The DOI matches its Crossref record; 209 of the 212 references it cites were found in a registry or an index.
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Open accessAbstract
Understanding the function of genes mutated in hereditary forms of Parkinson's disease yields insight into disease etiology and reveals new pathways in cell biology. Although mutations or variants in many genes increase the susceptibility to Parkinson's disease, only a handful of monogenic causes of parkinsonism have been identified. Biochemical and genetic studies reveal that the products of two genes that are mutated in autosomal recessive parkinsonism, PINK1 and Parkin, normally work together in the same pathway to govern mitochondrial quality control, bolstering previous evidence that mitochondrial damage is involved in Parkinson's disease. PINK1 accumulates on the outer membrane of damaged mitochondria, activates Parkin's E3 ubiquitin ligase activity, and recruits Parkin to the dysfunctional mitochondrion. Then, Parkin ubiquitinates outer mitochondrial membrane proteins to trigger selective autophagy. This review covers the normal functions that PINK1 and Parkin play within cells, their molecular mechanisms of action, and the pathophysiological consequences of their loss.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“PINK1 plays critical roles in mitochondrial quality control, particularly in induction of mitophagy [39].”
From miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1) (2016) · cites this paper as [39]
The cited source says what the claim attributes to it.
In the citing paper
“In PD or AD, only a minor subset of patients has a genetic mutation responsible for disease development (e.g., SNCA , PINK1 and PARK2 mutations in PD (Abeliovich and Gitler, 2016)(Pickrell and Youle, 2015), and APP, PSEN1, PSEN2 in AD (Van Cauwenberghe et al., 2016)).”
From TET2 Regulates the Neuroinflammatory Response in Microglia (2019) · cites this paper as Pickrell and Youle, 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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 9,740
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis
Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914
Autophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,444
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
Self-citationChronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674
Self-citationHereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
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
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
Self-citationFission 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
Cited by
Sorted by citations
Items 901–1,000 of 1,002
GDNF/RET signaling in dopamine neurons in vivo
Conway, J. A., Ince, S., Black, S., & Kramer, E. R. (2020) · Cell and Tissue Research · doi:10.1007/s00441-020-03268-9 · Cited by 33
Mitochondrial Ca2+ oscillation induces mitophagy initiation through the PINK1-Parkin pathway
Yu, Z., Wang, H., Tang, W., Wang, S., Tian, X., Zhu, Y., & He, H. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03913-3 · Cited by 35
Mitophagy in Yeast: Molecular Mechanism and Regulation
Innokentev, A., & Kanki, T. (2021) · Cells · doi:10.3390/cells10123569 · Cited by 39
Kim, M. J., Jeong, H., & Krainc, D. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac047 · Cited by 34
Cross-species models of attention-deficit/hyperactivity disorder and autism spectrum disorder
Vecchia, E. D., Mortimer, N., Palladino, V. S., Kittel‐Schneider, S., Lesch, K., Reif, A., Schenck, A., & Norton, W. (2018) · Psychiatric Genetics · doi:10.1097/ypg.0000000000000211 · Cited by 36
Mitophagy regulation in aging and neurodegenerative disease
Banarase, T. A., Sammeta, S. S., Wankhede, N. L., Mangrulkar, S. V., Rahangdale, S. R., Aglawe, M. M., Taksande, B. G., Upaganlawar, A. B., Umekar, M. J., & Kale, M. B. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01057-6 · Cited by 35
Sánchez-Martínez, Á., Martinez, A., & Whitworth, A. J. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002244 · Cited by 32
