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

Sequence and organization of the human mitochondrial genome

Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,640 · see citing works

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works

Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis

Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914 · see citing works

Autophagy and Viruses: Adversaries or Allies?

Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,441 · see citing works

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · 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

Mitochondrial Fission, Fusion, and Stress

Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · 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

Mechanisms of mitophagy

Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works

α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies

Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 3,151 · see citing works

Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · 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

Anesthesiology

Wiklund, R. A., & Rosenbaum, S. H. (1997) · New England Journal of Medicine · doi:10.1056/nejm199710163371606 · Cited by 2,159 · see citing works

Parkinson's Disease

Lang, A. E., & Lozano, A. M. (1998) · New England Journal of Medicine · doi:10.1056/nejm199810083391506 · Cited by 2,041 · see citing works

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · see citing works

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

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

Movement of Bax from the Cytosol to Mitochondria during Apoptosis

Wolter, K. G., Hsu, Y., Smith, C. L., Nechushtan, A., Xi, X., & Youle, R. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.5.1281 · Cited by 1,809 · 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 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

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

High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease

Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570 · see citing works

Rotenone, Paraquat, and Parkinson’s Disease

Tanner, C. M., Kamel, F., Ross, G. W., Hoppin, J. A., Goldman, S. M., Korell, M., Marras, C., Bhudhikanok, G. S., Kasten, M., Chade, A. R., et al. (2011) · Environmental Health Perspectives · doi:10.1289/ehp.1002839 · Cited by 1,485 · 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

Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction

Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 1× · see citing works

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · see citing works

Autophagy-deficient mice develop multiple liver tumors

Takamura, A., Komatsu, M., Hara, T., Sakamoto, A., Kishi, C., Waguri, S., Eishi, Y., Hino, O., Tanaka, K., & Mizushima, N. (2011) · Genes &amp; Development · doi:10.1101/gad.2016211 · Cited by 1,342 · see citing works

PINK1-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

Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine

Nicklas, W. J., Vyas, I. L., & Heikkila, R. E. (1985) · Life Sciences · doi:10.1016/0024-3205(85)90146-8 · Cited by 1,266 · see citing works

Parkinsonism-inducing neurotoxin, N-methyl-4-phenyl-1,2,3,6 -tetrahydropyridine: uptake of the metabolite N-methyl-4-phenylpyridine by dopamine neurons explains selective toxicity.

Javitch, J. A., D’Amato, R. J., Strittmatter, S. M., & Snyder, S. H. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.7.2173 · Cited by 1,264 · see citing works

A Role for Ubiquitin in Selective Autophagy

Kirkin, V., McEwan, D. G., Novak, I., & Đikić, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,227 · see citing works

Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants

Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works

Parkinson's disease. Second of two parts.

Lang, A., & Lozano, A. (1998) · New England Journal of Medicine · doi:10.1056/nejm199810153391607 · Cited by 1,193 · 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

Mitochondrial Import and Accumulation of α-Synuclein Impair Complex I in Human Dopaminergic Neuronal Cultures and Parkinson Disease Brain

Devi, L., Raghavendran, V., Prabhu, B. M., Avadhani, N. G., & Anandatheerthavarada, H. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710012200 · Cited by 1,087 · see citing works

A mitochondrial specific stress response in mammalian cells

Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · 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

Mitochondrial Dysfunction and Oxidative Damage in parkin-deficient Mice

Palacino, J. J., Sagi, D., Goldberg, M. S., Krauss, S., Motz, C., Wacker, M., Klose, J., & Shen, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401135200 · Cited by 995 · see citing works

Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy

Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works

PARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease

Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953 · see citing works

PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · see citing works

Parkin-deficient Mice Exhibit Nigrostriatal Deficits but Not Loss of Dopaminergic Neurons

Goldberg, M. S., Fleming, S. M., Palacino, J. J., Cepeda, C., Lam, H. A., Bhatnagar, A., Meloni, E. G., Wu, N., Ackerson, L. C., Klapstein, G. J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308947200 · Cited by 913 · see citing works

Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy

Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · 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 DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons

Kraytsberg, Y., Kudryavtseva, E., McKee, A. C., Geula, C., Kowall, N. W., & Khrapko, K. (2006) · Nature Genetics · doi:10.1038/ng1778 · Cited by 884 · see citing works

The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy

Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., Foreman, O., Kirkpatrick, D. S., & Sheng, M. (2014) · Nature · doi:10.1038/nature13418 · Cited by 855 · see citing works

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · 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

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

p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

Narendra, D. P., Kane, L. A., Hauser, D. N., Fearnley, I. M., & Youle, R. J. (2010) · Autophagy · doi:10.4161/auto.6.8.13426 · Cited by 789 · see citing works

The Interplay Between Mitochondrial Dynamics and Mitophagy

Twig, G., & Shirihai, O. S. (2011) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works

CENTRAL CERVICAL CORD SYNDROME AFTER HEADING A FOOTBALL

Scoppetta, C., & Vaccario, M. L. (1978) · The Lancet · doi:10.1016/s0140-6736(78)92517-5 · Cited by 755 · see citing works

Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control

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

<i>Drosophila</i> Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin

Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735 · see citing works

Mitochondrial 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

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

Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis

Ordureau, 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

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

PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death

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

Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin

Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works

PINK1 is degraded through the N-end rule pathway

Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works

A Sensitive and Quantitative Technique for Detecting Autophagic Events Based on Lysosomal Delivery

Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T., & Miyawaki, A. (2011) · Chemistry &amp; Biology · doi:10.1016/j.chembiol.2011.05.013 · Cited by 650 · see citing works

Environmental risk factors and Parkinson's disease

Liou, H., Tsai, M.-C., Chen, C., Jeng, J., Chang, Y. C., Chen, S. Y., & Chen, R.-T. (1997) · Neurology · doi:10.1212/wnl.48.6.1583 · Cited by 616 · see citing works

Parkin Mediates Proteasome-dependent Protein Degradation and Rupture of the Outer Mitochondrial Membrane

Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612 · see citing works

PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1

Pridgeon, J. W., Olzmann, J. A., Chin, L.-S., & Li, L. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050172 · Cited by 596 · see citing works

The ubiquitin ligase parkin mediates resistance to intracellular pathogens

Manzanillo, P. S., Ayres, J. S., Watson, R. O., Collins, A. C., Souza, G., Rae, C. S., Schneider, D. S., Nakamura, K., Shiloh, M. U., & Cox, J. S. (2013) · Nature · doi:10.1038/nature12566 · Cited by 588 · see citing works

PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy

Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., & Hattori, N. (2012) · Scientific Reports · doi:10.1038/srep01002 · Cited by 577 · see citing works

UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids

Wenzel, D. M., Lissounov, A., Brzović, P. S., & Klevit, R. E. (2011) · Nature · doi:10.1038/nature09966 · Cited by 560 · 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

Parkinsonism, premature menopause, and mitochondrial DNA polymerase γ mutations: clinical and molecular genetic study

