Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission

Parkinson's Disease

Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469 · see citing works

Chronic systemic pesticide exposure reproduces features of Parkinson's disease

Betarbet, R., Sherer, T., Mackenzie, G., Garcia-Osuna, M., Panov, A., & Greenamyre, J. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,797 · see citing works

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>

Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works

PINK1/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

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 · see citing works

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

Schägger, H., & von JAGOW, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,237 · see citing works

Mitochondria: Dynamic Organelles in Disease, Aging, and Development

Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987 · see citing works

Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells

Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938 · see citing works

Oxidative stress in neurodegeneration: Cause or consequence?

Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869 · see citing works

Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin

Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works

Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin

Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · see citing works

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works

Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A

Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works

Abnormalities of the electron transport chain in idiopathic parkinson's disease

Parker, W. D., Boyson, S. J., & Parks, J. K. (1989) · Annals of Neurology · doi:10.1002/ana.410260606 · Cited by 1,061 · see citing works

Loss of PINK1 Function Promotes Mitophagy through Effects on Oxidative Stress and Mitochondrial Fission

Dagda, R. K., Cherra, S. J., Kulich, S. M., Tandon, A., Park, D., & Chu, C. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808515200 · Cited by 954 · see citing works

The PINK1/Parkin pathway regulates mitochondrial morphology

Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works

Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of <i>Drosophila</i> Pink1 is rescued by Parkin

Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works

Oxidatively modified proteins in aging and disease1, 2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease” The full list of papers may be found on the homepage of the journal

Beal, M. F. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00780-3 · Cited by 763 · see citing works

[42]Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines

Trounce, I. A., Kim, Y. L., Jun, A. S., & Wallace, D. C. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64044-0 · Cited by 749 · see citing works

Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress

Gautier, C. A., Kitada, T., & Shen, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802076105 · Cited by 698 · see citing works

Parkinson's Disease α-Synuclein Transgenic Mice Develop Neuronal Mitochondrial Degeneration and Cell Death

Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684 · see citing works

The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila

Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works

Anatomic and Disease Specificity of NADH CoQ1 Reductase (Complex I) Deficiency in Parkinson's Disease

Schapira, A. H. V., Mann, V. M., Cooper, J. A. D., Dexter, D. T., Daniel, S. E., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb05809.x · Cited by 673 · see citing works

Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery

Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 536 · see citing works

Mitochondria, Oxidative Damage, and Inflammation in Parkinson's Disease

Beal, M. F. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07470.x · Cited by 523 · see citing works

Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function

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

Parkinson Phenotype in Aged PINK1-Deficient Mice Is Accompanied by Progressive Mitochondrial Dysfunction in Absence of Neurodegeneration

Gispert, S., Ricciardi, F., Kurz, A., Azizov, M., Hoepken, H.-H., Becker, D., Voos, W., Leuner, K., Müller, W. E., Kudin, A. P., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005777 · Cited by 382 · see citing works

Intersecting pathways to neurodegeneration in Parkinson's disease: Effects of the pesticide rotenone on DJ-1, α-synuclein, and the ubiquitin–proteasome system

Betarbet, R. S., Canet-Aviles, R., Sherer, T., Mastroberardino, P. G., McLendon, C., Kim, J.-H., Lund, S. A., Na, H. M., Taylor, G., Bence, N., et al. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.12.003 · Cited by 342 · see citing works

Mitochondrial oxidative phosphorylation defects in parkinson's disease

Shoffner, J. M., Watts, R. L., Juncos, J. L., Torroni, A., & Wallace, D. C. (1991) · Annals of Neurology · doi:10.1002/ana.410300304 · Cited by 333 · see citing works

PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons

Wood-Kaczmar, A., Gandhi, S., Yao, Z., Abramov, A. S. Y., Miljan, E. A., Keen, G., Stanyer, L., Hargreaves, I., Klupsch, K., Deas, E., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002455 · Cited by 316 · see citing works