A comprehensive review on signaling attributes of serine and serine metabolism in health and disease
Wu, D., Zhang, K., Khan, F. A., Pandupuspitasari, N. S., Guan, K., Sun, F., & Huang, C. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129607 · Cited by 35
Mitochondrial medicine: “from bench to bedside” 3PM-guided concept
Shao, Q., Noah, M. L. N., Golubnitschaja, O., & Zhan, X. (2025) · The EPMA Journal · doi:10.1007/s13167-025-00409-4 · Cited by 36
Zhang, C., Wang, R., Liu, Z., Bunker, E. N., Lee, S., Giuntini, M., Chapnick, D. A., & Liu, X. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006506 · Cited by 34
Haga, H., Matsuo, K., Yabuki, Y., Zhang, C., Han, F., & Fukunaga, K. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.104492 · Cited by 33
Cornelissen, T., Spinazzi, M., Martin, S., Imberechts, D., Vangheluwe, P., Bird, M., Strooper, B. D., & Vandenberghe, W. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa028 · Cited by 33
NIPSNAP protein family emerges as a sensor of mitochondrial health
Fathi, E., Yarbro, J. M., & Homayouni, R. (2021) · BioEssays · doi:10.1002/bies.202100014 · Cited by 35
Kim, H., Perentis, R. J., Caldwell, G. A., & Caldwell, K. A. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0619-5 · Cited by 35
miR-34a-5p regulates PINK1-mediated mitophagy via multiple modes
Tai, Y., Pu, M., Yuan, L., Guo, H., Qiao, J., Lu, H., Wang, G., Chen, J., Qi, X., Tao, Z., et al. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119415 · Cited by 33
Shen, Y., Wang, X., Nan, N., Fu, X., Zeng, R., Yang, Y., Xian, S., Shi, J., Wu, Q., & Zhou, S. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03830-w · Cited by 33
VDAC1: A Key Player in the Mitochondrial Landscape of Neurodegeneration
Argueti-Ostrovsky, S., Barel, S., Kahn, J., & Israelson, A. (2024) · Biomolecules · doi:10.3390/biom15010033 · Cited by 31
Silva, K. A. S., Ghiarone, T., Schreiber, K. L., Grant, D. G., White, T., Frisard, M. I., Sukhanov, S., Chandrasekar, B., Delafontaine, P., & Yoshida, T. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00898.2018 · Cited by 32
Chiricosta, L., Gugliandolo, A., Diomede, F., Pizzicannella, J., Trubiani, O., Iori, R., Tardiolo, G., Guarnieri, S., Bramanti, P., & Mazzon, E. (2019) · Molecules · doi:10.3390/molecules24183217 · Cited by 32
Pharmacological Tools to Modulate Autophagy in Neurodegenerative Diseases
Suresh, S., Chakravorty, A., Giridharan, M., Garimella, L., & Manjithaya, R. R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.023 · Cited by 34
Bcl-xL inhibits PINK1/Parkin-dependent mitophagy by preventing mitochondrial Parkin accumulation
Si, Y., Du, M., Yin, A., Mai, Z., Wang, Y., Zhao, M., Wang, X., & Chen, T. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105720 · Cited by 32
Zhang, Y., Sun, R., Li, X., & Fang, W. (2020) · Viruses · doi:10.3390/v12030289 · Cited by 32
Is there a link between inorganic polyphosphate (polyP), mitochondria, and neurodegeneration?
Borden, E. A., Furey, M., Gattone, N. J., Hambardikar, V. D., Liang, X. H., Scoma, E. R., Samra, A. A., D-Gary, L. R., Dennis, D. J., Fricker, D., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105211 · Cited by 32
Wang, M., Wan, C., He, T., Han, C., Zhu, K., Waddington, J. L., & Zhen, X. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108360 · Cited by 33
Selective autophagy: the rise of the zebrafish model
Pant, D. C., & Nazarko, T. Y. (2020) · Autophagy · doi:10.1080/15548627.2020.1853382 · Cited by 32
Neuroprotective mechanisms of red clover and soy isoflavones in Parkinson's disease models
Jacquet, A. D. R., Ambaw, A., Tambe, M. A., Ma, S. Y., Timmers, M. A., Grace, M. H., Wu, Q., Simon, J. E., McCabe, G. P., Lila, M. A., et al. (2021) · Food & Function · doi:10.1039/d1fo00007a · Cited by 32
Bazylianska, V., SHARMA, A. K., Chauhan, H., Schneider, B. L., & Moszczyńska, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010363 · Cited by 32
Neuroprotective effect of YIAEDAER peptide against Parkinson’s disease like pathology in zebrafish
