Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease
Abstract
Parkinson's disease (PD) is a progressive neurodegenerative disorder characterised by the preferential loss of dopaminergic neurons in the substantia nigra. Mitochondrial dysfunction is increasingly appreciated as a key determinant of dopaminergic neuronal susceptibility in PD and is a feature of both familial and sporadic disease, as well as in toxin-induced Parkinsonism. Recently, the mechanisms by which PD-associated mitochondrial proteins phosphatase and tensin homolog deleted on chromosome 10 (PTEN)-induced putative kinase 1 (PINK1) and parkin function and induce neurodegeneration have been identified. In addition, increasing evidence implicates other PD-associated proteins such as α-synuclein (α-syn) and leucine-rich repeat kinase 2 (LRRK2) in mitochondrial dysfunction in genetic cases of PD with the potential for a large functional overlap with sporadic disease. This review highlights how recent advances in understanding familial PD-associated proteins have identified novel mechanisms and therapeutic strategies for addressing mitochondrial dysfunction in PD.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Mitochondrial malfunction is a key determinant of dopaminergic neurodegeneration and an overlapping risk factor for sporadic and familial PD.
“mitochondrial malfunction is increasingly considered a key determinant of dopaminergic neurodegeneration, serving as an overlapping risk factor for both sporadic and familial cases [11]”
From Healthy Human Fecal Microbiota Transplantation into Mice Attenuates MPTP-Induced Neurotoxicity <i>via</i> AMPK/SOD2 Pathway (2023) · cites this paper as [11]
Mitochondrial dysfunction has been associated with a number of age-related diseases such as neurological disorders, CVD, liver and kidney diseases, diabetes and cancer.
“it has been associated with a number of age-related diseases such as neurological disorders, CVD, liver and kidney diseases, diabetes and cancer”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Ryan et al., 2015
Mitochondrial dysfunction has been associated with age-related diseases such as neurological disorders, cardiovascular disease, liver and kidney diseases, diabetes and cancer.
“it has been associated with a number of age-related diseases such as neurological disorders, cardiovascularCVD, liver and kidney diseases, diabetes and cancer (Lane et al., 2015; Payne and Chinnery, 2015; Ryan et al., 2015; Wallace, 2012).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Ryan et al., 2015
Cites
1 retracted
TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease
Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 150 · see citing works
RetractedPINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969 · see citing works
International Parkinson's Disease Genomics Consortium (IPDGC), Nalls, M. A., Parkinson's Study Group (PSG) Parkinson's Research: The Organized GENetics Initiative (PROGENI), 23andMe, GenePD, NeuroGenetics Research Consortium (NGRC), Hussman Institute of Human Genomics (HIHG), Investigator, T. A. J. D., (CHARGE), C. F. H. A. A. R. I. G. E., North American Brain Expression Consortium (NABEC), et al. (2014) · Nature Genetics · doi:10.1038/ng.3043 · Cited by 1,895 · see citing works
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 · see citing works
Autophagosomes form at ER–mitochondria contact sites
Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,747 · see citing works
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works
Self-citationPINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323 · see citing works
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298 · see citing works
PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility
Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,161 · see citing works
Canet-Aviles, R., Wilson, M. A., Miller, D. W., Ahmad, R., McLendon, C., Bandyopadhyay, S., Baptista, M. J., Ringe, D., Petsko, G. A., & Cookson, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402959101 · Cited by 1,115 · see citing works
Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083 · see citing works
Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
Brand, M. D., Affourtit, C., Esteves, T. C., Green, K., Lambert, A. J., Miwa, S., Pakay, J. L., & Parker, N. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.034 · Cited by 1,032 · see citing works
Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Sarraf, S. A., Raman, M., Guarani, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,020 · see citing works
‘Rejuvenation’ protects neurons in mouse models of Parkinson’s disease
Chan, C. S., Guzmán, J. N., Ilijić, E., Mercer, J. N., Rick, C., Tkatch, T., Meredith, G. E., & Surmeier, D. J. (2007) · Nature · doi:10.1038/nature05865 · Cited by 905 · see citing works
Kim, C., Ho, D.-H., Suk, J.-E., You, S., Michael, S., Kang, J., Joong Lee, S., Masliah, E., Hwang, D., Lee, H.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2534 · Cited by 856 · see citing works
Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842 · see citing works
Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1
Guzmán, J. N., Sánchez-Padilla, J., Wokosin, D. L., Kondapalli, J., Ilijić, E., Schumacker, P. T., & Surmeier, D. J. (2010) · Nature · doi:10.1038/nature09536 · Cited by 836 · see citing works
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806 · see citing works
A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes
Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755 · see citing works
Self-citationLRRK2 Mutant iPSC-Derived DA Neurons Demonstrate Increased Susceptibility to Oxidative Stress
Nguyen, H. N., Byers, B., Cord, B. J., Shcheglovitov, A., Byrne, J., Gujar, P., Kee, K., Schüle, B., Dolmetsch, R. E., Langston, J. W., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.01.013 · Cited by 748 · see citing works
