobiology · doi:10.1016/bs.irn.2020.03.019 · Cited by 114
Rehman, M. U., Sehar, N., Dar, N. J., Khan, A., Arafah, A., Rashid, S., Rashid, S. M., & Ganaie, M. A. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104961 · Cited by 130
Masilamoni, G. J., Bogenpohl, J. W., Alagille, D., Delevich, K. M., Tamagnan, G. D., Votaw, J. R., Wichmann, T., & Smith, Y. (2011) · Brain · doi:10.1093/brain/awr137 · Cited by 118
Analysis of the mitochondrial proteome in multiple sclerosis cortex
Broadwater, L., Pandit, A., Clements, R. J., Azzam, S., Vadnal, J., Sulak, M. A., Yong, V. W., Freeman, E. J., Gregory, R. B., & McDonough, J. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.01.012 · Cited by 119
Dynamics of Human Mitochondrial Complex I Assembly: Implications for Neurodegenerative Diseases
Giachin, G., Bouverot, R., Acajjaoui, S., Pantalone, S., & Soler‐López, M. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00043 · Cited by 118
l-DOPA: A scapegoat for accelerated neurodegeneration in Parkinson's disease?
Lipski, J., Nisticò, R., Berretta, N., Guatteo, E., Bernardi, G., & Mercuri, N. B. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.06.005 · Cited by 120
Jana, S., Sinha, M. S., Chanda, D., Roy, T., Banerjee, K., Munshi, S., Patro, B. S., & Chakrabarti, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.02.013 · Cited by 115
Nrf2 activation by tauroursodeoxycholic acid in experimental models of Parkinson's disease
Moreira, S., Fonseca, I., Nunes, M. J., Rosa, A., Lemos, L., Rodrigues, E., Carvalho, A. N., Outeiro, T. F., Rodrigues, C. M. P., Gama, M. J., et al. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.009 · Cited by 112
The Yeast Complex I Equivalent NADH Dehydrogenase Rescues pink1 Mutants
Vilain, S., Esposito, G., Haddad, D., Schaap, O., Dobreva, M. P., Vos, M. H., Meensel, S. V., Morais, V. A., Strooper, B. D., & Verstreken, P. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002456 · Cited by 115
Donnelly, P. S., Liddell, J. R., Lim, S., Paterson, B. M., Cater, M. A., Savva, M. S., Mot, A. I., James, J. L., Trounce, I. A., White, A. R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116227108 · Cited by 110
Toyofuku, T., Okamoto, Y., Ishikawa, T., Sasawatari, S., & Kumanogoh, A. (2019) · The EMBO Journal · doi:10.15252/embj.2018100875 · Cited by 107
Drosophila as a Model to Study Mitochondrial Dysfunction in Parkinson's DiseasePreprint
Guo, M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009944 · Cited by 111
Multifaceted deaths orchestrated by mitochondria in neurones
Nagley, P., Higgins, G. C., Atkin, J. D., & Beart, P. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.004 · Cited by 107
Protein folding diseases and neurodegeneration: Lessons learned from yeast
Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 108
Mitochondrial Dysfunction: A Key Player in Brain Aging and Diseases
Bartman, S., Coppotelli, G., & Ross, J. M. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46030130 · Cited by 110
Human mesenchymal stromal cells release functional mitochondria in extracellular vesicles
Thomas, M. A., Fahey, M. J., Pugliese, B. R., Irwin, R. M., Antonyak, M. A., & Delco, M. L. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.870193 · Cited by 99
“Tissue healing is an energy intensive process, and MT dysfunction mediates many degenerative diseases, including Parkinson’s (Winklhofer and Haass, 2010), cardiomyopathy (Pacak et al.”
BackgroundJiang, P., Gan, M., Ebrahim, A. S., Castanedes‐Casey, M., Dickson, D. W., & Yen, S.-H. C. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.001 · Cited by 99
Ho, D. H., Je, A. R., Lee, H.-J., Son, I., Kweon, H., Kim, H., & Seol, W. (2018) · Experimental Neurobiology · doi:10.5607/en.2018.27.3.171 · Cited by 100
Thadathil, N., Delotterie, D. F., Xiao, J., Hori, R., McDonald, M. P., & Khan, M. M. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02109-8 · Cited by 94
PGC-1α activity in nigral dopamine neurons determines vulnerability to α-synuclein
Ciron, C., Zheng, L., Bobela, W., Knott, G. W., Leone, T. C., Kelly, D. P., & Schneider, B. L. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0200-8 · Cited by 98
Miranda, B. R. D., Rocha, E. M., Bai, Q., Ayadi, A. E., Hinkle, D., Burton, E. A., & Greenamyre, J. T. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.04.008 · Cited by 99
Mitochondrial dysfunction in astrocytes: A role in Parkinson’s disease?