Ren, Q., Jiang, X. J., Zhang, S., Gao, X., Paudel, Y. N., Zhang, P., Wang, R., Liu, K., & Jin, M. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112629 · Cited by 32
Nam, J.-H., Lee, J., Choi, H., Choi, S.-Y., Noh, K.-E., Jung, N.-C., Song, J. Y., Choi, J., Seo, H. G., Jung, Y., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105650 · Cited by 32
The Potential Role of Voltage‐Dependent Anion Channel in the Treatment of Parkinson’s Disease
He, Y., Wang, W., Yang, T., Thomas, E. R., Dai, R., & Li, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4665530 · Cited by 31
Lamine-Ajili, A., Fahmy, A. M., Létourneau, M., Chatenet, D., Labonté, P., Vaudry, D., & Fournier, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.01.005 · Cited by 32
Postsynaptic movement disorders: clinical phenotypes, genotypes, and disease mechanisms
Abela, L., & Kurian, M. A. (2018) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-018-0205-0 · Cited by 33
Genetics of Parkinson's Disease: From Causes to TreatmentPreprint
Westenberger, A., Brüggemann, N., & Klein, C. (2024) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041774 · Cited by 39
Ubiquitination at the mitochondria in neuronal health and disease
Covill‐Cooke, C., Howden, J. H., Birsa, N., & Kittler, J. T. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.07.003 · Cited by 33
Autophagy and lysosomal pathways in nervous system disorders
Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 32
Jung, S., Chung, Y., Lee, Y., Lee, Y., Cho, J. W., Shin, E., Kim, H., & Oh, Y. J. (2019) · Cell Death Discovery · doi:10.1038/s41420-019-0210-6 · Cited by 31
Sarkar, A. K., Stellrecht, C. M., Vangapandu, H. V., Ayres, M., Kaipparettu, B. A., Park, J. H., Balakrishnan, K., Burks, J. K., Pandita, T. K., Hittelman, W. N., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.234385 · Cited by 30
Zhang, H., Yin, C., Liu, X., Bai, X., Wang, L., Xu, H., Ju, J., & Zhang, L. (2020) · Medical Science Monitor · doi:10.12659/msm.923227 · Cited by 31
Kartawy, M., Халиулин, И. Г., & Amal, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-70383-6 · Cited by 29
VDAC1 promotes cardiomyocyte autophagy in anoxia/reoxygenation injury via the PINK1/Parkin pathway
Yang, X., Zhou, Y., Liang, H., Meng, Y., Liu, H., Zhou, Y., Huang, C., An, B., Mao, H., & Liao, Z. (2021) · Cell Biology International · doi:10.1002/cbin.11583 · Cited by 30
Progressive parkinsonism due to mitochondrial impairment: Lessons from the MitoPark mouse model
Beckstead, M. J., & Howell, R. D. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113707 · Cited by 34
Epigenetic inactivation of the autophagy–lysosomal system in appendix in Parkinson’s disease
Gordevičius, J., Li, P., Marshall, L. L., Killinger, B. A., Lang, S., Ensink, E., Kuhn, N. C., Cui, W., Maroof, N., Lauria, R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25474-x · Cited by 36
Broad activation of the Parkin pathway induces synaptic mitochondrial deficits in early tauopathy
Jeong, Y. Y., Han, S., Jia, N., Zhang, M., Sheshadri, P., Tammineni, P., Cheung, J., Nissenbaum, M., Baskar, S. S., Kwan, K. Y., et al. (2022) · UCL Discovery (University College London) · Cited by 32
Microbes and Parkinson’s disease: from associations to mechanisms
Cannon, T., & Gruenheid, S. (2022) · Trends in Microbiology · doi:10.1016/j.tim.2022.01.004 · Cited by 33
The emergent role of mitochondrial surveillance in cellular health
Tjahjono, E., Kirienko, D. R., & Kirienko, N. V. (2022) · Aging Cell · doi:10.1111/acel.13710 · Cited by 30
Mitochondrial regulatory mechanisms in spinal cord injury: A narrative review
Chengjiang, L., Liu, Y., Ma, B., Zhou, M., Zhao, X., Fu, X., Kan, S.-L., Hu, W., & Zhu, R. (2022) · Medicine · doi:10.1097/md.0000000000031930 · Cited by 31
Yang, Q., Zhou, Y., Yin, H., Li, H., Zhou, M., Sun, G., Cao, Z., Man, R., Wang, H., & Li, J. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00403 · Cited by 31
Human Rights Here and Now: Celebrating the Universal Declaration of Human Rights.