McLelland, G., Soubannier, V., Chen, C. X., McBride, H. M., & Fon, E. A. (2014) · The EMBO Journal · doi:10.1002/embj.201385902 · Cited by 743 · see citing works
Self-citationMitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment
Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711 · see citing works
Self-citationOrdureau, A., Sarraf, S. A., Duda, D. M., Heo, J., Jedrychowski, M. P., Sviderskiy, V. O., Olszewski, J. L., Koerber, J. T., Xie, T., Beausoleil, S. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.007 · Cited by 693 · see citing works
Gandhi, S., Wood-Kaczmar, A., Yao, Z., Plun-Favreau, H., Deas, E., Klupsch, K., Downward, J., Latchman, D. S., Tabrizi, S. J., Wood, N. W., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.013 · Cited by 682 · see citing works
Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease
Appel‐Cresswell, S., Vilariño‐Güell, C., Encarnacion, M. J., Sherman, H. E., Yu, I. S., Shah, B., Weir, D. M., Thompson, C., Szu‐Tu, C., Trinh, J., et al. (2013) · Movement Disorders · doi:10.1002/mds.25421 · Cited by 669 · see citing works
MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
Vance, J. E. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 665 · see citing works
Kinase activity of mutant LRRK2 mediates neuronal toxicity
Smith, W. W., Pei, Z., Jiang, H., Dawson, V. L., Dawson, T. M., & Ross, C. A. (2006) · Nature Neuroscience · doi:10.1038/nn1776 · Cited by 619 · see citing works
Snow, B. J., Rolfe, F. L., Lockhart, M. M., Frampton, C. M., O'Sullivan, J. D., Fung, V., Smith, R. A. J., Murphy, M. P., Taylor, K. M., & On behalf of the Protect Study Group (2010) · Movement Disorders · doi:10.1002/mds.23148 · Cited by 606 · see citing works
Okatsu, K., Oka, T., Iguchi, M., Imamura, K., Kosako, H., Tani, N., Kimura, M., Go, E., Koyano, F., Funayama, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms2016 · Cited by 602 · see citing works
Interplay of LRRK2 with chaperone-mediated autophagy
Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works
Sànchez-Dànes, A., Richaud-Patin, Y., Carballo-Carbajal, I., Jiménez-Delgado, S., Caig, C., Mora, S., Guglielmo, C. D., Ezquerra, M., Patel, B., Giralt, A., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200215 · Cited by 576 · see citing works
Dynamic regulation of mitochondrial fission through modification of the dynamin‐related protein Drp1
Chang, C., & Blackstone, C. D. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05629.x · Cited by 570 · see citing works
Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
Trempe, J.-F., Sauvé, V., Grenier, K., Seirafi, M., Tang, M. Y. H., Ménade, M., Al-Abdul-Wahid, S., Krett, J. D., Wong, K. T. K., Kozlov, G., et al. (2013) · Science · doi:10.1126/science.1237908 · Cited by 549 · see citing works
Self-citationCooper, O., Seo, H., Andrabi, S., Guardia-Laguarta, C., Graziotto, J., Sundberg, M., McLean, J. R., Carrillo-Reid, L., Xie, Z., Osborn, T., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003985 · Cited by 508 · see citing works
Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502 · see citing works
PINK1 cleavage at position A103 by the mitochondrial protease PARL
Deas, E., Plun‐Favreau, H., Gandhi, S., Desmond, H., Kjaer, S., Loh, S. H. Y., Renton, A. E., Harvey, R. J., Whitworth, A. J., Martins, L. M., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq526 · Cited by 501 · see citing works
Reinhardt, P., Schmid, B., Burbulla, L. F., Schöndorf, D. C., Wagner, L., Glatza, M., Höing, S., Hargus, G., Heck, S. A., Dhingra, A., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.01.008 · Cited by 500 · see citing works
α-Synuclein Is Localized to Mitochondria-Associated ER Membranes
Guardia-Laguarta, C., Area-Gómez, E., Rüb, C., Liu, Y.-H., Magrané, J., Becker, D., Voos, W., Schon, E., & Przedborski, S. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2507-13.2014 · Cited by 489 · see citing works
Morais, V. A., Verstreken, P., Röthig, A. H. J., Smet, J., Snellinx, A., Vanbrabant, M., Haddad, D., Frezza, C., Mandemakers, W. J., Weisenhorn, D. M. V., et al. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900006 · Cited by 444 · see citing works
Living on the edge with too many mouths to feed: Why dopamine neurons die
Bolam, J. P., & Pissadaki, E. K. (2012) · Movement Disorders · doi:10.1002/mds.25135 · Cited by 439 · see citing works
Ryan, S. D., Dolatabadi, N., Chan, S. F., Zhang, X., Akhtar, M. W., Parker, J., Soldner, F., Sunico, C. R., Nagar, S., Talantova, M. V., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.009 · Cited by 430 · see citing works
LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1
Wang, X., Ma, Y., Fujioka, H., Liu, J., Wilson‐Delfosse, A. L., Chen, S. G., Perry, G. L., Casadesús, G., & Zhu, X. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds003 · Cited by 423 · see citing works
Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works
A Randomized Clinical Trial of High-Dosage Coenzyme Q10 in Early Parkinson Disease
The Parkinson Study Group QE3 Investigators, Beal, M. F., Oakes, D., Shoulson, I., Henchcliffe, C., Galpern, W. R., Haas, R., Juncos, J. L., Nutt, J. G., Voss, T., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2014.131 · Cited by 410 · see citing works
Parkin Ubiquitinates Drp1 for Proteasome-dependent Degradation
Wang, H., Song, P., Du, L., Tian, W., Yue, W., Liu, M., Li, D., Wang, B., Zhu, Y., Cao, C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.144238 · Cited by 376 · see citing works
Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002537 · Cited by 371 · see citing works
Morais, V. A., Haddad, D., Craessaerts, K., Bock, P. D., Swerts, J., Vilain, S., Aerts, L., Overbergh, L., Grünewald, A., Seibler, P., et al. (2014) · Science · doi:10.1126/science.1249161 · Cited by 364 · see citing works
Vitamin K 2 Is a Mitochondrial Electron Carrier That Rescues Pink1 Deficiency