The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy

Michiorri, S., Gelmetti, V, Giarda, E., Lombardi, F., Romano, F., Marongiu, R., Nerini-Molteni, S., Sale, P., Vago, R., Arena, G., et al. (2010) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2009.200 · Cited by 260 · see citing works

MITOCHONDRIAL FUNCTION IN PARKINSON'S DISEASE

Bindoff, L. A., Birch‐Machin, M. A., Cartlidge, N. E. F., Parker, W. D., & Turnbull, D. M. (1989) · The Lancet · doi:10.1016/s0140-6736(89)90291-2 · Cited by 245 · see citing works

Silencing of PINK1 Expression Affects Mitochondrial DNA and Oxidative Phosphorylation in DOPAMINERGIC Cells

Gegg, M. E., Cooper, J. M., Schapira, A. H. V., & Taanman, J.-W. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004756 · Cited by 198 · see citing works

OPA1 (Kjer Type) Dominant Optic Atrophy: A Novel Mitochondrial Disease

Delettre, C., Lenaers, G., Pelloquin, L., Belenguer, P., & Hamel, C. (2002) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2001.3278 · Cited by 191 · see citing works

The role of mitochondria in inherited neurodegenerative diseases

Kwong, J. Q., Beal, M. F., & Manfredi, G. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03990.x · Cited by 180 · see citing works

Mitochondrial Alterations in PINK1 Deficient Cells Are Influenced by Calcineurin-Dependent Dephosphorylation of Dynamin-Related Protein 1

Matton, A., Craig, K. J. T., Beilina, A. G., van der Brug, M., Harwig, M. C., Ahmad, R., Miller, D. W., Zambrano, I., Cowburn, R. F., Behbahani, H., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005701 · Cited by 176 · see citing works

PINK1 Defect Causes Mitochondrial Dysfunction, Proteasomal Deficit and α-Synuclein Aggregation in Cell Culture Models of Parkinson's Disease

Liu, W., Vives-Bauzá, C., Acín‐Pérez, R., Yamamoto, A., Tan, Y.-C., Li, Y., Magrané, J., Stavarache, M. A., Shaffer, S., Chang, S. H., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004597 · Cited by 135 · see citing works

Mechanistic Approaches to Parkinson's Disease Pathogenesis

Betarbet, R. S., Sherer, T., Monte, D. A. D., & Greenamyre, J. T. (2002) · Brain Pathology · doi:10.1111/j.1750-3639.2002.tb00468.x · Cited by 134 · see citing works

Obligatory Role for Complex I Inhibition in the Dopaminergic Neurotoxicity of 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Richardson, J. R., Caudle, W. M., Guillot, T. S., Watson, J. L., Nakamaru‐Ogiso, E., Seo, B. B., Sherer, T., Greenamyre, J. T., Yagi, T., Matsuno‐Yagi, A., et al. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl133 · Cited by 117 · see citing works

Endometrial Pinopodes and Uterine Receptivity

Nikas, G., & Makrigiannakis, A. (2003) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1290.042 · Cited by 115 · see citing works

Assay of Mitochondrial ATP Synthesis in Animal Cells and Tissues

Vives-Bauzá, C., Yang, L., & Manfredi, G. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80007-5 · Cited by 111 · see citing works

Modeling mitochondrial function in aging neurons

Melov, S. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.08.004 · Cited by 111 · see citing works

Hypersensitivity to oxygen and shortened lifespan in a <i>Drosophila</i> mitochondrial complex II mutant

Walker, D. W., Hájek, P., Muffat, J., Knoepfle, D., Cornelison, S., Attardi, G., & Benzer, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607918103 · Cited by 105 · see citing works

Oxidative stress and aging reduce COX I RNA and cytochrome oxidase activity in Drosophila

Schwarze, S. R., Weindruch, R. H., & Aiken, J. M. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00153-1 · Cited by 97 · see citing works

Mitochondrial DNA background modifies the bioenergetics of NARP/MILS ATP6 mutant cells

D’Aurelio, M., Vives-Bauzá, C., Davidson, M. M., & Manfredi, G. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp503 · Cited by 90 · see citing works

Leucine-rich repeat kinase 2: A new player with a familiar theme for Parkinson's disease pathogenesis

Li, C., & Beal, M. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508350102 · Cited by 17 · see citing works

The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease

Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310 · see citing works

Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease

Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works

Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.

Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274 · see citing works

Mitochondrial Dynamics — Mitochondrial Fission and Fusion in Human Diseases

Archer, S. L. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1215233 · Cited by 1,103 · see citing works

Mitochondrial Defects and Oxidative Stress in Alzheimer Disease and Parkinson Disease

Yan, M. H., Wang, X., & Zhu, X. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.014 · Cited by 718 · see citing works

PINK1 deficiency impairs mitochondrial homeostasis and promotes lung fibrosis

Bueno, M., Lai, Y.-C., Romero, Y., Brands, J., St. Croix, C. M., Kamga, C., Corey, C., Herazo-Maya, J. D., Sembrat, J., Lee, J. S., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci74942 · Cited by 627 · see citing works

The aging lung: Physiology, disease, and immunity

Schneider, J. L., Rowe, J. H., Garcia-de-Alba, C., Kim, C. F., Sharpe, A. H., & Haigis, M. C. (2021) · Cell · doi:10.1016/j.cell.2021.03.005 · Cited by 500 · see citing works

Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner

Frank, M., Duvezin-Caubet, S., Koob, S., Occhipinti, A., Jagasia, R., Petcherski, A., Ruonala, M. O., Priault, M., Salin, B., & Reichert, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.007 · Cited by 468 · see citing works

The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity

Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4130 · Cited by 453 · see citing works

Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology

Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 396 · see citing works

Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria

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

PINK1 Loss-of-Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling

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

The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons

Wang, W., Li, L., Lin, W.-L., Dickson, D. W., Petrucelli, L., Zhang, T., & Wang, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt319 · Cited by 340 · see citing works

BNIP3 Protein Suppresses PINK1 Kinase Proteolytic Cleavage to Promote Mitophagy

Zhang, T., Xue, L., Li, L., Tang, C., Wan, Z., Wang, R., Tan, J., Tan, Y., Han, H., Tian, R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733410 · Cited by 285 · see citing works

Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases

Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250 · see citing works

Inhibition of mitophagy drives macrophage activation and antibacterial defense during sepsis

Patoli, D., Mignotte, F., Deckert, V., Dusuel, A., Dumont, A., Rieu, A., Jalil, A., Dongen, K. V., Bourgeois, T., Gautier, T., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci130996 · Cited by 248 · see citing works

Abnormal Mitochondrial Dynamics in the Pathogenesis of Alzheimer's Disease

Zhu, X., Perry, G., Smith, M. A., & Wang, X. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129005 · Cited by 242 · see citing works

Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation

Su, Y.-C., & Qi, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt301 · Cited by 221 · see citing works

Alterations in Mitochondrial Quality Control in Alzheimer’s Disease

Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 215 · see citing works

PINK1 and Parkin Control Localized Translation of Respiratory Chain Component mRNAs on Mitochondria Outer Membrane

Gehrke, S., Wu, Z., Klinkenberg, M., Sun, Y., Auburger, G. W. J., Guo, S., & Lu, B. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.007 · Cited by 213 · see citing works

Mitochondrial dynamics and transport in Alzheimer's disease

Flannery, P. J., & Trushina, E. V. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.06.009 · Cited by 198 · see citing works

Antioxidant gene therapy against neuronal cell death

Navarro-Yepes, J., Zavala-Flores, L. M., Anandhan, A., Wang, F., Skotak, M., Chandra, N., Li, M., Pappa, A., Martínez‐Fong, D., Razo, L. M. D., et al. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.007 · Cited by 177 · see citing works

Inhibition of mitochondrial fragmentation protects against Alzheimer’s disease in rodent model