Luoma, P., Melberg, A., Rinne, J. O., Kaukonen, J. A., Nupponen, N. N., Chalmers, R. M., Oldfors, A., Rautakorpi, I., Peltonen, L., Majamaa, K., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16983-3 · Cited by 548 · see citing works

Impaired dopamine release and synaptic plasticity in the striatum of PINK1 -deficient mice

Kitada, T., Pisani, A., Porter, D. R., Yamaguchi, H., Tscherter, A., Martella, G., Bonsi, P., Zhang, C., Pothos, E. N., & Shen, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702717104 · Cited by 541 · 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

Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy

Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 517 · see citing works

Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse

Itier, J. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg239 · Cited by 507 · see citing works

Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin

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

Localization of a Novel Locus for Autosomal Recessive Early-Onset Parkinsonism, PARK6, on Human Chromosome 1p35-p36

Valente, E. M., Bentivoglio, A. R., Dixon, P. H., Ferraris, A., Ialongo, T., Frontali, M., Albanese, A., & Wood, N. W. (2001) · The American Journal of Human Genetics · doi:10.1086/319522 · Cited by 493 · see citing works

Prevalence of Parkinson's disease in the elderly

de Rijk, M. C., Breteler, M. M. B., Graveland, G. A., Ott, A., Grobbee, D. E., van der Meché, F. G. A., & Albert Hofman, D. (1995) · Neurology · doi:10.1212/wnl.45.12.2143 · Cited by 488 · see citing works

Image-based genome-wide siRNA screen identifies selective autophagy factors

Orvedahl, A., Sumpter, R., Xiao, G., Ng, A., Zou, Z., Tang, Y., Narimatsu, M., Gilpin, C. J., Sun, Q., Roth, M. G., et al. (2011) · Nature · doi:10.1038/nature10546 · Cited by 486 · see citing works

The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo

Vincow, E. S., Merrihew, G., Thomas, R. E., Shulman, N. J., Beyer, R. P., MacCoss, M. J., & Pallanck, L. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221132110 · Cited by 478 · see citing works

Parkin-deficient mice are not a robust model of parkinsonism

Perez, F. A., & Palmiter, R. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409598102 · Cited by 477 · see citing works

The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1

Plun‐Favreau, H., Klupsch, K., Moisoi, N., Gandhi, S., Kjaer, S., Frith, D., Harvey, K., Deas, E., Harvey, R. J., McDonald, N. Q., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1644 · Cited by 476 · see citing works

Parkin Protein Deficiency Exacerbates Cardiac Injury and Reduces Survival following Myocardial Infarction

Kubli, D. A., Zhang, X., Lee, Y., Hanna, R. A., Quinsay, M. N., Nguyen, C. K., Jimenez, R., Petrosyan, S., Murphy, A. N., & Gustafsson, Å. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411363 · Cited by 476 · 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

Susceptibility to leprosy is associated with PARK2 and PACRG

Mira, M. T., Alcaïs, A., Thuc, N. V., Moraes, M. O., Flumeri, C. D., Thai, V. H., Phuong, M. C., Hương, N. T., Ba, N. N., Khoa, P. X., et al. (2004) · Nature · doi:10.1038/nature02326 · Cited by 467 · 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

Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress

Pesah, Y., Pham, T., Burgess, H., Middlebrooks, B. W., Verstreken, P., Zhou, Y., Harding, M. J., Bellen, H. J., & Mardon, G. (2004) · Development · doi:10.1242/dev.01095 · Cited by 441 · see citing works

The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway

Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440 · see citing works

ROS-induced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy

Wang, Y., Nartiss, Y., Steipe, B., McQuibban, G. A., & Kim, P. K. (2012) · Autophagy · doi:10.4161/auto.21211 · Cited by 427 · see citing works

Increased glutathione S -transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease

Whitworth, A. J., Theodore, D. A., Greene, J. C., Beneš, H., Wes, P. D., & Pallanck, L. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501078102 · Cited by 421 · see citing works

p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding

Itakura, E., & Mizushima, N. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009067 · Cited by 418 · see citing works

Energy-dependent uptake of N-methyl-4-phenylpyridinium, the neurotoxic metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine, by mitochondria.

Ramsay, R. R., & Singer, T. P. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57434-8 · Cited by 415 · see citing works

PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function

Billia, F., Hauck, L., Konecny, F., Rao, V., Shen, J., & Mak, T. W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106291108 · Cited by 414 · see citing works

The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria

Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works

AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1

Strappazzon, F., Nazio, F., Corrado, M., Cianfanelli, V, Romagnoli, A., Fimia, G. M., Campello, S., Nardacci, R., Piacentini, M., Campanella, M., et al. (2015) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2014.139 · Cited by 399 · see citing works

p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria

Okatsu, K., Saisho, K., Shimanuki, M., Nakada, K., Shitara, H., Sou, Y., Kimura, M., Sato, S., Hattori, N., Komatsu, M., et al. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01426.x · Cited by 397 · cited 3× · see citing works

Parkin and PINK1: much more than mitophagy

Scarffe, L. A., Stevens, D. A., Dawson, V. L., & Dawson, T. M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.004 · Cited by 392 · see citing works

Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 iPS cells

Seibler, P., Graziotto, J., Jeong, H., Šimunović, F., Klein, C., & Krainc, D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4441-10.2011 · Cited by 384 · see citing works

Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway

Unoki, M., & Nakamura, Y. (2001) · Oncogene · doi:10.1038/sj.onc.1204608 · Cited by 382 · see citing works

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking

Meißner, C., Lorenz, H., Weihofen, A., Selkoe, D. J., & Lemberg, M. K. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07253.x · Cited by 375 · see citing works

USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin

Durcan, T. M., Tang, M. Y., Pérusse, J. R., Dashti, E. A., Aguileta, M. A., McLelland, G., Gros, P., Shaler, T. A., Faubert, D., Coulombe, B., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201489729 · Cited by 375 · 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

Localization of a gene for an autosomal recessive form of juvenile Parkinsonism to chromosome 6q25.2-27.