Vos, M. H., Esposito, G., Edirisinghe, J. N., Vilain, S., Haddad, D., Slabbaert, J. R., Meensel, S. V., Schaap, O., Strooper, B. D., Meganathan, R., et al. (2012) · Science · doi:10.1126/science.1218632 · Cited by 364 · see citing works
Pissadaki, E. K., & Bolam, J. P. (2013) · Frontiers in Computational Neuroscience · doi:10.3389/fncom.2013.00013 · Cited by 349 · see citing works
Soubannier, V., Rippstein, P. U., Kaufman, B. A., Shoubridge, E. A., & McBride, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052830 · Cited by 346 · see citing works
Deficits in dopaminergic transmission precede neuron loss and dysfunction in a new Parkinson model
Janezic, S., Threlfell, S., Dodson, P. D., Dowie, M. J., Taylor, T. N., Potgieter, D., Parkkinen, L., Senior, S. L., Anwar, S., Ryan, B., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309143110 · Cited by 344 · see citing works
Self-citationTran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 324 · see citing works
Luth, E. S., Stavrovskaya, I. G., Bartels, T., Kristal, B. S., & Selkoe, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545749 · Cited by 281 · see citing works
A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013) · Cell · doi:10.1016/j.cell.2013.07.030 · Cited by 275 · see citing works
Bordet, T., Buisson, B., Michaud, M., Drouot, C., Galéa, P., Delaage, P., Akentieva, N., Evers, A. S., Covey, D. F., Ostuni, M. A., et al. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.123000 · Cited by 267 · see citing works
Human DJ-1 and its homologs are novel glyoxalases
Lee, J., Song, J., Kwon, K., Jang, S., Kim, C., Baek, K., Kim, J., & Park, C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds155 · Cited by 259 · see citing works
Calcium, Bioenergetics, and Neuronal Vulnerability in Parkinson's Disease
Surmeier, D. J., & Schumacker, P. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.410530 · Cited by 233 · see citing works
Su, Y.-C., & Qi, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt301 · Cited by 221 · see citing works
Dysregulation of glucose metabolism is an early event in sporadic Parkinson's disease
Dunn, L., Allen, G., Mamais, A., Ling, H., Li, A., Duberley, K., Hargreaves, I., Pope, S., Holton, J., Lees, A., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.001 · Cited by 217 · see citing works
Schmid, A. W., Fauvet, B., Moniatte, M., & Lashuel, H. A. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r113.032730 · Cited by 212 · see citing works
Mitochondrial DNA damage: Molecular marker of vulnerable nigral neurons in Parkinson's disease
Sanders, L. H., McCoy, J. L., Hu, X., Mastroberardino, P. G., Dickinson, B. C., Chang, C. J., Chu, C. T., Houten, B. V., & Greenamyre, J. T. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.014 · Cited by 192 · see citing works
Neuronal vulnerability in Parkinson’s disease
Hirsch, É. C., Faucheux, B. A., Damier, P., Prigent, A., & Agid, Y. (1997) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6842-4_9 · Cited by 192 · see citing works
Impaired intracellular trafficking defines early Parkinson's disease
Hunn, B. H. M., Cragg, S. J., Bolam, J. P., Spillantini, M., & Wade‐Martins, R. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2014.12.009 · Cited by 185 · see citing works
Self-citationMitochondrial translocation of α-synuclein is promoted by intracellular acidification
Cole, N. B., DiEuliis, D., Leo, P., Mitchell, D. C., & Nussbaum, R. L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.03.012 · Cited by 183 · see citing works
The H50Q Mutation Enhances α-Synuclein Aggregation, Secretion, and Toxicity
Khalaf, O., Fauvet, B., Oueslati, A., Dikiy, I., Mahul‐Mellier, A., Ruggeri, F. S., Mbefo, M. K., Vercruysse, F., Dietler, G., Lee, S., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.553297 · Cited by 179 · see citing works
The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway
Pedro, J. M. B., Niso‐Santano, M., Gómez‐Sánchez, R., Pizarro‐Estrella, E., Aiastui, A., Gorostidi, A., Climent, V. E., de Maturana, R. L., Sánchez‐Pernaute, R., de Munaín, A. L., et al. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1061-y · Cited by 175 · see citing works
G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization
Papkovskaia, T. D., Chau, K., Iñesta-Vaquera, F., Papkovsky, D. B., Healy, D. G., Nishio, K., Staddon, J. M., Duchen, M. R., Hardy, J., Schapira, A. H. V., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds244 · Cited by 164 · see citing works
Zondler, L., Miller‐Fleming, L., Repici, M., Gonçalves, S. A., Tenreiro, S., Rosado-Ramos, R., Betzer, C., Straatman, K. R., Jensen, P. H., Giorgini, F., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.307 · Cited by 161 · see citing works
Leucine‐rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin‐like protein
Niu, J., Yu, M., Wang, C., & Xu, Z. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07809.x · Cited by 159 · see citing works
The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance
Bertolin, G., Ferrando-Miguel, R., Jacoupy, M., Traver, S., Grenier, K., Greene, A. W., Dauphin, A., Waharte, F., Bayot, A., Salamero, J., et al. (2013) · Autophagy · doi:10.4161/auto.25884 · Cited by 154 · see citing works
Self-citationTufi, R., Gandhi, S., de Castro, I. P., Lehmann, S., Angelova, P. R., Dinsdale, D. D., Deas, E., Plun‐Favreau, H., Nicotera, P., Abramov, A. Y., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb2901 · Cited by 153 · see citing works
Stafa, K., Tsika, E., Moser, R., Musso, A., Glauser, L., Jones, A., Biskup, S., Xiong, Y., Bandopadhyay, R., Dawson, V. L., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt600 · Cited by 134 · see citing works
Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection
Trempe, J., & Fon, E. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00038 · Cited by 130 · see citing works
Self-citationCosta, A. C., Loh, S. H. Y., & Martins, L. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2012.205 · Cited by 129 · see citing works
Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy
Fedorowicz, M. A., de Vries, R. L. A., Rüb, C., Becker, D., Huang, Y., Zhou, C., Wolken, D. M. A., Voos, W., Liu, Y., & Przedborski, S. (2013) · EMBO Reports · doi:10.1002/embr.201337294 · Cited by 127 · see citing works
Ursocholanic acid rescues mitochondrial function in common forms of familial Parkinson’s disease
Mortiboys, H., Aasly, J. O., & Bandmann, O. (2013) · Brain · doi:10.1093/brain/awt224 · Cited by 124 · see citing works
Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein
Subramaniam, S., Vergnes, L., Franich, N. R., Reue, K., & Chesselet, M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.017 · Cited by 119 · see citing works
Ryan, B. J., Nissim, A., & Winyard, P. G. (2014) · Redox Biology · doi:10.1016/j.redox.2014.05.004 · Cited by 119 · see citing works
Self-citationThe Impact of Mitochondrial Fusion and Fission Modulation in Sporadic Parkinson’s Disease
Santos, D., Esteves, A. R., Silva, D. F., Januário, C., & Cardoso, S. M. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8893-4 · Cited by 111 · see citing works
TRAP1 rescues PINK1 loss-of-function phenotypes
Zhang, L., Karsten, P., Hamm, S., Pogson, J. H., Müller-Rischart, A. K., Exner, N., Haass, C., Whitworth, A. J., Winklhofer, K. F., Schulz, J. B., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt132 · Cited by 109 · see citing works
Perfeito, R., Lázaro, D. F., Outeiro, T. F., & Rego, A. C. (2014) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.08.002 · Cited by 102 · see citing works
PINK1 Triggers Autocatalytic Activation of Parkin to Specify Cell Fate Decisions
Zhang, C., Lee, S., Peng, Y., Bunker, E. N., Giaime, E., Shen, J., Zhou, Z., & Liu, X. (2014) · Current Biology · doi:10.1016/j.cub.2014.07.014 · Cited by 101 · see citing works
Interaction of α-synuclein with vesicles that mimic mitochondrial membranes
Zigoneanu, I. G., Yang, Y. J., Krois, A. S., Haque, M. E., & Pielak, G. J. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.024 · Cited by 100 · see citing works
Plotegher, N., Gratton, E., & Bubacco, L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.02.013 · Cited by 95 · see citing works
Parkinson Disease Protein DJ-1 Binds Metals and Protects against Metal-induced Cytotoxicity
Björkblom, B., Adilbayeva, A., Maple‐Grødem, J., Piston, D., Ökvist, M., Xu, X. M., Brede, C., Larsen, J. P., & Møller, S. G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482091 · Cited by 95 · see citing works
The Impact of Pathogenic Mitochondrial DNA Mutations on Substantia Nigra Neurons
Reeve, A. K., Meagher, M., Lax, N., Simcox, E. M., Hepplewhite, P. D., Jaros, E., & Turnbull, D. M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3525-12.2013 · Cited by 92 · see citing works
Alpha‐Synuclein Binds to the Inner Membrane of Mitochondria in an α‐Helical Conformation
Robotta, M., Gerding, H. R., Vogel, A., Hauser, K., Schildknecht, S., Karreman, C., Leist, M., Subramaniam, V., & Drescher, M. (2014) · ChemBioChem · doi:10.1002/cbic.201402281 · Cited by 91 · see citing works
Ret rescues mitochondrial morphology and muscle degeneration of Drosophila Pink1 mutants
Klein, P., Müller-Rischart, A. K., Motori, E., Schönbauer, C., Schnorrer, F., Winklhofer, K. F., & Klein, R. (2014) · The EMBO Journal · doi:10.1002/embj.201284290 · Cited by 87 · see citing works
Pogson, J. H., Ivatt, R. M., Sánchez-Martínez, Á., Tufi, R., Wilson, E. L., Mortiboys, H., & Whitworth, A. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004815 · Cited by 85 · see citing works
The effect of α‐synuclein knockdown on MPP+ toxicity in models of human neurons
Fountaine, T. M., Venda, L. L., Warrick, N., Christian, H., Brundin, P., Channon, K. M., & Wade‐Martins, R. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06527.x · Cited by 78 · see citing works
Self-citationGirotto, S., Sturlese, M., Bellanda, M., Tessari, I., Cappellini, R., Bisaglia, M., Bubacco, L., & Mammi, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311589 · Cited by 73 · see citing works
Cannon, J. R., Geghman, K. D., Tapias, V., Sew, T., Dail, M. K., Li, C., & Greenamyre, J. T. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.11.007 · Cited by 72 · see citing works
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 · see citing works
Liu, M., Bender, S. A., Cuny, G. D., Sherman, W., Glicksman, M. A., & Ray, S. S. (2013) · Biochemistry · doi:10.1021/bi3012077 · Cited by 63 · see citing works
α‐Synuclein oligomers distinctively permeabilize complex model membranes
Stefanovic, A. N. D., Stöckl, M. T., Claessens, M. M. A. E., & Subramaniam, V. (2014) · FEBS Journal · doi:10.1111/febs.12824 · Cited by 60 · see citing works
Toyoda, Y., Erkut, C., Pan-Montojo, F. J., Boland, S., Stewart, M. P., Müller, D. J., Wurst, W., Hyman, A. A., & Kurzchalia, T. V. (2014) · Biology Open · doi:10.1242/bio.20149399 · Cited by 59 · see citing works
Taylor, T. N., Potgieter, D., Anwar, S., Senior, S. L., Janezic, S., Threlfell, S., Ryan, B. J., Parkkinen, L., Deltheil, T., Cioroch, M., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.005 · Cited by 56 · see citing works
Self-citationSmall Molecule Kinase Inhibitors for LRRK2 and Their Application to Parkinson's Disease Models
Kramer, T., Monte, F. L., Göring, S., Amombo, G. M. O., & Schmidt, B. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn200117j · Cited by 52 · see citing works
Tanti, G. K., & Goswami, S. K. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.009 · Cited by 52 · see citing works
Lopert, P., & Patel, M. (2014) · Redox Biology · doi:10.1016/j.redox.2014.04.010 · Cited by 52 · see citing works
Yakhine-Diop, S. M. S., Pedro, J. M. B., Gómez‐Sánchez, R., Pizarro‐Estrella, E., Rodríguez‐Arribas, M., Climent, V. E., Aiastui, A., de Munaín, A. L., Fuentes, J. M., & González‐Polo, R. A. (2014) · Toxicology · doi:10.1016/j.tox.2014.07.001 · Cited by 51 · see citing works
