The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
PINK1/Parkin-mediated mitophagy in mammalian cells
Abstract
Mitochondria-specific autophagy (mitophagy) is a fundamental process critical for maintaining mitochondrial fitness in a myriad of cell types. Particularly, mitophagy contributes to mitochondrial quality control by selectively eliminating dysfunctional mitochondria. In mammalian cells, the Ser/Thr kinase PINK1 and the E3 ubiquitin ligase Parkin act cooperatively in sensing mitochondrial functional state and marking damaged mitochondria for disposal via the autophagy pathway. Notably, ubiquitin and deubiquitinases play vital roles in modulating Parkin activity and mitophagy efficiency. In this review, we highlight recent breakthroughs addressing the key issues of how PINK1 activates Parkin in response to mitochondrial malfunction, how Parkin localizes specifically to impaired mitochondria, and how ubiquitination and deubiquitination regulate PINK1/Parkin-mediated mitophagy.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“There are apparently several pathways to mitophagy [169,170], but the most important and the better understood one is the canonical PINK1/PARKIN pathway [171,172,173,174,175,176].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [173]
Citations
Cites
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
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
Hereditary 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
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
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
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
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
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
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
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
Flagged first, then by citations
Research works printed but not linked: 1
- Fiesel, 2014, A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently, J Cell Sci, 127, 3488
Cited by
Sorted by citations
Items 201–300 of 606
The multifaceted roles of natural products in mitochondrial dysfunction
Chen, Q., Ruan, D., Shi, J., Du, D., & Bian, C. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1093038 · Cited by 39
Wang, C., Cao, S., Zhang, Q., Shen, Z., Feng, J., Hong, Q., Lu, J., Xie, F., Peng, Y., & Hu, C. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b06208 · Cited by 37
Xie, J., Cui, Y., Chen, X., Yu, H., Chen, J., Huang, T., He, M., Zhang, L., & Meng, Q. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108640 · Cited by 36
Dong, G., Xu, N., Wang, M., Zhao, Y., Jiang, F., Bu, H., Liu, J., Yuan, B., & Li, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111422 · Cited by 36
The Role of Mitophagy in Viral Infection
Li, Y., Wu, K., Zeng, S., Zou, L., Li, X., Xu, C., Li, B., Liu, X., Li, Z., Zhu, W., et al. (2022) · Cells · doi:10.3390/cells11040711 · Cited by 35
Zhang, X., Yuan, D., Sun, Q., Xu, L., Lee, E. J., Lewis, A., Zuckerbraun, B. S., & Rosengart, M. R. (2017) · The FASEB Journal · doi:10.1096/fj.201601096rrr · Cited by 35
Testosterone ameliorates age-related brain mitochondrial dysfunction
Yan, W., Zhang, T., Kang, Y., Zhang, G., Ji, X., Feng, X., & Shi, G. (2021) · Aging · doi:10.18632/aging.203153 · Cited by 35
Positive regulation of human PINK1 and Parkin gene expression by nuclear respiratory factor 1
Lu, Y., Ding, W., Wang, B., Wang, L., Kan, H., Wang, X., Wang, D., & Zhu, L. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.12.002 · Cited by 34