Matsumine, H., Saito, M., Shimoda‐Matsubayashi, S., Tanaka, H., Ishikawa, A., Nakagawa-Hattori, Y., Yokochi, M., Kobayashi, T., Igarashi, S., Takano, H., et al. (1997) · Europe PMC (PubMed Central) · Cited by 371 · see citing works

Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases

Riley, B. E., Lougheed, J. C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T. A., Walker, D., Yang, Y., Regnström, K. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2982 · Cited by 368 · see citing works

High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy

Hasson, S. A., Kane, L. A., Yamano, K., Huang, C.-H., Sliter, D. A., Buehler, E., Wang, C., Heman-Ackah, S. M., Hessa, T., Guha, R., et al. (2013) · Nature · doi:10.1038/nature12748 · Cited by 365 · 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

Loss of locus coeruleus neurons and reduced startle in parkin null mice

von Coelln, R., Thomas, B., Savitt, J. M., Lim, K. L., Sasaki, M., Hess, E. J., Dawson, V. L., & Dawson, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401297101 · Cited by 347 · see citing works

Preconditioning Involves Selective Mitophagy Mediated by Parkin and p62/SQSTM1

Huang, C., Andres, A. M., Ratliff, E. P., Hernandez, G., Lee, P. P. W., & Gottlieb, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020975 · Cited by 344 · see citing works

Sulfhydration mediates neuroprotective actions of parkin

Vandiver, M. S., Paul, B. D., Xu, R., Karuppagounder, S. S., Rao, F., Snowman, A. M., Ko, H. S., Lee, Y. I., Dawson, V. L., Dawson, T. M., et al. (2013) · Nature Communications · doi:10.1038/ncomms2623 · Cited by 343 · see citing works

Mitochondrial Quality Control Mediated by PINK1 and Parkin: Links to ParkinsonismPreprint

Narendra, D. P., Walker, J. E., & Youle, R. J. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011338 · Cited by 341 · see citing works

Autoregulation of Parkin activity through its ubiquitin‐like domain

Chaugule, V. K., Burchell, L., Barber, K. R., Sidhu, A., Leslie, S. J., Shaw, G. S., & Walden, H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.204 · Cited by 339 · see citing works

The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy

Cornelissen, T., Haddad, D., Wauters, F., Humbeeck, C. V., Mandemakers, W. J., Koentjoro, B., Sue, C. M., Gevaert, K., Strooper, B. D., Verstreken, P., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu244 · Cited by 337 · see citing works

Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells

Suen, D., Narendra, D. P., Tanaka, A., Manfredi, G., & Youle, R. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914569107 · Cited by 335 · see citing works

Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan

Rana, A., Rera, M., & Walker, D. W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216197110 · Cited by 335 · see citing works

Structure of the human Parkin ligase domain in an autoinhibited state

Wauer, T., & Komander, D. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.125 · Cited by 334 · see citing works

MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin

Yun, J., Puri, R., Yang, H. M., Lizzio, M. A., Wu, C., Sheng, Z., & Guo, M. (2014) · eLife · doi:10.7554/elife.01958 · Cited by 325 · see citing works

The genetics and neuropathology of Parkinson’s disease

Houlden, H., & Singleton, A. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1013-5 · Cited by 320 · see citing works

The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations

Geisler, S., Holmström, K. M., Treis, A., Skujat, D., Weber, S. S., Fiesel, F. C., Kahle, P. J., & Springer, W. (2010) · Autophagy · doi:10.4161/auto.6.7.13286 · Cited by 311 · cited 6× · see citing works

Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy

Yamano, K., Fogel, A. I., Wang, C., van der Bliek, A. M., & Youle, R. J. (2014) · eLife · doi:10.7554/elife.01612 · Cited by 307 · see citing works

Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo

Sterky, F. H., Lee, S., Wibom, R., Olson, L., & Larsson, N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103295108 · Cited by 296 · see citing works

Molecular genetic analysis of a novel Parkin gene in Japanese families with autosomal recessive juvenile parkinsonism: Evidence for variable homozygous deletions in the Parkin gene in affected individuals

Hattori, N., Kitada, T., Matsumine, H., Asakawa, S., Yamamura, Y., Yoshino, H., Kobayashi, T., Yokochi, M., Wang, M., Yoritaka, A., et al. (1998) · Annals of Neurology · doi:10.1002/ana.410440612 · Cited by 295 · see citing works

Parkin Interacts with Ambra1 to Induce Mitophagy

Van Humbeeck, C., Cornelissen, T., Hofkens, H., Mandemakers, W., Gevaert, K., De Strooper, B., & Vandenberghe, W. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.1917-11.2011 · Cited by 287 · cited 1× · see citing works

Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy

Itakura, E., Kishi-Itakura, C., Koyama-Honda, I., & Mizushima, N. (2012) · Journal of Cell Science · doi:10.1242/jcs.094110 · Cited by 286 · 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

Mutant A53T α-Synuclein Induces Neuronal Death by Increasing Mitochondrial Autophagy

Choubey, V., Safiulina, D., Vaarmann, A., Cagalinec, M., Warȩski, P., Kuum, M., Zharkovsky, A., & Kaasik, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132514 · Cited by 261 · see citing works

Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila

Cha, G., Kim, S., Park, J., Lee, E., Kim, M., Lee, S. B., Kim, J., Chung, J., & Cho, K. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500346102 · Cited by 261 · see citing works

Characterization of PINK1 processing, stability, and subcellular localization

Lin, W., & Kang, U. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05398.x · Cited by 261 · see citing works

Absence of nigral degeneration in aged parkin/DJ‐1/PINK1 triple knockout mice

Kitada, T., Tong, Y., Gautier, C., & Shen, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06350.x · Cited by 260 · 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

PINK1-linked parkinsonism is associated with Lewy body pathology

Samaranch, L., Lorenzo‐Betancor, O., Arbelo, J. M., Ferrer, I., Lorenzo, E., Irigoyen, J., Pastor, M. A., Marrero, C., Isla, C., Herrera-Henriquez, J., et al. (2010) · Brain · doi:10.1093/brain/awq051 · Cited by 256 · see citing works

Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage

Kageyama, Y., Zhang, Z., Roda, R. H., Fukaya, M., Wakabayashi, J., Wakabayashi, N., Kensler, T. W., Reddy, P. H., Iijima, M., & Sesaki, H. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201110034 · Cited by 256 · see citing works

A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment

Okatsu, K., Uno, M., Koyano, F., Go, E., Kimura, M., Oka, T., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.509653 · Cited by 248 · see citing works

PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding

Lazarou, M., Narendra, D. P., Jin, S. M., Tekle, E., Banerjee, S., & Youle, R. J. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201210111 · Cited by 247 · see citing works

The Scaffold Protein Atg11 Recruits Fission Machinery to Drive Selective Mitochondria Degradation by Autophagy

Mao, K., Wang, K., Liu, X., & Klionsky, D. J. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.024 · Cited by 247 · see citing works

Lewy body Parkinson's disease in a large pedigree with 77Parkin mutation carriers

Pramstaller, P. P., Schlossmacher, M. G., Jacques, T. S., Scaravilli, F., Eskelson, C., Pepivani, I., Hedrich, K., Adel, S., McNeal, M. G., Hilker, R., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20587 · Cited by 244 · see citing works

Substrate Specificity of Rhomboid Intramembrane Proteases Is Governed by Helix-Breaking Residues in the Substrate Transmembrane Domain

Urban, S., & Freeman, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00181-3 · Cited by 241 · see citing works

VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations

Kim, N. C., Tresse, E., Kolaitis, R., Molliex, A., Thomas, R. E., Alami, N. H., Wang, B., Joshi, A., Smith, R. B., Ritson, G. P., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.029 · Cited by 240 · see citing works

Mutations in PINK1 and Parkin Impair Ubiquitination of Mitofusins in Human Fibroblasts

Raković, A., Grünewald, A., Kottwitz, J., Brüggemann, N., Pramstaller, P. P., Lohmann, K., & Klein, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016746 · Cited by 234 · see citing works