Pukaß, K., & Richter‐Landsberg, C. (2013) · Journal of Molecular Neuroscience · doi:10.1007/s12031-013-0154-x · Cited by 48 · see citing works
Bahnassawy, L., Nicklas, S., Palm, T., Menzl, I., Birzele, F., Gillardon, F., & Schwamborn, J. C. (2013) · Stem Cells and Development · doi:10.1089/scd.2013.0163 · Cited by 46 · see citing works
Grünewald, A., Arns, B., Meier, B., Brockmann, K., Tadić, V., & Klein, C. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5737 · Cited by 39 · see citing works
Short Mitochondrial ARF Triggers Parkin/PINK1-dependent Mitophagy
Grenier, K., Kontogiannea, M., & Fon, E. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.607150 · Cited by 38 · see citing works
Self-citationDetailed analysis of mitochondrial respiratory chain defects caused by loss of PINK1
Amo, T., Saiki, S., Sawayama, T., Sato, S., & Hattori, N. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.07.045 · Cited by 34 · see citing works
Richter, F., Gao, F., Medvedeva, V. P., Lee, P. C., Bove, N., Fleming, S. M., Michaud, M., Lemesre, V., Patassini, S., Rosa, K. D. L., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.05.012 · Cited by 33 · see citing works
Gouarné, C., Tracz, J., Giraudon‐Paoli, M., Deluca, V., Seimandi, M., Tardif, G., Xilouri, M., Stefanis, L., Bordet, T., & Pruss, R. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12939 · Cited by 31 · see citing works
Ryan, B. J., Venda, L. L., Crabtree, M. J., Hale, A., Channon, K. M., & Wade‐Martins, R. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.008 · Cited by 31 · see citing works
Self-citationYY1 binds to α-synuclein 3′-flanking region SNP and stimulates antisense noncoding RNA expression
Mizuta, I., Takafuji, K., Ando, Y., Satake, W., Kanagawa, M., Kobayashi, K., Nagamori, S., Shinohara, T., Ito, C., Yamamoto, M., et al. (2013) · Journal of Human Genetics · doi:10.1038/jhg.2013.90 · Cited by 30 · see citing works
Wu, K., Liu, J., Zhuang, N., & Wang, T. (2014) · The FASEB Journal · doi:10.1096/fj.14-255802 · Cited by 23 · see citing works
Flagged first, then by citations
1 of the 115 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Hallmarks of Brain Aging: Adaptive and Pathological Modification by Metabolic States
Mattson, M. P., & Arumugam, T. V. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.011 · Cited by 1,242 · see citing works
Selective neuronal vulnerability in Parkinson disease
Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,120 · see citing works
The SH-SY5Y cell line in Parkinson’s disease research: a systematic review
Xicoy, H., Wieringa, B., & Martens, G. J. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0149-0 · Cited by 1,036 · see citing works
Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes
Shahmoradian, S. H., Lewis, A. J., Genoud, C., Hench, J., Moors, T. E., Navarro, P. P., Castaño‐Díez, D., Schweighauser, G., Graff-Meyer, A., Goldie, K. N., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0423-2 · Cited by 974 · see citing works
Oxidative stress and Parkinson’s disease
Blesa, J., Trigo-Damas, I., Quiroga-Varela, A., & Jackson-Lewis, V. R. (2015) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2015.00091 · Cited by 878 · see citing works
Alpha-synuclein: Pathology, mitochondrial dysfunction and neuroinflammation in Parkinson’s disease
Rocha, E. M., Miranda, B. D., & Sanders, L. H. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.004 · Cited by 769 · see citing works
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works
Selective vulnerability in neurodegenerative diseases
Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585 · see citing works
The role of mitochondria in amyotrophic lateral sclerosis
Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.052 · Cited by 556 · see citing works
Park, J.-S., Davis, R. L., & Sue, C. M. (2018) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-018-0829-3 · Cited by 516 · see citing works
Mitochondria‐targeted antioxidants
Oyewole, A. O., & Birch‐Machin, M. A. (2015) · The FASEB Journal · doi:10.1096/fj.15-275404 · Cited by 467 · see citing works
Hsieh, C.-H., Shaltouki, A., Gonzalez, A. E., da Cruz, A. B., Burbulla, L. F., Lawrence, E. S., Schüle, B., Krainc, D., Palmer, T. D., & Wang, X. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.08.002 · Cited by 459 · see citing works
Lou, G., Palikaras, K., Lautrup, S., Scheibye‐Knudsen, M., Tavernarakis, N., & Fang, E. F. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.07.002 · Cited by 449 · see citing works
The Mitochondrial Basis of Aging and Age-Related Disorders
Srivastava, S. (2017) · Genes · doi:10.3390/genes8120398 · Cited by 428 · see citing works
PINK1/Parkin-mediated mitophagy in neurodegenerative diseases
Li, J., Yang, D., Li, Z., Zhao, M., Wang, D., Sun, Z., Wen, P., Dai, Y., Gou, F., Ji, Y., et al. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101817 · Cited by 388 · see citing works
McLelland, G., Goiran, T., Yi, W., Dorval, G., Chen, C. X., Lauinger, N. D., Krahn, A. I., Valimehr, S., Raković, A., Rouiller, I., et al. (2018) · eLife · doi:10.7554/elife.32866 · Cited by 386 · see citing works
Self-citationMitophagy in neurodegeneration and aging
Fivenson, E. M., Lautrup, S., Sun, N., Scheibye-Knudsen, M., Stevnsner, T., Nilsen, H., Bohr, V. A., & Fang, E. F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.02.007 · Cited by 364 · see citing works
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363 · see citing works
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 355 · see citing works
Elfawy, H. A., & Das, B. B. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.029 · Cited by 343 · see citing works
Alpha-synuclein oligomers: a new hope
Bengoa‐Vergniory, N., Roberts, R. F., Wade‐Martins, R., & Alegre‐Abarrategui, J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1755-1 · Cited by 335 · see citing works
Self-citationHuman Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339 · see citing works