Wang, W., Yin, J., Ma, X., Zhao, F., Siedlak, S. L., Wang, Z., Torres, S., Fujioka, H., Xu, Y., Perry, G., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx299 · Cited by 175 · see citing works

A Small Molecule Promotes Mitochondrial Fusion in Mammalian Cells

Wang, D., Wang, J., Bonamy, G. M. C., Meeusen, S., Brusch, R. G., Turk, C. N., Yang, P., & Schultz, P. G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204589 · Cited by 162 · see citing works

The role of mitochondrial DNA mutation on neurodegenerative diseases

Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 153 · see citing works

Inhibition of Drp1 mitochondrial translocation provides neural protection in dopaminergic system in a Parkinson’s disease model induced by MPTP

Filichia, E., Hoffer, B., Qi, X., & Luo, Y. (2016) · Scientific Reports · doi:10.1038/srep32656 · Cited by 155 · see citing works

Mitochondria initiate and regulate sarcopenia

Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153 · see citing works

Cyanidin‐3‐O‐glucoside improves non‐alcoholic fatty liver disease by promoting PINK1‐mediated mitophagy in mice

Li, X., Shi, Z., Zhu, Y., Shen, T., Wang, H., Shui, G., Loor, J. J., Fang, Z., Chen, M., Wang, X., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15083 · Cited by 145 · see citing works

A Mitocentric View of Parkinson's Disease

Haelterman, N. A. T., Yoon, W. H., Sandoval, H., Jaiswal, M., Shulman, J. M., & Bellen, H. J. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014317 · Cited by 138 · see citing works

Mitochondrial Respiratory Chain Supercomplexes: From Structure to Function

Guan, S., Zhao, L., & Peng, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213880 · Cited by 142 · see citing works

A review of genome‐wide transcriptomics studies in Parkinson's disease

Borrageiro, G., Haylett, W. L., Seedat, S., Kuivaniemi, H., & Bardien, S. (2017) · European Journal of Neuroscience · doi:10.1111/ejn.13760 · Cited by 117 · see citing works

PINK1-mediated mitophagy protects against hepatic ischemia/reperfusion injury by restraining NLRP3 inflammasome activation

Xu, Y., Tang, Y., Lu, J., Zhang, W., Zhu, Y., Zhang, S., Ma, G., Jiang, P., & Zhang, W. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.015 · Cited by 113 · see citing works

Mitochondrial Dynamics: The Intersection of Form and Function

Ferree, A. W., & Shirihai, O. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_2 · Cited by 110 · see citing works

PINK1-mediated Drp1S616 phosphorylation modulates synaptic development and plasticity via promoting mitochondrial fission

Gao, Q., Tian, R., Han, H., Slone, J. D., Wang, C., Ke, X., Zhang, T., Li, X., He, Y., Liao, P., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00933-z · Cited by 109 · see citing works

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 106 · see citing works

Mfn2 ablation causes an oxidative stress response and eventual neuronal death in the hippocampus and cortex

Jiang, S., Nandy, P., Wang, W., Ma, X., Hsia, J., Wang, C., Wang, Z., Niu, M., Siedlak, S. L., Torres, S. L., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0238-8 · Cited by 104 · see citing works

MFN2 couples glutamate excitotoxicity and mitochondrial dysfunction in motor neurons

Wang, W., Zhang, F., Li, L., Tang, F., Siedlak, S. L., Fujioka, H., Liu, Y., Su, B., Pi, Y., & Wang, X. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.617167 · Cited by 103 · see citing works

Function and Characteristics of PINK1 in Mitochondria

Matsuda, S., Kitagishi, Y., & Kobayashi, M. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/601587 · Cited by 102 · see citing works

Role of Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Oxygen Sensing and Constriction of the Ductus Arteriosus

Hong, Z., Kutty, S., Tóth, P. T., Marsboom, G., Hammel, J. M., Chamberlain, C., Ryan, J. J., Zhang, H. J., Sharp, W. W., Morrow, E., et al. (2013) · Circulation Research · doi:10.1161/circresaha.111.300285 · Cited by 99 · see citing works