Phenotypic characterization of recessive gene knockout rat models of Parkinson's disease

Dave, K. D., Silva, S., Sheth, N. P., Ramboz, S., Beck, M. J., Quang, C., Switzer, R. C., Ahmad, S. O., Sunkin, S. M., Walker, D., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.009 · Cited by 222 · see citing works

Bcl-2 Family Proteins Participate in Mitochondrial Quality Control by Regulating Parkin/PINK1-Dependent Mitophagy

Hollville, É., Carroll, R. G., Cullen, S. P., & Martin, S. J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.001 · Cited by 221 · see citing works

Phosphatase and Tensin Homolog (PTEN)-induced Putative Kinase 1 (PINK1)-dependent Ubiquitination of Endogenous Parkin Attenuates Mitophagy

Rakovic, A., Shurkewitsch, K., Seibler, P., Grünewald, A., Zanon, A., Hagenah, J., Krainc, D., & Klein, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.391680 · Cited by 218 · see citing works

Calcium Entry and -Synuclein Inclusions Elevate Dendritic Mitochondrial Oxidant Stress in Dopaminergic Neurons

Dryanovski, D. I., Guzmán, J. N., Xie, Z., Galteri, D. J., Volpicelli‐Daley, L. A., Lee, V. M. Y., Miller, R. J., Schumacker, P. T., & Surmeier, D. J. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5311-12.2013 · Cited by 213 · see citing works

Piecemeal Microautophagy of the Nucleus Requires the Core Macroautophagy Genes

Krick, R., Mühe, Y., Prick, T., Bremer, S., Schlotterhose, P., Eskelinen, E., Millen, J. I., Goldfarb, D. S., & Thumm, M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-04-0363 · Cited by 212 · see citing works

The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING‐IBR‐RING domain and the unique LDD extension

Smit, J. J., Monteferrario, D., Noordermeer, S. M., van Dijk, W. J., van der Reijden, B. A., & Sixma, T. K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.217 · Cited by 210 · see citing works

The E3 Ligase Parkin Maintains Mitochondrial Integrity by Increasing Linear Ubiquitination of NEMO

Müller-Rischart, A. K., Pilsl, A., Beaudette, P., Patra, M., Hadian, K., Funke, M., Peis, R., Deinlein, A., Schweimer, C., Kuhn, P., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.036 · Cited by 210 · see citing works

Mutations in Fis1 disrupt orderly disposal of defective mitochondria

Shen, Q., Yamano, K., Head, B. P., Kawajiri, S., Cheung, J. T. M., Wang, C., Cho, J.-H., Hattori, N., Youle, R. J., & van der Bliek, A. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0525 · Cited by 209 · see citing works

Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation

Iguchi, M., Kujuro, Y., Okatsu, K., Koyano, F., Kosako, H., Kimura, M., Suzuki, N., Uchiyama, S., Tanaka, K., & Matsuda, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.467530 · Cited by 209 · see citing works

Tissue- and cell-type–specific manifestations of heteroplasmic mtDNA 3243A>G mutation in human induced pluripotent stem cell-derived disease model

Hämäläinen, R. H., Manninen, T., Koivumäki, H., Kislin, M., Otonkoski, T., & Suomalainen, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311660110 · Cited by 201 · see citing works

Depletion of PINK1 affects mitochondrial metabolism, calcium homeostasis and energy maintenance

Heeman, B., Van den Haute, C., Aelvoet, S.-A., Valsecchi, F., Rodenburg, R. J., Reumers, V., Debyser, Z., Callewaert, G., Koopman, W. J. H., Willems, P. H. G. M., et al. (2011) · Journal of Cell Science · doi:10.1242/jcs.078303 · Cited by 198 · see citing works

Genetic and genomic studies of Drosophila parkin mutants implicate oxidative stress and innate immune responses in pathogenesis

Greene, J. C., Whitworth, A. J., Andrews, L. A., Parker, T. J., & Pallanck, L. J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi074 · Cited by 194 · see citing works

Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission

Liu, W., Acín-Peréz, R., Geghman, K. D., Manfredi, G., Lu, B., & Li, C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107332108 · Cited by 190 · see citing works

The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax

Johnson, B. N., Berger, A. K., Cortese, G. P., & LaVoie, M. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113248109 · Cited by 189 · see citing works

Increased Mitochondrial Calcium Sensitivity and Abnormal Expression of Innate Immunity Genes Precede Dopaminergic Defects in Pink1-Deficient Mice

Akundi, R. S., Huang, Z., Eason, J., Pandya, J. D., Zhi, L., Cass, W. A., Sullivan, P. G., & Büeler, H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016038 · Cited by 187 · see citing works

Homozygous deletions in parkin gene in European and North African families with autosomal recessive juvenile parkinsonism

Lücking, C. B., Abbas, N., Dürr, A., Bonifati, V., Bonnet, A. M., de Broucker, T., Michele, G. D., Wood, N. W., Agid, Y., & Brice, A. (1998) · The Lancet · doi:10.1016/s0140-6736(05)60746-5 · Cited by 187 · see citing works

The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process

Park, J., Lee, G., & Chung, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.086 · Cited by 181 · see citing works

Point Mutations (Thr240Arg and Ala311Stop) in theParkinGene

Hattori, N., Matsumine, H., Asakawa, S., Kitada, T., Yoshino, H., Elibol, B., Brookes, A. J., Yamamura, Y., Kobayashi, T., Wang, M., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9134 · Cited by 181 · see citing works

Mono- and double-mutant mouse models of Parkinson's disease display severe mitochondrial damage

Stichel, C. C., Zhu, X., Bader, V., Linnartz‐Gerlach, B., Schmidt, S., & Lübbert, H. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm083 · Cited by 179 · see citing works

Mitofusin 2 is necessary for striatal axonal projections of midbrain dopamine neurons

Lee, S., Sterky, F. H., Mourier, A., Terzioglu, M., Cullheim, S., Olson, L., & Larsson, N. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds352 · Cited by 177 · see citing works

Mitochondrial autophagy in cells with mtDNA mutations results from synergistic loss of transmembrane potential and mTORC1 inhibition

Gilkerson, R., de Vries, R. L. A., Lebot, P., Wikström, J. D., Törgyekes, E., Shirihai, O. S., Przedborski, S., & Schon, E. A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr529 · Cited by 169 · see citing works

Functional interplay between Parkin and Drp1 in mitochondrial fission and clearance

Buhlman, L. M., Damiano, M. G., Bertolin, G., Ferrando-Miguel, R., Lombès, A., Brice, A., & Corti, O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.012 · Cited by 165 · see citing works

Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregation

Meng, F., Yao, D., Shi, Y., Kabakoff, J., Wu, W., Reicher, J. J., Ma, Y., Moosmann, B., Masliah, E., Lipton, S. A., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-34 · Cited by 165 · see citing works

Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function

Periquet, M., Corti, O., Jacquier, S., & Brice, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03442.x · Cited by 160 · see citing works