Bantle, C. M., Hirst, W. D., Weihofen, A., & Shlevkov, E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.608026 · Cited by 95
Kynurenine-3-monooxygenase: a review of structure, mechanism, and inhibitors
Smith, J. R., Jamie, J. F., & Guillemin, G. J. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.11.001 · Cited by 97
Boonpraman, N., Yoon, S., Kim, C. Y., Moon, J., & Yi, S. S. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102698 · Cited by 95
Islam, M. S., Nolte, H., Jacob, W., Ziegler, A. B., Pütz, S., Grosjean, Y., Szczepanowska, K., Trifunović, A., Braun, T. W., Heumann, H., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw352 · Cited by 97
Tuon, T., Souza, P. S., Santos, M. F., Pereira, F. T., Pedroso, G. S., Luciano, T. F., De Souza, C. T., Dutra, R. C., Silveira, P. C. L., & Pinho, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/261809 · Cited by 92
Nashine, S., Cohen, P., Chwa, M., Lu, S. Y., Nesburn, A. B., Kuppermann, B. D., & Kenney, M. C. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.348 · Cited by 93
Rocha, S., Freitas, A., Guimarães, S., Vitorino, R. M. P., Aroso, M., & Gómez-Lázaro, M. (2017) · Antioxidants · doi:10.3390/antiox7010001 · Cited by 93
Tabata, Y., Imaizumi, Y., Sugawara, M., Andoh-Noda, T., Banno, S., Chai, M., Sone, T., Yamazaki, K., Ito, M., Tsukahara, K., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.09.006 · Cited by 90
“PARK2-Dopaminergic Neurons Showed Increased Susceptibility to Rotenone-Induced Stress Because it has been reported thatmitochondrial respiratory chain complex I activity is reduced in the brains of PD patients (Schapira et al., 1989; Winklhofer and Haass, 2010), we used rotenone, amitochondrial complex I inhibitor (Du”
MethodDietary Antioxidants and Parkinson’s Disease
Park, H., & Ellis, A. C. (2020) · Antioxidants · doi:10.3390/antiox9070570 · Cited by 91
Gershoni, M., Levin, L., Ovadia, O., Toiw, Y., Shani, N., Dadon, S., Barzilai, N., Bergman, A., Atzmon, G., Wainstein, J., et al. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu208 · Cited by 87
“Because complex I is the protein complex most involved in mitochondrial disorders, being vital in complex disorders, such as Parkinson’s disease (Winklhofer and Haass 2010) and oncocytomas (Zimmermann et al. 2011), deciphering the functionality of the 44 subunits of the complex and their network of…”
BackgroundLiu, J., Wen, J., Zhang, Z., Liu, H., & Sun, Y. (2015) · Microsystems & Nanoengineering · doi:10.1038/micronano.2015.20 · Cited by 89
Tau-induced neurodegeneration: mechanisms and targets
Beharry, C., Cohen, L. S., Di, J., Ibrahim, K., Briffa-Mirabella, S., & Alonso, A. D. C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1414-z · Cited by 92
Nouws, J., Nijtmans, L. G. J., Smeitink, J. A. M., & Vogel, R. O. (2011) · Brain · doi:10.1093/brain/awr261 · Cited by 90
Neurochemistry and the non-motor aspects of PD
Ferrer, I., López‐González, I., Carmona, M., Dalfó, E., Pujol, A., & Martínez, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.10.019 · Cited by 92
Mitochondria in Multiple Sclerosis: Molecular Mechanisms of Pathogenesis
Patergnani, S., Fossati, V., Bonora, M., Giorgi, C., Marchi, S., Missiroli, S., Rusielewicz, T., Wieckowski, M. R., & Pinton, P. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.003 · Cited by 86
Autophagy in adipose tissue biology
Zhang, Y., Zeng, X., & Jin, S. V. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.09.004 · Cited by 92
Promising Polyphenols in Parkinson’s Disease Therapeutics
Singh, A. K., Tripathi, P., Yadawa, A. K., & Singh, S. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03058-3 · Cited by 91
“Role of complex I inhibition of electron transport chain leading to Parkinsonism was first time came into picture before five decades [27, 28] but still the disease etiology is not known.”