The Role of Autophagy and Mitophagy in Bone Metabolic Disorders
Wang, S., Deng, Z.-T., Ma, Y.-C., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F.-J., & Zheng, Q. (2020) · International Journal on Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 305 · see citing works
Ubiquitin-mediated regulation of autophagy
Chen, R., Chen, Y.-H., & Huang, T.-Y. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0569-y · Cited by 320 · see citing works
Kovács, G. G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020189 · Cited by 322 · see citing works
Battogtokh, G., Choi, Y. S., Kang, D. S., Park, S. J., Shim, M. S., Huh, K. M., Cho, Y., Lee, J. Y., Lee, H. S., & Kang, H. C. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.05.006 · Cited by 311 · see citing works
Hallmarks of Aging: An Autophagic Perspective
Barbosa, M. C., Grosso, R. A., & Fader, C. M. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00790 · Cited by 265 · see citing works
Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson’s Disease
Alecu, I., & Bennett, S. A. L. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00328 · Cited by 260 · see citing works
Raefsky, S. M., & Mattson, M. P. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.045 · Cited by 274 · see citing works
Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system
McLelland, G., Lee, S., McBride, H. M., & Fon, E. A. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603105 · Cited by 253 · see citing works
Self-citationMitochondrial dysfunction and mitophagy defect triggered by heterozygous GBA mutations
Li, H.-Y., Ham, A., Ma, T. C., Kuo, S.-H., Kanter, E., Kim, D., Ko, H., Quan, Y., Sardi, S., Li, A.-Q., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1509818 · Cited by 211 · see citing works
Holper, L., Ben‐Shachar, D., & Mann, J. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0090-0 · Cited by 234 · see citing works
MPTP-induced mouse model of Parkinson’s disease: A promising direction of therapeutic strategies
Mustapha, M., & Taib, C. N. M. (2020) · Biomolecules and Biomedicine · doi:10.17305/bjbms.2020.5181 · Cited by 229 · see citing works
Reggiori, F., & Molinari, M. (2022) · Physiological Reviews · doi:10.1152/physrev.00038.2021 · Cited by 220 · see citing works
The genetic landscape of Parkinson's disease
Lunati, A., Lesage, S., & Brice, A. (2018) · Revue Neurologique · doi:10.1016/j.neurol.2018.08.004 · Cited by 218 · see citing works
Zhang, J., Li, X., & Li, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00381 · Cited by 213 · see citing works
Autophagy in aging and longevity
Wong, S. Q., Kumar, A. V., Mills, J., & Lapierre, L. R. (2019) · Human Genetics · doi:10.1007/s00439-019-02031-7 · Cited by 204 · see citing works
Truban, D., Hou, X., Caulfield, T. R., Fiesel, F. C., & Springer, W. (2016) · Journal of Parkinson’s Disease · doi:10.3233/jpd-160989 · Cited by 237 · see citing works
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works
Fujita, Y., Taniguchi, Y., Shinkai, S., Tanaka, M., & Ito, M. (2016) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.12724 · Cited by 199 · see citing works
The Glutathione System in Parkinson’s Disease and Its Progression
Bjørklund, G., Peana, M., Maes, M., Dadar, M., & Severin, B. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.10.004 · Cited by 186 · see citing works
Koentjoro, B., Park, J.-S., & Sue, C. M. (2017) · Scientific Reports · doi:10.1038/srep44373 · Cited by 191 · see citing works
Song, Y., Li, F., Lu, S., Ren, L., Bian, S., Liu, M., Zhao, D., Wang, S., & Wang, J. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.114739 · Cited by 194 · see citing works
Ghosh, A., Tyson, T., George, S., Hildebrandt, E. N., Steiner, J. A., Madaj, Z., Schulz, E., Machiela, E., McDonald, W. G., Galvis, M. L. E., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aag2210 · Cited by 187 · see citing works
The role of Ca2+ signaling in Parkinson's disease
Zaichick, S., McGrath, K. M., & Caraveo, G. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028738 · Cited by 188 · see citing works
Dupont, A.-C., Largeau, B., Santiago Ribeiro, M., Guilloteau, D., Tronel, C., & Arlicot, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040785 · Cited by 182 · see citing works
Mitochondria: a therapeutic target in acute kidney injury
Ishimoto, Y., & Inagi, R. (2015) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfv317 · Cited by 184 · see citing works
Wang, L., Cho, Y.-L., Tang, Y., Wang, J., Park, J., Wu, Y., Wang, C., Tong, Y., Chawla, R., Zhang, J., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0056-0 · Cited by 179 · see citing works
Qiu, J., Chen, Y., Zhuo, J., Zhang, L., Liu, J., Wang, B., Sun, D., Yu, S., & Lou, H. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.108963 · Cited by 170 · see citing works
UBA1: At the Crossroads of Ubiquitin Homeostasis and Neurodegeneration
Groen, E. J. N., & Gillingwater, T. H. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.08.003 · Cited by 157 · see citing works
LRRK2 Biology from structure to dysfunction: research progresses, but the themes remain the same
Berwick, D. C., Heaton, G. R., Azeggagh, S., & Harvey, K. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0344-2 · Cited by 164 · see citing works
Yeshaw, W. M., van der Zwaag, M., Pinto, F., Lahaye, L. L., Faber, A. I. E., Gómez‐Sánchez, R., Dolga, A. M., Poland, C., Monaco, A. P., van IJzendoorn, S. C., et al. (2019) · eLife · doi:10.7554/elife.43561 · Cited by 162 · see citing works
Redox homeostasis, oxidative stress and mitophagy
Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 161 · see citing works
Membrane trafficking in health and disease
Yarwood, R., Hellicar, J., Woodman, P. G., & Lowe, M. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.043448 · Cited by 150 · see citing works
MitophAging: Mitophagy in Aging and Disease
Bakula, D., & Scheibye‐Knudsen, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00239 · Cited by 150 · see citing works