Deletions in the Parkin gene and genetic heterogeneity in a Greek family with early onset Parkinson's disease

Leroy, E., Anastasopoulos, D., Konitsiotis, S., Lavedan, C. N., & Polymeropoulos, M. H. (1998) · Human Genetics · doi:10.1007/s004390050845 · Cited by 159 · see citing works

Fluorescence-Based Sensors to Monitor Localization and Functions of Linear and K63-Linked Ubiquitin Chains in Cells

van Wijk, S. J. L., Fiškin, E., Putyrski, M., Pampaloni, F., Hou, J., Wild, P. S., Kensche, T., Grecco, H. E., Bastiaens, P. I. H., & Đikić, I. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.017 · Cited by 155 · see citing works

Mitochondrial Contagion Induced by Parkin Deficiency in Drosophila Hearts and Its Containment by Suppressing Mitofusin

Bhandari, P., Song, M., Chen, Y., Burelle, Y., & Dorn, G. W. (2013) · Circulation Research · doi:10.1161/circresaha.114.302734 · Cited by 153 · see citing works

Novel Monoclonal Antibodies Demonstrate Biochemical Variation of Brain Parkin with Age

Pawlyk, A. C., Giasson, B. I., Sampathu, D. M., Perez, F. A., Lim, K. L., Dawson, V. L., Dawson, T. M., Palmiter, R. D., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306889200 · Cited by 149 · see citing works

Parkin and mitochondrial quality control: toward assembling the puzzle

Winklhofer, K. F. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.01.001 · Cited by 149 · see citing works

A molecular explanation for the recessive nature of parkin-linked Parkinson’s disease

Spratt, D. E., Martinez-Torres, R. J., Noh, Y. J., Mercier, P., Manczyk, N., Barber, K. R., Aguirre, J. D., Burchell, L., Purkiss, A. G., Walden, H., et al. (2013) · Nature Communications · doi:10.1038/ncomms2983 · Cited by 144 · see citing works

Identification of a Novel Zn2+-binding Domain in the Autosomal Recessive Juvenile Parkinson-related E3 Ligase Parkin

Hristova, V. A., Beasley, S., Rylett, R. J., & Shaw, G. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808700200 · Cited by 142 · see citing works

Bit-by-bit autophagic removal of parkin-labelled mitochondria

Yang, J., & Yang, W. Y. (2013) · Nature Communications · doi:10.1038/ncomms3428 · Cited by 140 · see citing works

Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity

Kazlauskaite, A., Kelly, V. C., Johnson, C., Baillie, C., Hastie, C. J., Peggie, M. W., Macartney, T., Woodroof, H. I., Alessi, D. R., Pedrioli, P. G. A., et al. (2014) · Open Biology · doi:10.1098/rsob.130213 · Cited by 136 · see citing works

Genome-wide RNAi screen identifies the Parkinson disease GWAS risk locus <i>SREBF1</i> as a regulator of mitophagy

Ivatt, R. M., Sanchez-Martinez, A., Godena, V. K., Brown, S., Ziviani, E., & Whitworth, A. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321207111 · Cited by 130 · see citing works

Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson’s disease

Costa, 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

PINK1-Parkin Pathway Activity Is Regulated by Degradation of PINK1 in the Mitochondrial Matrix

Thomas, R. E., Andrews, L. A., Burman, J. L., Lin, W.-Y., & Pallanck, L. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004279 · Cited by 129 · see citing works

Genetic analysis of mitochondrial protein misfolding in Drosophila melanogaster

Pimenta de Castro, I., Costa, A. C., Lam, D., Tufi, R., Fedele, V, Moisoi, N., Dinsdale, D., Deas, E., Loh, S. H. Y., & Martins, L. M. (2012) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2012.5 · Cited by 128 · see citing works

Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling

Sims, J. J., Scavone, F., Cooper, E. M., Kane, L. A., Youle, R. J., Boeke, J. D., & Cohen, R. E. (2012) · Nature Methods · doi:10.1038/nmeth.1888 · Cited by 121 · see citing works

Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy

Abeliovich, H., Zarei, M., Rigbolt, K. T. G., Youle, R. J., & Dengjel, J. (2013) · Nature Communications · doi:10.1038/ncomms3789 · Cited by 119 · see citing works

PARK6-linked parkinsonism occurs in several European families.

Valente, E. M., Brancati, F., Ferraris, A., Graham, E. A., Davis, M. B., Breteler, M. M. B., Gasser, T., Bonifati, V., Bentivoglio, A. R., Michele, G. D., et al. (2002) · PubMed · Cited by 110 · see citing works

The Yeast Complex I Equivalent NADH Dehydrogenase Rescues pink1 Mutants

Vilain, S., Esposito, G., Haddad, D., Schaap, O., Dobreva, M. P., Vos, M. H., Meensel, S. V., Morais, V. A., Strooper, B. D., & Verstreken, P. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002456 · Cited by 110 · see citing works

UBE2N, UBE2L3 and UBE2D2/3 ubiquitin-conjugating enzymes are essential for parkin-dependent mitophagy

Geisler, S., Vollmer, S., Golombek, S., & Kahle, P. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.146035 · Cited by 109 · 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

Park6‐linked parkinsonism occurs in several european families

Valente, E. M., Brancati, F., Ferraris, A., Graham, E. A., Davis, M. B., Breteler, M. M. B., Gasser, T., Bonifati, V., Bentivoglio, A. R., Michele, G. D., et al. (2001) · Annals of Neurology · doi:10.1002/ana.10053 · Cited by 107 · 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

Role of Membrane Association and Atg14-Dependent Phosphorylation in Beclin-1-Mediated Autophagy

Fogel, A. I., Dlouhy, B. J., Wang, C., Ryu, S., Neutzner, A., Hasson, S. A., Sideris, D. P., Abeliovich, H., & Youle, R. J. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00079-13 · Cited by 97 · see citing works

Hexokinase activity is required for recruitment of parkin to depolarized mitochondria

McCoy, M. K., Kaganovich, A., Rudenko, I. N., Ding, J., & Cookson, M. R. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt407 · Cited by 97 · see citing works

Muscle choline kinase beta defect causes mitochondrial dysfunction and increased mitophagy

Mitsuhashi, S., Hatakeyama, H., Karahashi, M., Koumura, T., Nonaka, I., Hayashi, Y. K., Noguchi, S., Sher, R. B., Nakagawa, Y., Manfredi, G., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr305 · Cited by 95 · see citing works

Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism

Zheng, X., & Hunter, T. R. (2013) · Cell Research · doi:10.1038/cr.2013.66 · Cited by 94 · 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

Regulation of mitochondrial permeability transition pore by PINK1

Gautier, C., Giaime, E., Caballero, E., Núñez, L., Song, Z., Chan, D. C., Villalobos, C., & Shen, J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-22 · Cited by 91 · see citing works