BackgroundFlierl, A., Oliveira, L. M. A., Falomir‐Lockhart, L. J., Mak, S. K., Hesley, J., Soldner, F., Arndt‐Jovin, D. J., Jaenisch, R., Langston, J. W., Jovin, T. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112413 · Cited by 87
Maternal transmission of Alzheimer's disease: prodromal metabolic phenotype and the search for genes
Mosconi, L., Berti, V., Swerdlow, R. H., Pupi, A., Duara, R., & de Leon, M. (2010) · Human Genomics · doi:10.1186/1479-7364-4-3-170 · Cited by 85
mTORC Inhibitors as Broad-Spectrum Therapeutics for Age-Related Diseases
Walters, H. E., & Cox, L. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082325 · Cited by 85
“Failure of mitophagy, through defects in PINK1/Parkin, may also be important, and defective mitochondria are observed in PD [146].”
BackgroundHwang, C. K., & Chun, H. S. (2012) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.110842 · Cited by 85
Pimentel, C., Batista-Nascimento, L. S., Rodrigues‐Pousada, C., & Menezes, R. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/132146 · Cited by 86
Tea Polyphenols in Parkinson’s Disease
Caruana, M., & Vassallo, N. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-18365-7_6 · Cited by 88
Tan, H. Y., Cho, H., & Lee, L. P. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-00643-3 · Cited by 87
Negga, R., Stuart, J. A., Machen, M. L., Salva, J., Lizek, A. J., Richardson, S. J., Osborne, A. S., Mirallas, O., McVey, K. A., & Fitsanakis, V. A. (2011) · Neurotoxicity Research · doi:10.1007/s12640-011-9274-7 · Cited by 84
Mitochondrial Dysfunction in Neurodegenerative Diseases
Schapira, A. H. V. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9855-x · Cited by 85
Parkin functionally interacts with PGC-1α to preserve mitochondria and protect dopaminergic neurons
Zheng, L., Bernard‐Marissal, N., Moullan, N., D'Amico, D. F., Auwerx, J. H., Moore, D. J., Knott, G. W., Aebischer, P., & Schneider, B. L. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw418 · Cited by 86
Pink1-deficiency in mice impairs gait, olfaction and serotonergic innervation of the olfactory bulb
Glasl, L., Kloos, K., Giesert, F., Röthig, A. H. J., Benedetto, B. D., Kühn, R., Zhang, J., Hafen, U., Zerle, J., Hofmann, A., et al. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.002 · Cited by 87
“Besides influencing ETC complex activity and mitophagy, Pink1deficiency also has an impact on mitochondrial morphology (Dagda et al., 2009; Lutz et al., 2009; Sandebring et al., 2009; Winklhofer and Haass, 2010).”
BackgroundSelf-citationRosa, A. I., Fonseca, I., Nunes, M. J., Moreira, S., Rodrigues, E., Carvalho, A. N., Rodrigues, C. M. P., Gama, M. J., & Castro-Caldas, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.004 · Cited by 82
Koob, S., Barrera, M., Anand, R., & Reichert, A. S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.004 · Cited by 83
DJ-1 knock-down impairs astrocyte mitochondrial function
Larsen, N. J., Ambrosi, G., Mullett, S. J., Berman, S. B., & Hinkle, D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.016 · Cited by 82
“Mitochondrial dysfunction is linked to the pathogenesis of Parkinson’s disease (PD) (Schapira, 2004; Büeler, 2009; Van Laar and Berman, 2009; Winklhofer and Haass, 2010; Zhu and Chu, 2010).”