Duan, T., Hu, T., Wu, C., Yeh, Y., Lu, J., Zhang, Q., Li, X., Jian, W., & Luo, P. (2020) · Toxicology in Vitro · doi:10.1016/j.tiv.2020.104857 · Cited by 35
Dual Role of Mitophagy in Cardiovascular Diseases
Li, Y., Meng, W., Hou, Y., Li, D., Wang, X., Wu, K., Sun, S., Liu, H., Li, X., Lin, F., et al. (2021) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001046 · Cited by 33
Hypoxia Inducible Factor-1α Is a Regulator of Autophagy in Osteoarthritic Chondrocytes
Lu, J., Peng, Y., Zou, J., Wang, J., Lu, S., Fu, T., Jiang, L., Zhang, C., & Zhang, J. (2021) · Cartilage · doi:10.1177/19476035211035434 · Cited by 35
Liu, B., Wang, D., Cao, Y., Wu, J., Zhou, Y., Wu, W., Wu, J., Zhou, J., & Qiu, J. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175136 · Cited by 34
Großmann, D., Malburg, N., Glaß, H., Weeren, V., Sondermann, V., Pfeiffer, J. F., Petters, J., Lukáš, J., Seibler, P., Klein, C., et al. (2023) · Movement Disorders · doi:10.1002/mds.29525 · Cited by 34
Hepatic autophagy and mitophagy status in dairy cows with subclinical and clinical ketosis
Shen, T., Xu, F., Fang, Z., Loor, J. J., Ouyang, H., Chen, M., Jin, B., Wang, X., Shi, Z., Zhu, Y., et al. (2021) · Journal of Dairy Science · doi:10.3168/jds.2020-19150 · Cited by 34
Zhu, Q., Zhuo, H., Yang, L., Ouyang, H., Chen, J., Liu, B., & Huang, H. (2022) · Molecules · doi:10.3390/molecules27185839 · Cited by 34
Ali, M. Z., & Dholaniya, P. S. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105344 · Cited by 33
Shaping Up Mitochondria in Diabetic Nephropathy
Mise, K., Galvan, D. L., & Danesh, F. R. (2020) · Kidney360 · doi:10.34067/kid.0002352020 · Cited by 33
Baicalin mitigated IL‐1β‐Induced osteoarthritis chondrocytes damage through activating mitophagy
He, J., & He, J. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14215 · Cited by 33
Xin, R., Xu, Y., Long, D., Mao, G., Liao, H., Zhang, Z., & Kang, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.911716 · Cited by 32
Zhang, C., Fei, Y., Li, M., Li, J., Tang, M., Wang, G., Li, J., Wang, Y., Ding, Y., Peng, C., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142080 · Cited by 34
Yu, M., Yang, J., Gao, X., Sun, W., Liu, S., Han, Y., Lu, X., Jin, C., Wu, S., & Cai, Y. (2020) · Metallomics · doi:10.1039/c9mt00291j · Cited by 32
Roles of microglial mitophagy in neurological disorders
Liu, Y., Wang, M., Hou, X., & Hu, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.979869 · Cited by 31
Xiao, Y.-Y., Xiao, J.-X., Wang, X., Wang, T., Qu, X.-H., Jiang, L., Tou, F., Chen, Z., & Han, X. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.956190 · Cited by 32
Chemical mitophagy modulators: Drug development strategies and novel regulatory mechanisms
Dong, Y. J., Zhuang, X., Wang, Y.-T., Tan, J., Feng, D., Li, M., Zhong, Q., Song, Z., Shen, H., Fang, E. F., et al. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106835 · Cited by 36
Cao, J., Ma, X., Yan, X., Zhang, G., Hong, S. K., Ma, R., Wang, Y., & Ma, M. (2023) · Phytotherapy Research · doi:10.1002/ptr.7838 · Cited by 33
Russo, T., Kolisnyk, B., Aswathy, B. S., Kim, T. W., Martin, J., Plessis‐Belair, J., Ni, J., Pearson, J. A., Park, E. J., Sher, R. B., et al. (2024) · Aging Cell · doi:10.1111/acel.14077 · Cited by 30
Metformin: From diabetes to cancer to prolongation of life
Sirtori, C. R., Castiglione, S., & Pavanello, C. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107367 · Cited by 38