Inclusion Body Formation and Neurodegeneration Are Parkin Independent in a Mouse Model of α-Synucleinopathy

von Coelln, R., Thomas, B., Andrabi, S. A., Lim, K. L., Savitt, J. M., Saffary, R., Stirling, W. L. H., Bruno, K. J., Hess, E. J., Lee, M. K., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0414-06.2006 · Cited by 90 · 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

Loss-of-Function Analysis Suggests ThatOmi/HtrA2Is Not an Essential Component of thepink1/parkinPathwayIn Vivo

Yun, J., Cao, J. H., Dodson, M. W., Clark, I. E., Kapahi, P., Chowdhury, R. B., & Guo, M. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5141-08.2008 · Cited by 85 · see citing works

Genome-wide RNAi screen identifies ATPase inhibitory factor 1 (ATPIF1) as essential for PARK2 recruitment and mitophagy

Lefebvre, V., Du, Q., Baird, S. D., Ng, A. C., Nascimento, M., Campanella, M., McBride, H. M., & Screaton, R. A. (2013) · Autophagy · doi:10.4161/auto.25413 · Cited by 78 · see citing works

Erratum: AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1

Strappazzon, F., Nazio, F., Corrado, M., Cianfanelli, V., Romagnoli, A., Fimia, G. M., Campello, S., Nardacci, R., Piacentini, M., Campanella, M., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.190 · Cited by 78 · see citing works

Role of the Ubiquitin Conjugation System in the Maintenance of Mitochondrial Homeostasis

Neutzner, A., Bénard, G., Youle, R. J., & Karbowski, M. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.012 · Cited by 75 · see citing works

PINK1-Mediated Phosphorylation of Parkin Boosts Parkin Activity in Drosophila

Shiba‐Fukushima, K., Inoshita, T., Hattori, N., & Imai, Y. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004391 · Cited by 73 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).

Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works

Parkinson disease

Poewe, W., Seppi, K., Tanner, C. M., Halliday, G. M., Brundin, P., Volkmann, J., Schrag, A.-E., & Lang, A. E. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.13 · Cited by 5,415 · see citing works

Ageing as a risk factor for neurodegenerative disease

Hou, Y., Dan, X., Babbar, M., Wei, Y., Hasselbalch, S. G., Croteau, D. L., & Bohr, V. A. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0244-7 · Cited by 3,310 · see citing works

The PI3K Pathway in Human Disease

Fruman, D. A., Chiu, H., Hopkins, B. D., Bagrodia, S., Cantley, L. C., & Abraham, R. T. (2017) · Cell · doi:10.1016/j.cell.2017.07.029 · Cited by 2,749 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) ¹

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works

Oxidative Stress: A Key Modulator in Neurodegenerative Diseases

Singh, A., Kukreti, R., Saso, L., & Kukreti, S. (2019) · Molecules · doi:10.3390/molecules24081583 · Cited by 2,305 · see citing works

Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance

Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081 · see citing works

Hallmarks of neurodegenerative diseases

Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works

The mitochondrial basis of aging

Sun, N., Youle, R. J., & Finkel, T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.028 · Cited by 1,441 · see citing works

Molecular mechanisms and physiological functions of mitophagy

Onishi, M., Yamano, K., Sato, M., Matsuda, N., & Okamoto, K. (2021) · The EMBO Journal · doi:10.15252/embj.2020104705 · Cited by 1,429 · see citing works

Autophagy in healthy aging and disease

Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313 · see citing works

Mitochondrial dynamics in health and disease: mechanisms and potential targets

Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306 · see citing works

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

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

NF-κB Restricts Inflammasome Activation via Elimination of Damaged Mitochondria

Zhong, Z., Umemura, A., Sanchez-Lopez, E., Liang, S., Shalapour, S., Wong, J., He, F., Boassa, D., Perkins, G., Ali, S. R., et al. (2016) · Cell · doi:10.1016/j.cell.2015.12.057 · Cited by 1,197 · see citing works

Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities

Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134 · see citing works

Neuronal Cell Death

Fricker, M., Tolkovsky, A. M., Borutaitė, V., Coleman, M. P., & Brown, G. C. (2018) · Physiological Reviews · doi:10.1152/physrev.00011.2017 · Cited by 1,122 · 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

Cargo recognition and degradation by selective autophagy

Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067 · see citing works

Mechanisms of Deubiquitinase Specificity and Regulation

Mevissen, T. E. T., & Komander, D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044916 · Cited by 1,035 · see citing works

The mechanisms and roles of selective autophagy in mammals

Vargas, J. N. S., Hamasaki, M., Kawabata, T., Youle, R. J., & Yoshimori, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00542-2 · Cited by 1,030 · see citing works

The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy

Heo, J.-M., Ordureau, A., Paulo, J. A., Rinehart, J., & Harper, J. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.016 · Cited by 906 · see citing works

Mitochondria–lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis

Wong, Y. C., Ysselstein, D., & Krainc, D. (2018) · Nature · doi:10.1038/nature25486 · Cited by 885 · 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

Mitochondrial dysfunction in Parkinson's disease

Bose, A., & Beal, M. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13731 · Cited by 598 · see citing works

Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor

Wei, Y., Chiang, W., Sumpter, R., Mishra, P., & Levine, B. (2016) · Cell · doi:10.1016/j.cell.2016.11.042 · Cited by 853 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

The mammalian ULK1 complex and autophagy initiation

Zachari, M., & Ganley, I. G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170021 · Cited by 789 · see citing works

Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans

Palikaras, K., Lionaki, E., & Tavernarakis, N. (2015) · Nature · doi:10.1038/nature14300 · Cited by 770 · see citing works

Autophagy as a promoter of longevity: insights from model organisms

Hansen, M., Rubinsztein, D. C., & Walker, D. W. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0033-y · Cited by 754 · see citing works

Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria

Richter, B., Sliter, D. A., Herhaus, L., Stolz, A., Wang, C., Beli, P., Zaffagnini, G., Wild, P., Martens, S., Wagner, S. A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523926113 · Cited by 755 · see citing works

Brain metabolism in health, aging, and neurodegeneration

Camandola, S., & Mattson, M. P. (2017) · The EMBO Journal · doi:10.15252/embj.201695810 · Cited by 752 · see citing works

Deciphering the Molecular Signals of PINK1/Parkin Mitophagy

Nguyen, T. N., Padman, B. S., & Lazarou, M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.008 · Cited by 732 · see citing works

Role of pyroptosis in inflammation and cancer

Xiang, W. D., Xie, F., Zhou, X., Wu, Y., Yan, H., Liu, T., Huang, J. S., Wang, F., Zhou, F., & Zhang, L. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00905-x · Cited by 715 · see citing works

Building and decoding ubiquitin chains for mitophagy

Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 668 · see citing works

AUTACs: Cargo-Specific Degraders Using Selective Autophagy

Takahashi, D., Moriyama, J., Nakamura, T., Miki, E., Takahashi, E., Sato, A., Akaike, T., Itto-Nakama, K., & Arimoto, H. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.009 · Cited by 675 · see citing works