The mitochondrial kinase PINK 1: functions beyond mitophagy

Voigt, A., Berlemann, L. A., & Winklhofer, K. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13655 · Cited by 98 · see citing works

Mechanisms of Parkinson's Disease

Hewitt, V. L., & Whitworth, A. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.005 · Cited by 94 · see citing works

Probing Mechanisms That Underlie Human Neurodegenerative Diseases in Drosophila

Jaiswal, M., Sandoval, H., Zhang, K., Bayat, V., & Bellen, H. J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155456 · Cited by 95 · see citing works

Genes associated with Parkinson's disease: regulation of autophagy and beyond

Beilina, A. G., & Cookson, M. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13266 · Cited by 93 · see citing works

Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links Co-translational Quality Control to PINK1-Directed Mitophagy

Wu, Z., Wang, Y., Lim, J., Liu, B., Li, Y., Vartak, R. S., Stankiewicz, T. R., Montgomery, S. B., & Lu, B. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.007 · Cited by 84 · 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

PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency

Pirooznia, S. K., Yuan, C., Khan, M. R., Karuppagounder, S. S., Wang, L., Xiong, Y., Kang, S. U., Lee, Y., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00363-x · Cited by 88 · see citing works

Parkinson's Disease Phenotypes in Patient Neuronal Cultures and Brain Organoids Improved by 2‐Hydroxypropyl‐β‐Cyclodextrin Treatment

Jarazo, J., Barmpa, K., Modamio, J., Saraiva, C., Sabaté‐Soler, S., Rosety, I., Griesbeck, A., Skwirblies, F., Zaffaroni, G., Smits, L. M., et al. (2021) · Movement Disorders · doi:10.1002/mds.28810 · Cited by 96 · see citing works

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 83 · see citing works

The Complex I Subunit NDUFA10 Selectively Rescues Drosophila pink1 Mutants through a Mechanism Independent of Mitophagy

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

PINK1 in the limelight: multiple functions of an eclectic protein in human health and disease

Arena, G., & Valente, E. M. (2016) · The Journal of Pathology · doi:10.1002/path.4815 · Cited by 78 · see citing works

Aconitase Causes Iron Toxicity in Drosophila pink1 Mutants

Esposito, G., Vos, M. H., Vilain, S., Swerts, J., Valadas, J. S., Meensel, S. V., Schaap, O., & Verstreken, P. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003478 · Cited by 74 · see citing works

The Parkinson’s gene PINK1 regulates cell cycle progression and promotes cancer-associated phenotypes

O’Flanagan, C. H., Morais, V. A., Wurst, W., Strooper, B. D., & O’Neill, C. (2014) · Oncogene · doi:10.1038/onc.2014.81 · Cited by 75 · see citing works

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 71 · see citing works

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 71 · see citing works

The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease

Trinh, D., Israwi, A. R., Arathoon, L. R., Gleave, J. A., & Nash, J. E. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15154 · Cited by 72 · see citing works

The complicated role of mitochondria in the podocyte

Gujarati, N. A., Vasquez, J. M., Bogenhagen, D. F., & Mallipattu, S. K. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00393.2020 · Cited by 67 · see citing works

CircEPS15, as a sponge of MIR24-3p ameliorates neuronal damage in Parkinson disease through boosting PINK1-PRKN-mediated mitophagy

Zhou, Y., Liu, Y., Kang, Z., Yao, H. P., Song, N., Wang, M., Song, C., Zhang, K., Ding, J., Tang, J., et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2196889 · Cited by 71 · see citing works

Mitochondrial dynamics and mitophagy in Parkinson's disease: A fly point of view

von Stockum, S., Nardin, A., Schrepfer, E., & Ziviani, E. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.11.002 · Cited by 67 · see citing works

SLP-2 interacts with Parkin in mitochondria and prevents mitochondrial dysfunction in Parkin-deficient human iPSC-derived neurons andDrosophila