Markowska, J., Kasprzak‐Drozd, K., Niziński, P., Dragan, M., Kondracka, A., Gondek, E., Oniszczuk, T., & Oniszczuk, A. (2024) · Molecules · doi:10.3390/molecules29225245 · Cited by 32
Schumann, A., Schaller, K., Belche, V., Cybulla, M., Grünert, S. C., Moers, N., Sass, J. O., Kaech, A., Hannibal, L., & Spiekerkoetter, U. (2021) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12373 · Cited by 31
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
Lin, C., Chen, J., Hu, M., Zheng, W., Song, Z., & Qin, H. (2021) · Food & Nutrition Research · doi:10.29219/fnr.v65.7577 · Cited by 32
Glucose- and Non-Glucose-Induced Mitochondrial Dysfunction in Diabetic Kidney Disease
Ito, M., Gurumani, M. Z., Merscher, S., & Fornoni, A. (2022) · Biomolecules · doi:10.3390/biom12030351 · Cited by 34
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
Tan, T., Zimmermann, M., & Reichert, A. S. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0125 · Cited by 33
Zhang, C., Yu, X., Gao, J., Zhang, Q., Sun, S., Zhu, H., Yang, X., & Yan, H. (2018) · Toxicology in Vitro · doi:10.1016/j.tiv.2018.03.002 · Cited by 31
Endothelial FUNDC1 Deficiency Drives Pulmonary Hypertension
Pei, Y., Ren, D., Yin, Y., Shi, J., Ai, Q., Hao, W., Luo, X., Zhang, C., Zhao, Y., Bai, C., et al. (2024) · Circulation Research · doi:10.1161/circresaha.124.325156 · Cited by 31
Research Progress on the Mechanism of Mitochondrial Autophagy in Cerebral Stroke
Li, L., Yang, S., Lu, X., Zhang, Y., & Li, T. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.698601 · Cited by 31
Zhou, L., Su, W., Wang, Y., Zhang, Y., Xia, Z., & Lei, S. (2023) · Diabetes Obesity and Metabolism · doi:10.1111/dom.15369 · 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
Dysregulation of Parkin-mediated mitophagy in thyroid Hürthle cell tumors
Lee, J., Ham, S., Lee, M. H., Kim, S. J., Park, J. H., Lee, S. E., Chang, J. Y., Joung, K. H., Kim, T. Y., Kim, J., et al. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv122 · Cited by 33
Exposure of zebrafish to a cold environment triggered cellular autophagy in zebrafish liver
Chen, H., Zhao, F., Chen, K., Guo, Y., Liang, Y., Zhao, H., & Chen, S. (2022) · Journal of Fish Diseases · doi:10.1111/jfd.13620 · Cited by 29
ncRNAs and their impact on dopaminergic neurons: Autophagy pathways in Parkinson's disease
Thapa, R., Moglad, E. H. O., Afzal, M., Gupta, G., Bhat, A. A., Almalki, W. H., Kazmi, I. A., Alzarea, S. I., Pant, K., Ali, H., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102327 · 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
Double-edged alliance: mitochondrial surveillance by the UPS and autophagy
Franz, A., Kevei, É., & Hoppe, T. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.08.004 · Cited by 29
Su, Y., Lin, H. L., Tu, Y., Wang, M., Zhang, G., Yang, J., Liu, H., & Su, Z. (2022) · Chemical Science · doi:10.1039/d1sc06722b · Cited by 28
Russo, C., Valle, M. S., Casabona, A., Spicuzza, L., Sambataro, G., & Malaguarnera, L. (2022) · Biomedicines · doi:10.3390/biomedicines10040898 · Cited by 32
Wang, G., Liu, Y., Zhu, X., Lin, K., Li, M., Wu, Z., Zhang, R., Zheng, Q., Li, D., & An, T. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109154 · Cited by 31
Serum starvation induces anti-apoptotic cIAP1 to promote mitophagy through ubiquitination
Mukhopadhyay, S., Naik, P. P., Panda, P. K., Sinha, N., Das, D. N., & Bhutia, S. K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.143 · Cited by 28
Gao, L., Xiao, K., Wu, Y.-Z., Chen, D., Yang, X., Shi, Q., & Dong, X. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00039 · Cited by 27