Autophagy genes in biology and disease

Yamamoto, H., Zhang, S., & Mizushima, N. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-022-00562-w · Cited by 631 · see citing works

Basal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand

McWilliams, T. G., Prescott, A. R., Montava-Garriga, L., Ball, G., Singh, F., Barini, E., Muqit, M. M. K., Brooks, S. P., & Ganley, I. G. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.008 · Cited by 591 · see citing works

Parkinson’s Disease-Related Proteins PINK1 and Parkin Repress Mitochondrial Antigen Presentation

Matheoud, D., Sugiura, A., Bellemare-Pelletier, A., Laplante, A., Rondeau, C., Chemali, M., Fazel, A., Bergeron, J. J., Trudeau, L.-E., Burelle, Y., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.039 · Cited by 582 · see citing works

Parkinson's disease: Mechanisms, translational models and management strategies

Raza, C., Anjum, R., & Shakeel, N. U. A. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.057 · Cited by 604 · see citing works

Parkinson’s Disease: Etiology, Neuropathology, and Pathogenesis

Kouli, A., Torsney, K., & Kuan, W. (2018) · Codon Publications eBooks · doi:10.15586/codonpublications.parkinsonsdisease.2018.ch1 · Cited by 556 · see citing works

Mitostasis in Neurons: Maintaining Mitochondria in an Extended Cellular Architecture

Misgeld, T., & Schwarz, T. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.055 · Cited by 546 · see citing works

The role of PINK1–Parkin in mitochondrial quality control

Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 580 · see citing works

Mitochondrial Dysfunction in Parkinson’s Disease: New Mechanistic Insights and Therapeutic Perspectives

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

PINK1 and Parkin mitochondrial quality control: a source of regional vulnerability in Parkinson’s disease

Ge, P., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00367-7 · Cited by 514 · see citing works

Selective autophagy of intracellular organelles: Recent research advances

Li, W., He, P., Huang, Y., Li, Y.-F., Lu, J., Li, M., Kurihara, H., Luo, Z., Meng, T., Onishi, M., et al. (2020) · Theranostics · doi:10.7150/thno.49860 · Cited by 510 · see citing works

Role of Cardiolipin in Mitochondrial Function and Dynamics in Health and Disease: Molecular and Pharmacological Aspects

Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2019) · Cells · doi:10.3390/cells8070728 · Cited by 504 · see citing works

Ubiquitin ligases in oncogenic transformation and cancer therapy

Senft, D., Qi, J., & Ronai, Z. A. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.105 · Cited by 490 · see citing works

Oxidative Stress and Advanced Lipoxidation and Glycation End Products (ALEs and AGEs) in Aging and Age-Related Diseases

Moldogazieva, N. T., Mokhosoev, I. M., Melnikova, T. I., Porozov, Y. B., & Terentiev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3085756 · Cited by 504 · see citing works

Oxidative stress and cellular pathologies in Parkinson’s disease

Puspita, L., Chung, S. Y., & Shim, J. (2017) · Molecular Brain · doi:10.1186/s13041-017-0340-9 · Cited by 486 · see citing works

Mitochondrial biogenesis and dynamics in the developing and diseased heart

Dorn, G. W., Vega, R. B., & Kelly, D. P. (2015) · Genes &amp; Development · doi:10.1101/gad.269894.115 · Cited by 470 · see citing works

Mechanism of phospho-ubiquitin-induced PARKIN activation

Wauer, T., Šimíček, M., Schubert, A. F., & Komander, D. (2015) · Nature · doi:10.1038/nature14879 · Cited by 479 · see citing works

Siderophores in Iron Metabolism: From Mechanism to Therapy Potential

Wilson, B., Bogdan, A. R., Miyazawa, M., Hashimoto, K., & Tsuji, Y. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.10.005 · Cited by 479 · see citing works

Mitochondrial fission facilitates the selective mitophagy of protein aggregates

Burman, J. L., Pickles, S., Wang, C., Sekine, S., Vargas, J. N. S., Zhang, Z., Youle, A. M., Nezich, C. L., Wu, X., Hammer, J. A., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612106 · Cited by 479 · see citing works

Signaling pathways in Parkinson’s disease: molecular mechanisms and therapeutic interventions

Xu, D.-C., Yong, C., Xu, Y., Chen-Yu, S., & Peng, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01353-3 · Cited by 498 · see citing works

Mitochondrial autophagy: molecular mechanisms and implications for cardiovascular disease

Li, A., Gao, M. Q., Liu, B., Qin, Y. H., Chen, L., Liu, H., Wu, H., & Gong, G. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04906-6 · Cited by 469 · see citing works

The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective

Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436 · see citing works

Defects in trafficking bridge Parkinson’s disease pathology and genetics

Abeliovich, A., & Gitler, A. D. (2016) · Nature · doi:10.1038/nature20414 · Cited by 462 · see citing works

Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice

Gong, G., Song, M., Csordás, G., Kelly, D. P., Matkovich, S. J., & Dorn, G. W. (2015) · Science · doi:10.1126/science.aad2459 · Cited by 441 · see citing works

E3 ubiquitin ligases: styles, structures and functions

Yang, Q., Zhao, J., Chen, D., & Wang, Y. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00043-2 · Cited by 435 · see citing works

A Molecular Approach to Mitophagy and Mitochondrial Dynamics.

Yoo, S., & Jung, Y. (2018) · PubMed Central · doi:10.14348/molcells.2018.2277 · Cited by 447 · see citing works

Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles

Yao, R.-Q., Ren, C., Xia, Z.-F., & Yao, Y.-M. (2021) · Autophagy · doi:10.1080/15548627.2020.1725377 · Cited by 441 · see citing works

Loss of VPS13C Function in Autosomal-Recessive Parkinsonism Causes Mitochondrial Dysfunction and Increases PINK1/Parkin-Dependent Mitophagy

Lesage, S., Drouet, V., Majounie, E., Deramecourt, V., Jacoupy, M., Nicolas, A., Cormier‐Dequaire, F., Hassoun, S. M., Pujol, C., Ciura, S., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.01.014 · Cited by 438 · see citing works

Mechanisms of autophagy–lysosome dysfunction in neurodegenerative diseases

Nixon, R. A., & Rubinsztein, D. C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00757-5 · Cited by 435 · see citing works

PHB2 (prohibitin 2) promotes PINK1-PRKN/Parkin-dependent mitophagy by the PARL-PGAM5-PINK1 axis

Yan, C., Gong, L., Chen, L., Xu, M., Abou‐Hamdan, H., Tang, M., Désaubry, L., & Song, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1628520 · Cited by 416 · see citing works

Mitochondrial dysfunction in Parkinson’s disease – a key disease hallmark with therapeutic potential

Henrich, M. T., Oertel, W. H., Surmeier, D. J., & Geibl, F. F. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00676-7 · Cited by 435 · see citing works

Cell biology of the mitochondrion

van der Bliek, A. M., Sedensky, M. M., & Morgan, P. G. (2017) · Genetics · doi:10.1534/genetics.117.300262 · Cited by 388 · see citing works