Zanon, A., Kalvakuri, S., Raković, A., Foco, L., Guida, M., Schwienbacher, C., Serafin, A., Rudolph, F., Trilck, M., Grünewald, A., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx132 · Cited by 67 · see citing works

Mitochondrial dynamic abnormalities in amyotrophic lateral sclerosis

Jiang, Z., Wang, W., Perry, G., Zhu, X., & Wang, X. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0037-x · Cited by 66 · see citing works

Metabolic Stress and Disorders Related to Alterations in Mitochondrial Fission or Fusion.

Babbar, M., & Sheikh, M. S. (2013) · PubMed · Cited by 66 · see citing works

PINK1 signalling in cancer biology

O’Flanagan, C. H., & O’Neill, C. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.10.006 · Cited by 65 · see citing works

The Multifaceted Roles of Zinc in Neuronal Mitochondrial Dysfunction

Liu, H. Y., Gale, J. R., Reynolds, I. J., Weiss, J. H., & Aizenman, E. (2021) · Biomedicines · doi:10.3390/biomedicines9050489 · Cited by 64 · see citing works

Involvement and interplay of Parkin, PINK1, and DJ1 in neurodegenerative and neuroinflammatory disorders

Wilhelmus, M. M. M., Nijland, P. G., Drukarch, B., de Vries, H. E., & van Horssen, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.040 · Cited by 62 · see citing works

Quantitative expression proteomics and phosphoproteomics profile of brain from PINK1 knockout mice: insights into mechanisms of familial Parkinson's disease

Triplett, J. C., Zhang, Z., Sultana, R., Cai, J., Klein, J. B., Büeler, H., & Butterfield, D. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13039 · Cited by 58 · see citing works

A reduction in Drp1-mediated fission compromises mitochondrial health in autosomal recessive spastic ataxia of Charlevoix Saguenay

Bradshaw, T. Y., Romano, L. E. L., Duncan, E. J., Nethisinghe, S., Abeti, R., Michael, G. J., Giunti, P., Vermeer, S., & Chapple, J. P. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw173 · Cited by 58 · see citing works

Mitochondrial dysfunction in Alzheimer’s disease: a key frontier for future targeted therapies

Wang, S., Liao, Z., Zhang, Q., Han, X., Liu, C., & Wang, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1484373 · Cited by 57 · see citing works

From physiology to pathology: Emerging roles of GPER in cardiovascular disease

Wang, Z., Liu, J., Chen, Y., Tang, Y., Chen, T., Zhou, C. S., Wang, S., Chang, R., Chen, Z., Yang, W., et al. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108801 · Cited by 57 · see citing works

Tricornered/NDR kinase signaling mediates PINK1-directed mitochondrial quality control and tissue maintenancePreprint

Wu, Z., Sawada, T., Shiba, K., Liu, S., Kanao, T., Takahashi, R., Hattori, N., Imai, Y., & Lu, B. (2013) · Genes & Development · doi:10.1101/gad.203406.112 · Cited by 56 · see citing works

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Marelja, Z., Leimkühler, S., & Missirlis, F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00050 · Cited by 57 · see citing works

The Parkinson's disease-related genes act in mitochondrial homeostasis

Sai, Y., Zou, Z., Peng, K., & Dong, Z. (2012) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2012.06.007 · Cited by 55 · see citing works

Near-Infrared 808 nm Light Boosts Complex IV-Dependent Respiration and Rescues a Parkinson-Related pink1 Model

Vos, M. H., Lovisa, B., Geens, A., Morais, V. A., Wagnières, G., van den Bergh, H., Ginggen, A., Strooper, B. D., Tardy, Y., & Verstreken, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078562 · Cited by 54 · see citing works

Mitochondrial respiratory chain disorganization in Parkinson's disease-relevant PINK1 and DJ1 mutants