The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease
Blondelle, J., Biju, A., & Lange, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217936 · Cited by 27
GPD1L inhibits renal cell carcinoma progression by regulating PINK1/Parkin‐mediated mitophagy
Liu, T., Zhu, H., Ge, M., Pan, Z., Zeng, Y., Leng, Y., Yang, K., & Fan, C. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17813 · Cited by 25
Yang, H., Niu, S., Guo, M., & Xue, Y. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124934 · Cited by 26
Liu, M., & Wu, Y. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.819454 · Cited by 27
Yu, X., Sun, Y., Cai, Q., Zhao, X., Liu, Z., Xue, X., & Fu, J. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4766 · Cited by 25
Xanthohumol-Induced Rat Glioma C6 Cells Death by Triggering Mitochondrial Stress
Hou, S., Song, Y., Sun, D., Zhu, S., & Wang, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094506 · Cited by 25
The Intertwining of Autophagy and the Ubiquitin Proteasome System in Podocyte (Patho)Physiology
Blume, L., & Meyer‐Schwesinger, C. (2021) · Cellular Physiology and Biochemistry · doi:10.33594/000000432 · Cited by 26
Li, L., Huang, T., Yang, J., Yang, P., Lan, H., Liang, J., Cai, D., Zhong, H., Jiao, W., & Song, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114533 · Cited by 24
Endometrial Aging and Reproductive Decline: The Central Role of Mitochondrial Dysfunction
Kobayashi, H., Nishio, M., Umetani, M., Shigetomi, H., Imanaka, S., & Hashimoto, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115060 · Cited by 28
Wang, W., Guo, H., Yan, X., Pan, X., Wang, X., Rong, Y., Bai, Z., Zhang, L., Wu, Z., Zhao, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63496-x · Cited by 29
Wu, G., Xiong, Q., Wei, X., Wang, Y., Hu, X., He, G., Liu, L., Lai, Q., Dai, Z., Anushesh, D., et al. (2019) · PeerJ · doi:10.7717/peerj.7209 · Cited by 23
Inflammatory injury and mitophagy induced by Cr(VI) in chicken liver
Wang, Y., Hao, J., Zhang, S., Li, L., Wang, R., Zhu, Y., Liu, Y., & Liu, J. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-08544-3 · Cited by 24
Mitophagy: A Novel Therapeutic Target for Treating DN
Yang, M., Li, C., Yang, S., Xiao, Y., Chen, W., Gao, P., Jiang, N., Xiong, S., Wei, L., Zhang, Q., et al. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327666201006152656 · Cited by 26
Wang, X., Wang, M., Cai, M., Shao, R., Xia, G., & Zhao, W. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.07.009 · Cited by 24
E3 ubiquitin ligases and their therapeutic potential in disease Management
Madhukar, G., Haque, M. A., Khan, S., Kim, J.-J., & Danishuddin (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116875 · Cited by 26
CaMKIV regulates mitochondrial dynamics during sepsis
Zhang, X., Griepentrog, J. E., Zou, B., Xu, L., Cyr, A. R., Chambers, L., Zuckerbraun, B. S., Shiva, S., & Rosengart, M. R. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102286 · Cited by 23
Glioma cells are resistant to inflammation‑induced alterations of mitochondrial dynamics
Fan, W., Song, Y., Ren, Z., Cheng, X., Li, P., Song, H., & Jia, L. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5134 · Cited by 23
Zeng, M., Zhang, X., Xing, W., Wang, Q., Liang, G.-B., & He, Z. (2022) · Toxicology Letters · doi:10.1016/j.toxlet.2022.01.017 · Cited by 23
PINK1/Parkin-mediated mitophagy mitigates T-2 toxin-induced nephrotoxicity
Zhang, X., Du, J., Li, B., Huo, S., Zhang, J., Cui, Y., Song, M., Shao, B., & Li, Y. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113078 · Cited by 23