BackgroundRajan, S., Tryphena, K. P., Khan, S. S., Vora, L. K., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101915 · Cited by 84
Charli, A., Jin, H., Anantharam, V., Kanthasamy, A., & Kanthasamy, A. G. (2015) · NeuroToxicology · doi:10.1016/j.neuro.2015.06.007 · Cited by 81
Lee, J., & Paull, T. T. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101511 · Cited by 83
Rasheed, M. Z., Tabassum, H., & Parvez, S. (2016) · PROTOPLASMA · doi:10.1007/s00709-015-0930-2 · Cited by 79
Zhao, J., Liang, Q., Sun, Q. Y., Chen, C., Xu, L., Ding, Y., & Zhou, P. (2017) · RSC Advances · doi:10.1039/c7ra03752j · Cited by 80
Corti, O., & Brice, A. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2012.11.002 · Cited by 79
Shchepinov, M. S., Chou, V., Pollock, E. D., Langston, J. W., Cantor, C. R., Molinari, R. J., & Manning-Bog, A. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.07.020 · Cited by 81
Lin, K.-L., Lin, K.-J., Wang, P., Chuang, J., Lin, H., Chen, S., Chuang, Y., Huang, S., Tiao, M., Chen, J., et al. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1489128 · Cited by 78
Mitra, S., Chakrabarti, N., & Bhattacharyya, A. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-163 · Cited by 77
Farmer, K., Smith, C. A., Hayley, S. P., & Smith, J. C. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160818865 · Cited by 77
Neuroprotective and anti‐inflammatory effects of morin in a murine model of Parkinson's disease
Lee, K. M., Lee, Y., Chun, H. J., Kim, A. H., Kim, J. Y., Lee, J. Y., Ishigami, A., & Lee, J. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23764 · Cited by 77
Jo, M. G., Ikram, M. A., Jo, M. H., Yoo, L., Chung, K. C., Nah, S.-Y., Hwang, H., Rhim, H., & Kim, M. O. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1020-1 · Cited by 76
RetractedJonas, E. A., Porter, G. A., Beutner, G., Mnatsakanyan, N., & Alavian, K. N. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.04.013 · Cited by 81
Bento‐Pereira, C., & Dinkova‐Kostova, A. T. (2020) · Medicinal Research Reviews · doi:10.1002/med.21714 · Cited by 79
“There are two subtypes of PD, an idiopathic form and a familial genetic form.(8) Seminal work in the past couple of decades has identified genes involved in the autosomal dominant and recessive forms of monogenetic PD.”
BackgroundMutational screening of the mortalin gene (HSPA9) in Parkinson’s disease
de Mena, L., Coto, E., Sánchez-Ferrero, E., Ribacoba, R., Guisasola, L. M., Salvador, C., Estrada, M. B., & Álvarez, V. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0273-2 · Cited by 75
Wu, G., Wang, X., Feng, X., Zhang, A., Li, J., Gu, K., Huang, J. A., Pang, S., Dong, H., Gao, H., et al. (2011) · Brain Research · doi:10.1016/j.brainres.2011.04.013 · Cited by 78
Potential Treatment of Parkinson’s Disease with Omega-3 Polyunsaturated Fatty Acids
Li, P., & Song, C. (2022) · Nutritional Neuroscience · doi:10.1080/1028415x.2020.1735143 · Cited by 74
Modeling Parkinson’s Disease Using Induced Pluripotent Stem Cells
Byers, B., Lee, H. D., & Pera, R. A. R. (2012) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-012-0270-y · Cited by 78
Neuroprotective Effects of Temsirolimus in Animal Models of Parkinson’s Disease
Siracusa, R., Paterniti, I., Cordaro, M., Crupi, R., Bruschetta, G., Campolo, M., Cuzzocrea, S., & Esposito, E. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0496-4 · Cited by 74
Aging Neural Progenitor Cells Have Decreased Mitochondrial Content and Lower Oxidative Metabolism
Stoll, E. A., Cheung, W., Mikheev, A. M., Sweet, I. R., Bielas, J. H., Zhang, J., Rostomily, R., & Horner, P. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.252171 · Cited by 75
Chu, Y., Goldman, J. G., Kelly, L. P., He, Y., Waliczek, T., & Kordower, J. H. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.003 · Cited by 71
Jalewa, J., Sharma, M. K., & Hölscher, C. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13736 · Cited by 77
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Peplow, P., & Martinez, B. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.221147 · Cited by 73
Ni, Y., Huang, H., Chen, Y., Cao, M., Zhou, H., & Zhang, Y. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0373-0 · Cited by 73
A possible role for mitochondrial dysfunction in migraine
Stuart, S., & Griffiths, L. R. (2012) · Molecular Genetics and Genomics · doi:10.1007/s00438-012-0723-7 · Cited by 72
Parkinson's disease proteins: Novel mitochondrial targets for cardioprotection