López-Fabuel, I., Martin-Martin, L., Resch-Beusher, M., Azkona, G., Sánchez‐Pernaute, R., & Bolaños, J. P. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.03.023 · Cited by 52 · see citing works

Mitochondrial Supercomplexes: Physiological Organization and Dysregulation in Age-Related Neurodegenerative Disorders

Novack, G. V., Galeano, P., Castaño, E. M., & Morelli, L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00600 · Cited by 52 · see citing works

Bcl-xL Is Necessary for Neurite Outgrowth in Hippocampal Neurons

Park, H., Licznerski, P., Alavian, K. N., Shanabrough, M., & Jonas, E. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5570 · Cited by 49 · see citing works

Parkinson's disease-associated pathogenic VPS35 mutation causes complex I deficits

Zhou, L., Wang, W., Hoppel, C. L., Liu, J., & Zhu, X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.032 · Cited by 49 · see citing works

Conditional deletion of Ndufs4 in dopaminergic neurons promotes Parkinson’s disease-like non-motor symptoms without loss of dopamine neurons

Choi, W., Kim, H.-W., Tronche, F., Palmiter, R. D., Storm, D. R., & Xia, Z. (2017) · Scientific Reports · doi:10.1038/srep44989 · Cited by 48 · see citing works

Mitoplasticity: Adaptation Biology of the Mitochondrion to the Cellular Redox State in Physiology and Carcinogenesis

José, C., Melser, S., Bénard, G., & Rossignol, R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4357 · Cited by 46 · see citing works

Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca 2+ -induced ATP production in cardiac H9c2 myoblasts

O‐Uchi, J., Jhun, B. S., Hurst, S., Bisetto, S., Gross, P., Chen, M., Kettlewell, S., Park, J., Oyamada, H., Smith, G. L., et al. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00094.2013 · Cited by 42 · see citing works

Loss of PINK1 causes age-dependent decrease of dopamine release and mitochondrial dysfunction

Zhi, L., Qin, Q., Muqeem, T., Seifert, E. L., Liu, W., Zheng, S., Li, C., & Zhang, H. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.025 · Cited by 45 · see citing works

Rescue of PINK1 Protein Null-specific Mitochondrial Complex IV Deficits by Ginsenoside Re Activation of Nitric Oxide Signaling

Kim, K., Song, K., Yoon, S., Shehzad, O., Kim, Y.-S., & Son, J. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.408146 · Cited by 45 · see citing works

Dendritic Cells Require PINK1-Mediated Phosphorylation of BCKDE1α to Promote Fatty Acid Oxidation for Immune Function

Basit, F., & de Vries, I. J. M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02386 · Cited by 43 · see citing works

A conserved retromer sorting motif is essential for mitochondrial DLP1 recycling by VPS35 in Parkinson’s disease model

Wang, W., Ma, X., Zhou, L., Liu, J., & Zhu, X. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw430 · Cited by 44 · see citing works

A High-Content Screen Identifies TPP1 and Aurora B as Regulators of Axonal Mitochondrial Transport

Shlevkov, E., Basu, H., Bray, M., Sun, Z., Wei, W., Apaydin, K. Z., Karhohs, K. W., Chen, P.-F., Smith, J. L. M., Wiskow, O., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.035 · Cited by 39 · see citing works

Therapeutic strategies in Parkinson's disease: what we have learned from animal models

Valadas, J. S., Vos, M. H., & Verstreken, P. (2014) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12577 · Cited by 38 · see citing works

PINK1 depletion sensitizes non-small cell lung cancer to glycolytic inhibitor 3-bromopyruvate: Involvement of ROS and mitophagy

Dai, K., Radin, D. P., & Leonardi, D. (2019) · Pharmacological Reports · doi:10.1016/j.pharep.2019.08.002 · Cited by 38 · see citing works

Genetic reduction of mitochondrial complex I function does not lead to loss of dopamine neurons in vivo

Kim, H.-W., Choi, W.-S., Sorscher, N., Park, H. J., Tronche, F., Palmiter, R. D., & Xia, Z. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.008 · Cited by 38 · see citing works