Mechanism of parkin activation by PINK1

Gladkova, C., Maslen, S., Skehel, M. J., & Komander, D. (2018) · Nature · doi:10.1038/s41586-018-0224-x · Cited by 390 · see citing works

Mitophagy programs: mechanisms and physiological implications of mitochondrial targeting by autophagy

Hamacher‐Brady, A., & Brady, N. R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2087-8 · Cited by 396 · see citing works

Microglia and astrocyte dysfunction in parkinson's disease

Kam, T., Hinkle, J. T., Dawson, T. M., & Dawson, V. L. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105028 · Cited by 399 · see citing works

Autophagy in acute kidney injury

Kaushal, G. P., & Shah, S. V. (2016) · Kidney International · doi:10.1016/j.kint.2015.11.021 · Cited by 389 · see citing works

Autophagy and cancer stem cells: molecular mechanisms and therapeutic applications

Nazio, F., Bordi, M., Cianfanelli, V., Locatelli, F., & Cecconi, F. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0292-y · Cited by 391 · 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

Nuclear DNA damage signalling to mitochondria in ageing

Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works

Synaptopathies: synaptic dysfunction in neurological disorders – A review from students to students

Lepeta, K., Lourenco, M. V., Schweitzer, B. C., Martino Adami, P. V., Banerjee, P., Catuara‐Solarz, S., de La Fuente Revenga, M., Guillem, A. M., Haidar, M., Ijomone, O. M., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13713 · Cited by 386 · see citing works

Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease

Bridi, J. C., & Hirth, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00080 · Cited by 381 · see citing works

mTOR Controls Mitochondrial Dynamics and Cell Survival via MTFP1

Morita, M., Prudent, J., Basu, K., Goyon, V., Katsumura, S., Hulea, L., Pearl, D., Siddiqui, N., Strack, S., McGuirk, S., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.013 · Cited by 368 · see citing works

Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities

Schmidt, M. F., Gan, Z. Y., Komander, D., & Dewson, G. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00706-7 · Cited by 373 · see citing works

Disease Modification in Parkinson's Disease: Current Approaches, Challenges, and Future Considerations

Lang, A. E., & Espay, A. J. (2018) · Movement Disorders · doi:10.1002/mds.27360 · Cited by 374 · see citing works

Intrinsically Disordered Protein TEX264 Mediates ER-phagy

Chino, H., Hatta, T., Natsume, T., & Mizushima, N. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.033 · Cited by 362 · see citing works

The role of mitochondria in aging

Jang, J. Y., Blum, A., Liu, J., & Finkel, T. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120842 · Cited by 358 · see citing works

Mitophagy 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

PINK1 and BECN1 relocalize at mitochondria-associated membranes during mitophagy and promote ER-mitochondria tethering and autophagosome formation

Gelmetti, V., Rosa, P. D., Torosantucci, L., Marini, E. S., Romagnoli, A., Rienzo, M. D., Arena, G., Vignone, D., Fimia, G. M., & Valente, E. M. (2017) · Autophagy · doi:10.1080/15548627.2016.1277309 · Cited by 355 · see citing works

Basal mitophagy is widespread in Drosophila but minimally affected by loss of Pink1 or parkin

Lee, J. J., Sánchez-Martínez, Á., Martinez, A., Benincá, C., Mayor, U., Clague, M. J., & Whitworth, A. J. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201801044 · Cited by 343 · see citing works

Crosstalk between mitochondrial dysfunction, oxidative stress, and age related neurodegenerative disease: Etiologies and therapeutic strategies

Elfawy, H. A., & Das, B. B. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.029 · Cited by 343 · see citing works

Regulation and Function of Mitochondria–Lysosome Membrane Contact Sites in Cellular Homeostasis

Wong, Y., Kim, S., Peng, W. J., & Krainc, D. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.004 · Cited by 319 · see citing works

Mitochondrial dysfunction in aging

Guo, Y., Guan, T., Shafiq, K., Yu, Q., Jiao, X., Na, D., Li, M., Zhang, G., & Kong, J. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101955 · Cited by 350 · see citing works

Elimination of paternal mitochondria in mouse embryos occurs through autophagic degradation dependent on PARKIN and MUL1

Rojansky, R. B., Cha, M.-Y., & Chan, D. C. (2016) · eLife · doi:10.7554/elife.17896 · Cited by 337 · see citing works

Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond

Bingol, B., & Sheng, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.015 · Cited by 333 · see citing works

Deubiquitinases in cancer

Dewson, G., Eichhorn, P. J. A., & Komander, D. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00633-y · Cited by 337 · see citing works

Endogenous Parkin Preserves Dopaminergic Substantia Nigral Neurons following Mitochondrial DNA Mutagenic Stress

Pickrell, A. M., Huang, C.-H., Kennedy, S. R., Ordureau, A., Sideris, D. P., Hoekstra, J. G., Harper, J. W., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.034 · Cited by 327 · see citing works

PINK1 and Parkin: emerging themes in mitochondrial homeostasis.

McWilliams, T. G., & Muqit, M. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.03.013 · Cited by 315 · 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

A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation

Liang, J. R., Lingeman, E., Luong, T., Ahmed, S., Muhar, M., Nguyen, T., Olzmann, J. A., & Corn, J. E. (2020) · Cell · doi:10.1016/j.cell.2020.02.017 · Cited by 310 · see citing works

Regulation of Liver Metabolism by Autophagy

Madrigal‐Matute, J., & Cuervo, A. M. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.09.042 · Cited by 312 · see citing works

Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy

Ordureau, A., Heo, J.-M., Duda, D. M., Paulo, J. A., Olszewski, J. L., Yanishevski, D., Rinehart, J., Schulman, B. A., & Harper, J. W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506593112 · Cited by 310 · see citing works

How mitochondrial dynamism orchestrates mitophagy

Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311 · see citing works

PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease

Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 306 · see citing works

Emerging therapies in Parkinson disease — repurposed drugs and new approaches

Elkouzi, A., Vedam‐Mai, V., Eisinger, R. S., & Okun, M. S. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0155-7 · Cited by 304 · see citing works

PINK1, Parkin, and Mitochondrial Quality Control: What can we Learn about Parkinson’s Disease Pathobiology?

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

Mitophagy and Parkinson's disease: The PINK1–parkin link

Deas, E., Wood, N. W., & Plun‐Favreau, H. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.08.007 · Cited by 222 · see citing works

Mitochondrial quality control turns out to be the principal suspect in parkin and PINK1-related autosomal recessive Parkinson's disease

Corti, O., & Brice, A. (2012) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2012.11.002 · Cited by 76 · see citing works

The function of PINK1 and parkin in mitochondrial quality control (234.2)

Fon, E. A. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.234.2

Mitochondrial Quality Control Mediated by PINK1 and Parkin: Links to ParkinsonismPreprint

Narendra, D. P., Walker, J. E., & Youle, R. J. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011338 · Cited by 341 · see citing works