Mitochondrial-Dependent and Independent Functions of PINK1
Chen, X., Wang, Q., Li, S., Li, X., & Yang, W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.954536 · Cited by 24
Oxidative Biomarkers Associated with the Pulmonary Manifestation of Post-COVID-19 Complications
Siekacz, K., Kumor‐Kisielewska, A., Miłkowska-Dymanowska, J., Pietrusińska, M., Bartczak, K. T., Majewski, S., Stańczyk, A., Piotrowski, W. J., & Białas, A. J. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12134253 · Cited by 25
Ferroptosis in Liver Disease: Natural Active Compounds and Therapeutic Implications
Wu, Z., Zhu, Y., Liu, W., Balasubramanian, B., Xu, X. L., Yao, J., & Lei, X. J. (2024) · Antioxidants · doi:10.3390/antiox13030352 · Cited by 26
Kojima, W., Kujuro, Y., Okatsu, K., Queliconi, B. B., Koyano, F., Kimura, M., Yamano, K., Tanaka, K., & Matsuda, N. (2016) · Genes to Cells · doi:10.1111/gtc.12382 · Cited by 22
Torres, A. K., Jara, C., Llanquinao, J., Lira, M., Cortés-Díaz, D., & Tapia‐Rojas, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065476 · Cited by 25
Lin, M., Xian, H., Chen, Z., Wang, S., Liu, M., Liang, W., Tang, Q., Liu, Y., Huang, W., Che, D., et al. (2023) · Nature Cardiovascular Research · doi:10.1038/s44161-023-00314-x · Cited by 23
Parkin regulates IGF2BP3 through ubiquitination in the tumourigenesis of cervical cancer
Sun, X., Ye, G., Li, J., Shou, H., Bai, G., & Zhang, J. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1457 · Cited by 22
Jo, D. S., Bae, D., Park, S. J., Seo, H. M., Kim, H. B., Oh, J. S., Chang, J. W., Kim, S., Shin, J.-W., & Cho, D. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.09.153 · Cited by 22
Wang, Z., Zhang, H., Liu, Z., Ma, Z., An, D., & Xu, D. (2020) · Journal of Biosciences · doi:10.1007/s12038-020-00047-0 · Cited by 22
Modulation of Autophagy: A Novel “Rejuvenation” Strategy for the Aging Liver
Xu, F., Tautenhahn, H., Dirsch, O., & Dahmen, U. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6611126 · Cited by 21
RIPOR2-mediated autophagy dysfunction is critical for aminoglycoside-induced hearing loss
Li, J., Liu, C., Müller, U., & Zhao, B. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.08.011 · Cited by 23
Xu, Q., Liu, S., Gong, Q., Zhu, R., Liu, J., Wu, Q., & Zhou, X. (2022) · Cells · doi:10.3390/cells12010137 · Cited by 21
Dutta, P., Haller, E. M., Sharp, A., & Nanjundan, M. (2016) · BMC Cancer · doi:10.1186/s12885-016-2053-3 · Cited by 22
Clementino, M., Kim, D., & Zhang, Z. (2019) · Toxicological Sciences · doi:10.1093/toxsci/kfz032 · Cited by 21
Zhang, Y., Liu, Q., Li, Y., Li, C., Zhu, Y., Xia, F., Xu, S., & Li, W. (2019) · Medical Science Monitor · doi:10.12659/msm.918536 · Cited by 21
Wang, Y., Hu, Y., Wang, H., Liu, N., Luo, L., Zhao, C., Zhou, D., Tong, H., Li, P., & Zhou, Q. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6192498 · Cited by 21
Dong, Y., Hu, M., Tan, K., & Dai, R. (2023) · Epigenetics · doi:10.1080/15592294.2023.2239592 · Cited by 20
D’Amico, A. G., Maugeri, G., Magrì, B., Bucolo, C., & D’Agata, V. (2024) · Experimental Eye Research · doi:10.1016/j.exer.2024.110024 · Cited by 22
Sui, C., Liu, Y., Jiang, J., Tang, J., Yu, L., & Lv, G. (2024) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2024.111043 · Cited by 21
Yadav, A. K., & Srikrishna, S. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.01.006 · Cited by 19
Cyclosporine attenuates Paraquat-induced mitophagy and pulmonary fibrosis