Flies with Parkinson's disease

Vanhauwaert, R., & Verstreken, P. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.02.020 · Cited by 36 · see citing works

Nitric Oxide Induction of Parkin Translocation in PTEN-induced Putative Kinase 1 (PINK1) Deficiency

Han, J., Kang, M., Kim, K., Han, P., Kim, H., Ha, J., & Son, J. H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624767 · Cited by 36 · see citing works

Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection

Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36 · see citing works

Beyond Mitophagy: Cytosolic PINK1 as a Messenger of Mitochondrial Health

Steer, E. K., Dail, M. K., & Chu, C. T. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6206 · Cited by 34 · see citing works

Inhibition of the deubiquitinase USP8 corrects a Drosophila PINK1 model of mitochondria dysfunction

von Stockum, S., Sánchez-Martínez, Á., Corrà, S., Chakraborty, J., Marchesan, E., Locatello, L., Da‐Ré, C., Cusumano, P., Caicci, F., Ferrari, V., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900392 · Cited by 31 · see citing works

Astrocytic Dynamin-Like Protein 1 Regulates Neuronal Protection against Excitotoxicity in Parkinson Disease

Hoekstra, J. G., Cook, T. J., Stewart, T., Mattison, H. A., Dreisbach, M. T., Hoffer, Z. S., & Zhang, J. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.10.022 · Cited by 33 · see citing works

Boosting mitochondrial health to counteract neurodegeneration

Burtscher, J., Romani, M., Bernardo, G., Popa, T., Ziviani, E., Hummel, F. C., Sorrentino, V., & Millet, G. P. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102289 · Cited by 34 · see citing works

Harnessing the Therapeutic Potential of the Nrf2/Bach1 Signaling Pathway in Parkinson’s Disease

Ahuja, M., Kaidery, N. A., Dutta, D., Attucks, O. C., Kazakov, E. H., Gazaryan, I. G., Matsumoto, M., Igarashi, K., Sharma, S. M., & Thomas, B. (2022) · Antioxidants · doi:10.3390/antiox11091780 · Cited by 34 · see citing works

Loss of Pink1 modulates synaptic mitochondrial bioenergetics in the rat striatum prior to motor symptoms: concomitant complex I respiratory defects and increased complex II‐mediated respiration

Stauch, K. L., Villeneuve, L. M., Purnell, P. R., Ottemann, B. M., Emanuel, K. M., & Fox, H. S. (2016) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201600005 · Cited by 31 · see citing works

Pantothenate kinase 2 interacts with PINK1 to regulate mitochondrial quality control via acetyl-CoA metabolism

Huang, Y., Wan, Z., Tang, Y., Xu, J., Laboret, B., Nallamothu, S., Yang, C., Liu, B., Lu, R. O., Lu, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30178-x · Cited by 32 · see citing works

Biomechanistic insights into the roles of oxidative stress in generating complex neurological disorders

Yusuf, M., Khan, M., Robaian, M. A., & Khan, R. A. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0250 · Cited by 31 · see citing works

PINK1 regulates mitochondrial morphology via promoting mitochondrial fission in porcine preimplantation embryos

Niu, Y., Nie, Z., Shin, K., Zhou, W., & Cui, X. (2019) · The FASEB Journal · doi:10.1096/fj.201802473r · Cited by 30 · see citing works

Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery

Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 536 · see citing works

The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila

Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works

The PINK1/Parkin pathway regulates mitochondrial morphology

Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works

PINK1 phosphorylates Drp1S616 to regulate mitophagy‐independent mitochondrial dynamics

Han, H., Tan, J., Wang, R., Wan, H., He, Y., Yan, X., Guo, J., Gao, Q., Li, J., Shang, S., et al. (2020) · EMBO Reports · doi:10.15252/embr.201948686 · Cited by 202 · see citing works

Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of <i>Drosophila</i> Pink1 is rescued by Parkin

Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works