Flowers, N. B. (1998) · Cited by 31
Physiological and Pathophysiological Roles of Mitochondrial Na+-Ca2+ Exchanger, NCLX, in Hearts
Takeuchi, A., & Matsuoka, S. (2021) · Biomolecules · doi:10.3390/biom11121876 · Cited by 32
DYRK1A Inhibitors and Perspectives for the Treatment of Alzheimer's Disease
de Souza, M. M., Cenci, A. R., Teixeira, K. F., Machado, V., Schülerb, M. C. G. M., Gonçalves, A. E., Dalmagro, A. P., Cazarin, C. A., Ferreira, L. L. G., de Oliveira, A. S., et al. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220620162018 · Cited by 30
Zou, J., Tan, W., Liu, K., Chen, B., Duan, T.-Q., & Xu, H. (2022) · The FASEB Journal · doi:10.1096/fj.202200366rr · Cited by 30
Khan, M. M., Paez, H. G., Pitzer, C. R., & Alway, S. E. (2022) · Current Neuropharmacology · doi:10.2174/1570159x05666220908100545 · Cited by 30
Ramezani, M., Wagenknecht-Wiesner, A., Wang, T., Holowka, D. A., Eliezer, D., & Baird, B. A. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00578-x · Cited by 33
Liu, M., Liu, S., Lin, Z.-H., Chen, X., Jiao, Q., Du, X., & Jiang, H. F. (2025) · Biomolecules · doi:10.3390/biom15010149 · Cited by 32
Superoxide dismutating molecules rescue the toxic effects of PINK1 and parkin loss
Biosa, A., Sánchez-Martínez, Á., Filograna, R., Terriente-Félix, A., Alam, S. M., Beltramini, M., Bubacco, L., Bisaglia, M., & Whitworth, A. J. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy069 · Cited by 32
Niu, Y., Nie, Z., Shin, K., Zhou, W., & Cui, X. (2019) · The FASEB Journal · doi:10.1096/fj.201802473r · Cited by 30
Neuronal microtubules and proteins linked to Parkinson’s disease: a relevant interaction?
Calogero, A. M., Mazzetti, S., Pezzoli, G., & Cappelletti, G. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0142 · Cited by 28
Phosphorylation of mitochondrial matrix proteins regulates their selective mitophagic degradation
Kolitsida, P., Zhou, J., Rackiewicz, M., Nolić, V., Dengjel, J., & Abeliovich, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901759116 · Cited by 29
Culprit or Bystander: Defective Mitophagy in Alzheimer’s Disease
Xie, C., Aman, Y., Adriaanse, B. A., Cader, M. Z., Plun‐Favreau, H., Xiao, J., & Fang, E. F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00391 · Cited by 29
Hidden phenotypes of PINK1/Parkin knockout mice
Paul, S., & Pickrell, A. M. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129871 · Cited by 31
Self-citationMitochondrial nanomedicine: Subcellular organelle-specific delivery of molecular medicines
Milane, L. S., Dolare, S., Jahan, T., & Amiji, M. M. (2021) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2021.102422 · Cited by 31
Meng, Q., Zaharieva, E. K., Sasatani, M., & Kobayashi, J. (2021) · Redox Report · doi:10.1080/13510002.2021.1971363 · Cited by 33
Biogenesis of mitochondrial outer membrane proteins, problems and diseases
Ellenrieder, L., Mårtensson, C. U., & Becker, T. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0170 · Cited by 30
Liu, H., Chen, S., Guo, C., Tang, W., Liu, W., & Liu, Y. (2018) · Medical Science Monitor · doi:10.12659/msm.908021 · Cited by 30
RetractedRen, X., Hinchie, A., Swomley, A., Powell, D. K., & Butterfield, D. A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.08.008 · Cited by 29
Dysfunction of synaptic endocytic trafficking in Parkinson’s disease
Ng, X. Y., & Cao, M. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01624 · Cited by 31
Ermini, F., Low, V. F., Song, J. J., Tan, A. Y. S., Faull, R. L. M., Dragunow, M., Curtis, M. A., & Dominy, S. S. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00705-2 · Cited by 29
Liang, J.-H., Yu, H., Xia, C., Zheng, Y., Zhang, Z., Chen, Y., Raza, M. A., Wu, L. H., & Yan, H. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117006 · Cited by 30
Mitochondrial-based therapies for neurodegenerative diseases: a review of the current literature
Wadan, A. S., Shaaban, A., El-Sadek, M. Z., Mostafa, S. A., Moshref, A. S., El‐Hussein, A., Ellakwa, D. E., & Mehanny, S. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04014-0 · Cited by 38
Cremer, J. N., Amunts, K., Schleicher, A., Palomero‐Gallagher, N., Piel, M., Rösch, F., & Zilles, K. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.10.054 · Cited by 30
Mitochondrial roles of the psychiatric disease risk factor DISC1.