Mukherjee, U., Ong, S., Ong, S., & Hausenloy, D. J. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.10.005 · Cited by 72
Parkin mediates the ubiquitination of VPS35 and modulates retromer-dependent endosomal sorting
Williams, E. T., Glauser, L., Tsika, E., Jiang, H., Islam, M. S., & Moore, D. J. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy224 · Cited by 71
Alternative oxidase rescues mitochondria-mediated dopaminergic cell loss in Drosophila
Humphrey, D. M., Parsons, R. B., Ludlow, Z. N., Riemensperger, T. D., Esposito, G., Verstreken, P., Jacobs, H. T., Birman, S., & Hirth, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds096 · Cited by 75
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Ferrer, I. (2011) · Parkinson s Disease · doi:10.4061/2011/708404 · Cited by 75
Lin, T., Cheng, C.-H., Chen, S., Liou, C., Huang, C., & Chuang, Y. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13078722 · Cited by 71
Lapchak, P. A. (2011) · Expert Review of Medical Devices · doi:10.1586/erd.11.64 · Cited by 70
Magrì, A., Belfiore, R., Reina, S., Tomasello, M. F., Rosa, M. C. D., Guarino, F., Leggio, L., Pinto, V. D., & Messina, A. A. (2016) · Scientific Reports · doi:10.1038/srep34802 · Cited by 70
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Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 74
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BackgroundSrivastava, S., & Haigis, M. C. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072526 · Cited by 70
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Vidal, P. M., & Pacheco, R. (2019) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-019-09834-5 · Cited by 71
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Robea, M. A., Balmuș, I.-M., Ciobica, A. S., Strungaru, Ș.-A., Plavan, G. I., Gorgan, L., Săvucă, A., & Nicoară, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1370837 · Cited by 68
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Lin, A., Poteet, E. C., Du, F., Choudhury, G. R., Liu, R., Wen, Y., Bresnen, A., Huang, S., Fox, P. T., Yang, S.-H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046585 · Cited by 66
Matenia, D., Hempp, C., Timm, T., Eikhof, A., & Mandelkow, E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262287 · Cited by 68
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Paiva, I., Jain, G., Lázaro, D. F., Gotovac, K., Hentrich, T., Kerimoglu, C., Pinho, R., Szegő, É. M., Burkhardt, S., Capece, V., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.08.001 · Cited by 68
Xia, M., Huang, R., Shi, Q., Boyd, W. A., Zhao, J., Sun, N., Rice, J. R., Dunlap, P. E., Hackstadt, A. J., Bridge, M. F., et al. (2018) · Environmental Health Perspectives · doi:10.1289/ehp2589 · Cited by 66
“Recent research indicated that several inhibitors of the electron transport chain can induce parkinsonism-like symptoms in rats (Winklhofer and Haass 2010).”
Chakraborty, S., Nian, F., Tsai, J., Karmenyan, A., & Chiou, A. (2016) · Scientific Reports · doi:10.1038/srep19145 · Cited by 67
Metadata
- Authors
- Winklhofer, K. F., & Haass, C.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Corresponding author
- Winklhofer, Konstanze F.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2010-01
- Volume
- 1802
- Issue
- 1
- Pages
- 29-44
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2130497877
- Cited by
- 688
- References
- 326
- Citations by year
- 2026: 10 · 2025: 16 · 2024: 13 · 2023: 27 · 2022: 30 · 2021: 37 · 2020: 55 · 2019: 38 · 2018: 72 · 2017: 51 · 2016: 61 · 2015: 39 · 2014: 29 · 2013: 37 · 2012: 49
- FWCI
- 5.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 596)
- German Ministry for Education and Research
- the Helmholtz Alliance “Mental Health in an Ageing Society,”
- the Center for Integrated Protein Science Munich
- the Hans and Ilse Breuer Foundation
- 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 › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dysfunction, Parkinson's disease, mitochondrial dynamics, mitochondrial morphology, mitochondrial complex I inhibition, parkinsonism, electron transport chain, calcium homeostasis, stress response, cell death pathways, neurodegeneration, aging, familial Parkinson's disease, sporadic Parkinson's disease
- MeSH terms
- Animals, DNA, Mitochondrial, Humans, Mitochondria, Models, Biological, Parkinson Disease, Oxidative Stress, Mitochondrial Proteins
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