Parkinson's disease: Alterations in iron and redox biology as a key to unlock therapeutic strategies
Ma, L., Azad, M. G., Dharmasivam, M., Richardson, V., Quinn, R. J., Feng, Y., Pountney, D. L., Tonissen, K. F., Mellick, G. D., Yanatori, I., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101896 · Cited by 148 · see citing works
Duda, J., Pötschke, C., & Liss, B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13572 · Cited by 149 · see citing works
Hou, X., Fiesel, F. C., Truban, D., Castanedes Casey, M., Lin, W.-L., Soto, A. I., Tacik, P., Rousseau, L. G., Diehl, N. N., Heckman, M. G., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1461294 · Cited by 147 · see citing works
The Role of Exosomal microRNAs and Oxidative Stress in Neurodegenerative Diseases
Wang, X., Zhou, Y., Gao, Q., Ping, D., Wang, Y., Wu, W., Xu, L., Fang, Y., Zhang, J., & Shao, A. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3232869 · Cited by 145 · see citing works
Gautier, C., Erpapazoglou, Z., Mouton‐Liger, F., Mp, M., Cormier‐Dequaire, F., Bigou, S., Duffaure, S., Girard, M., Forêt, B., Iannielli, A., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw148 · Cited by 141 · see citing works
The Chaperone TRAP1 As a Modulator of the Mitochondrial Adaptations in Cancer Cells
Masgras, I., Sànchez‐Martìn, C., Colombo, G., & Rasola, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00058 · Cited by 139 · see citing works
ccf-mtDNA as a Potential Link Between the Brain and Immune System in Neuro-Immunological Disorders
Gambardella, S., Limanaqi, F., Ferese, R., Biagioni, F., Campopiano, R., Centonze, D., & Fornai, F. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01064 · Cited by 141 · see citing works
Strategies for the Treatment of Parkinson’s Disease: Beyond Dopamine
Iarkov, A., Barreto, G. E., Grizzell, J. A., & Echeverrı́a, V. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00004 · Cited by 140 · see citing works
Moghadam, A. K., Charsouei, S., Bell, B., & Jabalameli, M. R. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-018-0587-4 · Cited by 137 · see citing works
Wang, W., Han, R., He, H., Li, J., Chen, S., Gu, Y., & Xie, C. (2021) · Aging · doi:10.18632/aging.202868 · Cited by 134 · see citing works
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 · see citing works
Targeting mitophagy in Parkinson's disease
Clark, E. H., de la Torre, A. V., Hoshikawa, T., & Briston, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.014294 · Cited by 128 · see citing works
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 128 · see citing works
Weindel, C. G., Bell, S. L., Huntington, T. E., Vail, K. J., Srinivasan, R., Patrick, K. L., & Watson, R. O. (2020) · eLife · doi:10.7554/elife.51071 · Cited by 121 · see citing works
Integrated molecular landscape of Parkinson’s disease
Klemann, C. J. H. M., Martens, G. J. M., Sharma, M., Martens, M. B., Ole Isacson, A., Gasser, T., Visser, J. E., & Poelmans, G. (2017) · npj Parkinson s Disease · doi:10.1038/s41531-017-0015-3 · Cited by 123 · see citing works
Sirt3 protects dopaminergic neurons from mitochondrial oxidative stress
Shi, H., Deng, H., Gius, D. R., Schumacker, P. T., Surmeier, D. J., & Ma, Y. C. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx100 · Cited by 122 · see citing works
Antioxidant Therapeutic Strategies in Neurodegenerative Diseases
Morén, C., deSouza, R. M., Giraldo, D. M., & Uff, C. E. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169328 · Cited by 123 · see citing works
Motor proteins at the mitochondria–cytoskeleton interface
Kruppa, A. J., & Buß, F. (2021) · Journal of Cell Science · doi:10.1242/jcs.226084 · Cited by 121 · see citing works
Zhang, Z., Yan, J., Bowman, A. B., Bryan, M. R., Singh, R., & Aschner, M. (2019) · Autophagy · doi:10.1080/15548627.2019.1688488 · Cited by 116 · see citing works
Challenges of modifying disease progression in prediagnostic Parkinson's disease
Salat, D., Noyce, A. J., Schrag, A. E., & TOLOSA, E. S. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)00060-0 · Cited by 119 · see citing works
Neuropathogenesis-on-chips for neurodegenerative diseases
Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 120 · see citing works
Mitochondrial dysfunction and increased glycolysis in prodromal and early Parkinson's blood cells
Smith, A. M., Depp, C., Ryan, B. J., Johnston, G. I., Alegre‐Abarrategui, J., Evetts, S. G., Rolinski, M., Baig, F., Ruffmann, C., Simon, A. K., et al. (2018) · Movement Disorders · doi:10.1002/mds.104 · Cited by 114 · see citing works
Self-citationEpigenetic regulation in Parkinson’s disease
Labbé, C., Lorenzo‐Betancor, O., & Ross, O. A. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1590-9 · Cited by 115 · see citing works
Celastrol Inhibits Dopaminergic Neuronal Death of Parkinson’s Disease through Activating Mitophagy
Lin, M., Lin, C., Chen, Y., Yang, H.-B., & Hung, S. (2019) · Antioxidants · doi:10.3390/antiox9010037 · Cited by 115 · see citing works
Neuroprotection through flavonoid: Enhancement of the glyoxalase pathway
Frandsen, J. R., & Narayanasamy, P. (2017) · Redox Biology · doi:10.1016/j.redox.2017.10.015 · Cited by 112 · see citing works
ROS as Regulators of Mitochondrial Dynamics in Neurons
Cid‐Castro, C., Hernández-Espinosa, D. R., & Morán, J. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-018-0584-7 · Cited by 111 · see citing works
Application of Precision Medicine in Neurodegenerative Diseases
Strafella, C., Caputo, V., Galota, R. M., Zampatti, S., Marella, G. L., Mauriello, S., Cascella, R., & Giardina, E. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00701 · Cited by 111 · see citing works
Que, R., Zheng, J., Chang, Z., Zhang, W., Li, H., Xie, Z., Huang, Z., Wang, H., Xu, J., Jin, D., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.794770 · Cited by 111 · see citing works
Mitochondria: A Therapeutic Target for Parkinson’s Disease?