Norkett, R., Modi, S., & Kittler, J. (2017) · Schizophrenia Research · doi:10.1016/j.schres.2016.12.025 · Cited by 25
UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN
Park, S. J., Foote, P. K., Krist, D. T., Rice, S. E., & Statsyuk, A. V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.773200 · Cited by 30
Bouhouche, A., Tesson, C., Regragui, W., Rahmani, M., Drouet, V., Tibar, H., Souirti, Z., Haj, R. B. E., Bouslam, N., Yahyaoui, M., et al. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00567 · Cited by 29
Stoll, S., Xi, J., Ma, B., Leimena, C., Behringer, E. J., Qin, G., & Qiu, H. (2019) · Toxicological Sciences · doi:10.1093/toxsci/kfz164 · Cited by 29
Biomedical Implications of Autophagy in Macromolecule Storage Disorders
Palhegyi, A. M., Seranova, E., Dimova, S., Hoque, S., & Sarkar, S. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00179 · Cited by 30
Using induced pluripotent stem cells for modeling Parkinson’s disease
Ke, M., Chong, C., & Su, H. (2019) · World Journal of Stem Cells · doi:10.4252/wjsc.v11.i9.634 · Cited by 31
Glucocerebrosidase as a therapeutic target for Parkinson’s disease
Chen, Y., Sam, R., Sharma, P., Chen, L., Do, J., & Sidransky, E. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1733970 · Cited by 30
Altered mitochondrial proteome and functional dynamics in patients with rheumatoid arthritis
Khanna, S., Padhan, P., Jaiswal, K. S., Jain, A., Ghosh, A., Tripathy, A., Gowda, H., Raghav, S. K., & Gupta, B. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.06.005 · Cited by 30
Defective mitochondrial ISCs biogenesis switches on IRP1 to fine tune selective mitophagy
Wu, H., Wei, H., Zhang, D., Sehgal, S. A., Zhang, D., Wang, X., Qin, Y., Liu, L., & Chen, Q. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101661 · Cited by 30
Cannon, T., Sinha, A., Trudeau, L., Maurice, C. F., & Gruenheid, S. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1830694 · Cited by 30
Mitophagy: A New Player in Stem Cell Biology
Cairns, G., Thumiah-Mootoo, M., Burelle, Y., & Khacho, M. (2020) · Biology · doi:10.3390/biology9120481 · Cited by 29
Intersection between Redox Homeostasis and Autophagy: Valuable Insights into Neurodegeneration
Park, H., Kim, J., Shin, C., & Lee, S. (2021) · Antioxidants · doi:10.3390/antiox10050694 · Cited by 32
Ubiquitinomics: History, methods, and applications in basic research and drug discovery
Steger, M., Karayel, Ö., & Demichev, V. (2022) · PROTEOMICS · doi:10.1002/pmic.202200074 · Cited by 30
Activated or Impaired: An Overview of DNA Repair in Neurodegenerative Diseases
Qin, N., Geng, A., & Xue, R. (2022) · Aging and Disease · doi:10.14336/ad.2021.1212 · Cited by 31
Kuzmenko, A., Derbikova, K., Salvatori, R., Tankov, S., Atkinson, G. C., Tenson, T., Ott, M., Kamenski, P. A., & Hauryliuk, V. (2016) · Scientific Reports · doi:10.1038/srep18749 · Cited by 29
Ephedrine-induced mitophagy via oxidative stress in human hepatic stellate cells
Lee, A. Y., Jang, Y., Hong, S., Chang, S.-H., Park, S. J., Kim, S., Kang, K., Kim, J., & Cho, M. (2017) · The Journal of Toxicological Sciences · doi:10.2131/jts.42.461 · Cited by 28
Mitochondrial chaotic dynamics: Redox-energetic behavior at the edge of stability
Kembro, J. M., Cortassa, S. C., Lloyd, D., Sollott, S. J., & Aon, M. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-33582-w · Cited by 29
Yao, Z., Li, X., Wang, W., Ren, P., Song, S., Wang, H., Xie, Y., Li, X., & Li, Z. (2023) · Food & Nutrition Research · doi:10.29219/fnr.v67.9547 · Cited by 28
FKBP5 activates mitophagy by ablating PPAR-γ to shape a benign remyelination environment