Liu, K., Zhan, Z., Gao, W., Feng, J., & Xie, X. (2020) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2020.1729176 · Cited by 20
Zhang, H., Liu, X., Fan, Y., Yu, Y., Loor, J. J., Loor, J. J., Peng, A., & Wang, H. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa428 · Cited by 20
Mitophagy: An Emergence of New Player in Alzheimer’s Disease
Sharma, B., Pal, D., Sharma, U., & Kumar, A. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.921908 · Cited by 21
Chai, G., Wu, J., Gong, J., Zhou, J.-L., Jiang, Z.-Q., Yi, H., Gu, Y., Huang, H.-H., Yao, Z.-Y., Zhang, Y., et al. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.09.020 · Cited by 23
Formononetin Inhibits Hepatic I/R‐Induced Injury through Regulating PHB2/PINK1/Parkin Pathway
Ma, Z., Zhang, D., Sun, J., Zhang, Q., Qiao, Y., Zhu, Y., Niu, J., Ren, Q., Zhou, L., Wen, A., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6481192 · Cited by 21
Mu, N., Zhang, T., Zhu, Y., Lu, B., Zheng, Q., & Duan, J. (2023) · BMC Cardiovascular Disorders · doi:10.1186/s12872-023-03226-7 · Cited by 20
Chen, Y., Cao, W., Li, B., Qiao, X., Wang, X., Yang, G., & Li, S. (2023) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2023.2281901 · Cited by 20
Thioredoxin-1 decreases alpha-synuclein induced by MPTP through promoting autophagy-lysosome pathway
Gu, R., Bai, L., Yan, F., Zhang, S., Zhang, X., Deng, R., Zeng, X., Sun, B., Hu, X., Li, Y., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01848-0 · Cited by 23
Targeting NKAα1 to treat Parkinson's disease through inhibition of mitophagy-dependent ferroptosis
Zhang, X., Li, G., Chen, H., Nie, X.-W., & Bian, J. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.04.002 · Cited by 22
Characterization of RING-Between-RING E3 Ubiquitin Transfer Mechanisms
Reiter, K. H., & Klevit, R. E. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8706-1_1 · Cited by 21
Lysosomes Dysfunction Causes Mitophagy Impairment in PBMCs of Sporadic ALS Patients
Bordoni, M., Pansarasa, O., Scarian, E., Cristofani, R., Leone, R., Fantini, V., Garofalo, M., Diamanti, L., Bernuzzi, S., Gagliardi, S., et al. (2022) · Cells · doi:10.3390/cells11081272 · Cited by 19
Mitochondrial proteotoxicity: implications and ubiquitin-dependent quality control mechanisms
Karbowski, M., Oshima, Y., & Verhoeven, N. A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04604-8 · Cited by 21
Metadata
- Authors
- Eiyama, A., & Okamoto, K.
- Affiliations
- The University of Osaka (JP)
- Corresponding author
- Okamoto, Koji
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2015-04
- Volume
- 33
- Pages
- 95-101
- ISSN
- 0955-0674 (ISSN-L)
- OpenAlex
- W2013642338
- Cited by
- 603
- References
- 61
- Citations by year
- 2026: 45 · 2025: 66 · 2024: 71 · 2023: 74 · 2022: 83 · 2021: 68 · 2020: 57 · 2019: 36 · 2018: 38 · 2017: 22 · 2016: 29 · 2015: 14
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (25291045, 25650067)
- Ministry of Education, Culture, Sports, Science and Technology (26111513)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- mitophagy, PINK1, Parkin, mitochondrial quality control, mitochondrial dysfunction, ubiquitination, deubiquitination, E3 ubiquitin ligase, Ser/Thr kinase, mammalian cells
- MeSH terms
- PTEN-Induced Putative Kinase, Animals, Enzyme Activation, Humans, Mammals, Mitochondria, Phosphorylation, Protein Kinases, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination, Mitophagy, Ubiquitin-Specific Proteases
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