Luo, Y., Hoffer, A., Hoffer, B. J., & Qi, X. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160920704 · Cited by 107 · see citing works
Myosin VI-Dependent Actin Cages Encapsulate Parkin-Positive Damaged Mitochondria
Kruppa, A. J., Kishi‐Itakura, C., Masters, T. A., Rorbach, J., Grice, G. L., Kendrick‐Jones, J., Nathan, J. A., Minczuk, M. A., & Buß, F. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.01.007 · Cited by 109 · see citing works
Mitophagy and reactive oxygen species interplay in Parkinson’s disease
Xiao, B., Kuruvilla, J., & Tan, E. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00402-y · Cited by 112 · see citing works
Liu, H., Ho, P. W., Leung, C.-T., Pang, S. Y.-Y., Chang, E. E. S., Choi, Z. Y.-K., Kung, M. H.-W., Ramsden, D. B., & Ho, S. (2020) · Autophagy · doi:10.1080/15548627.2020.1850008 · Cited by 109 · 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
Autophagy in Parkinson’s Disease
Nechushtai, L., Frenkel, D., & Pinkas‐Kramarski, R. (2023) · Biomolecules · doi:10.3390/biom13101435 · Cited by 102 · see citing works
Reynolds, R. H., Botía, J. A., Nalls, M. A., Noyce, A. J., Nicolas, A., Cookson, M., Bandrés‐Ciga, S., Gibbs, J. R., Hernandez, D. G., Singleton, A., et al. (2019) · npj Parkinson s Disease · doi:10.1038/s41531-019-0076-6 · Cited by 100 · see citing works
Gumeni, S., Papanagnou, E., Manola, M. S., & Trougakos, I. P. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03952-w · Cited by 100 · see citing works
Mitochondrial Transplantation as a Novel Therapeutic Strategy for Mitochondrial Diseases
Park, A., Oh, M., Lee, S. H., Oh, K., Lee, E., Lee, S.-W., Bae, K., Han, B., & Kim, W. Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094793 · Cited by 97 · see citing works
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 96 · see citing works
Chen, Y., Li, M., Cai, Z., Chen, Y., Wang, L., Teng, J., Feng, Q., Li, C., Rein, G., Tang, B. Q., et al. (2020) · Chinese Medicine · doi:10.4236/cm.2020.113007 · Cited by 92 · see citing works
Scopoletin: a review of its pharmacology, pharmacokinetics, and toxicity
Gao, X., Li, X.-Y., Zhang, C.-Y., & Bai, C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1268464 · Cited by 104 · see citing works
Current perspective of mitochondrial biology in Parkinson's disease
Kaidery, N. A., & Thomas, B. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.03.001 · Cited by 92 · see citing works
Han, X., Zhu, J., Zhang, X., Song, Q., Ding, J., Lu, M., Sun, S., & Hu, G. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00397 · Cited by 91 · see citing works
Denzer, I., Münch, G. W., & Friedland, K. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.11.019 · Cited by 90 · see citing works
Targeting α‐synuclein aggregation and its role in mitochondrial dysfunction in Parkinson's disease
Haque, M. E., Akther, M., Azam, S., Kim, I., Lin, Y., Lee, Y., & Choi, D. (2021) · British Journal of Pharmacology · doi:10.1111/bph.15684 · Cited by 91 · see citing works
Mitophagy-driven mitochondrial rejuvenation regulates stem cell fate
Vázquez‐Martín, A., den Haute, C. V., Cufí, S., Corominas-Faja, B., Cuyàs, E., López‐Bonet, E., Rodríguez‐Gallego, E., Fernández‐Arroyo, S., Joven, J., Baekelandt, V., et al. (2016) · Aging · doi:10.18632/aging.100976 · Cited by 88 · see citing works
- Authors
- Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R.
- Affiliations
- University of Oxford (GB)
- Montreal Neurological Institute and Hospital (CA)
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 40
- Issue
- 4
- Pages
- 200-210
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2021439462
- Cited by
- 524
- References
- 115
- Citations by year
- 2026: 25 · 2025: 30 · 2024: 37 · 2023: 28 · 2022: 45 · 2021: 65 · 2020: 56 · 2019: 50 · 2018: 63 · 2017: 53 · 2016: 52 · 2015: 20
- FWCI
- 8.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Parkinson's UK (J-0901)
- Canadian Institutes of Health Research
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Keywords
- Parkinson's disease, mitochondrial dysfunction, mitophagy, PINK1, Parkin, alpha-synuclein, LRRK2, dopaminergic neurons, familial Parkinson's disease, sporadic Parkinson's disease, neurodegeneration, treatment options
- MeSH terms
- Animals, Humans, Mitochondria, Parkinson Disease, alpha-Synuclein
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