Sun, X., Qian, M., Li, H., Wang, L., Zhao, Y., Yin, M., Dai, L., & Bao, H. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06260-7 · Cited by 30
Jiao, F., Meng, L., Du, K., & Li, X. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01195 · Cited by 30
Elevated α-synuclein levels inhibit mitophagic flux
Kinnart, I., Manders, L., Heyninck, T., Imberechts, D., Praschberger, R., Schoovaerts, N., Verfaillie, C. M., Verstreken, P., & Vandenberghe, W. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00696-0 · Cited by 33
Quiescent cell re-entry is limited by macroautophagy-induced lysosomal damage
Murley, A., Popovici, A. C., Hu, X., Lund, A., Wickham, K., Durieux, J., Joe, L. K., Koronyo, E., Zhang, H., Genuth, N. R., et al. (2025) · Cell · doi:10.1016/j.cell.2025.03.009 · Cited by 31
Mani, S., Wasnik, S., Shandilya, C., Srivastava, V., Khan, S., & Singh, K. K. (2025) · Frontiers in Aging · doi:10.3389/fragi.2025.1615764 · Cited by 33
Knockdown of the mitochondria‐localized protein p13 protects against experimental parkinsonism
Inoue, N., Ogura, S., Kasai, A., Nakazawa, T., Ikeda, K., Higashi, S., Isotani, A., Baba, K., Mochizuki, H., Fujimura, H., et al. (2018) · EMBO Reports · doi:10.15252/embr.201744860 · Cited by 29
Ding, Y., Xin, C., Zhang, C., Lim, K., Zhang, H., Fu, Z., Li, L., & Huang, W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00246 · Cited by 28
Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy
Quinet, G., Gonzalez-Santamarta, M., Louche, C., & Rodríguez, M. S. (2020) · Molecules · doi:10.3390/molecules25102352 · Cited by 27
Houzelle, A., Dahlmans, D., Nascimento, E. B. M., Schaart, G., Jörgensen, J. A., Moonen‐Kornips, E., Kersten, S., Wang, X., & Hoeks, J. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29797 · Cited by 28
Hayashida, A., Li, Y., Yoshino, H., Daida, K., Ikeda, A., Ogaki, K., Fuse, A., Mori, A., Takanashi, M., Nakahara, T., et al. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.06.017 · Cited by 28
Research on developing drugs for Parkinson's disease
Zhang, C., Han, Q.-W., Chen, N., & Yuan, Y. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.12.017 · Cited by 28
DNA Methyltransferase 1 Is Dysregulated in Parkinson’s Disease via Mediation of miR-17
Zhang, H.-Q., Wang, J., Li, Z.-F., Cui, L., Huang, S., Zhu, L.-B., Sun, Y., Yang, R., Fan, H.-H., Zhang, X., et al. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02298-w · Cited by 30
Metadata
- Authors
- Pickrell, A. M., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Youle, Richard J.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2015-01
- Volume
- 85
- Issue
- 2
- Pages
- 257-273
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4764997
- OpenAlex
- W2082425146
- Cited by
- 2,310
- References
- 212
- Citations by year
- 2026: 268 · 2025: 234 · 2024: 177 · 2023: 175 · 2022: 228 · 2021: 261 · 2020: 239 · 2019: 197 · 2018: 178 · 2017: 174 · 2016: 123 · 2015: 54
- FWCI
- 23.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences
- National Institute of Neurological Disorders and Stroke (Z01NS002859)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- PINK1, Parkin, Parkinson's disease, mitochondrial quality control, mitochondrial damage, E3 ubiquitin ligase, selective autophagy, mitophagy, autosomal recessive parkinsonism, mitochondrial outer membrane
- MeSH terms
- PTEN-Induced Putative Kinase, Humans, Mitochondria, Parkinson Disease, Protein Kinases, Parkinsonian Disorders, Ubiquitin-Protein Ligases, Proteolysis, Mitophagy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review