The DOI matches its Crossref record; 160 of the 166 references it cites were found in a registry or an index.
Mitophagy: mechanisms, pathophysiological roles, and analysis
Open accessAbstract
Mitochondria are essential organelles that regulate cellular energy homeostasis and cell death. The removal of damaged mitochondria through autophagy, a process called mitophagy, is thus critical for maintaining proper cellular functions. Indeed, mitophagy has been recently proposed to play critical roles in terminal differentiation of red blood cells, paternal mitochondrial degradation, neurodegenerative diseases, and ischemia or drug-induced tissue injury. Removal of damaged mitochondria through autophagy requires two steps: induction of general autophagy and priming of damaged mitochondria for selective autophagic recognition. Recent progress in mitophagy studies reveals that mitochondrial priming is mediated either by the Pink1-Parkin signaling pathway or the mitophagic receptors Nix and Bnip3. In this review, we summarize our current knowledge on the mechanisms of mitophagy. We also discuss the pathophysiological roles of mitophagy and current assays used to monitor mitophagy.
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?
In the citing paper
“The PINK1/Parkin) pathway is among the best characterized pathways through which mitophagy is induced in mammalian cells[28]”
From Overexpression of pink1 or parkin in indirect flight muscles promotes mitochondrial proteostasis and extends lifespan in Drosophila melanogaster (2019) · cites this paper as [28]
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
1 retracted
Mitochondrial Autophagy Is an HIF-1-dependent Adaptive Metabolic Response to Hypoxia
Zhang, H., Bosch-Marce, M., Shimoda, L. A., Tan, Y. S., Baek, J. H., Wesley, J. B., Gonzalez, F. J., & Semenza, G. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800102200 · Cited by 1,601
RetractedAutophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057
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
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
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
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Cited by
Sorted by citations
Items 601–700 of 1,001
Rapani, A., Nikiforaki, D., Karagkouni, D., Sfakianoudis, K., Tsioulou, P., Grigoriadis, S., Maziotis, E., Pantou, A., Voutsina, A., Pantou, A., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.590106 · Cited by 15
The Mitochondrial Deubiquitinase USP30 Regulates AKT/mTOR Signaling
Zhang, R., Ozgen, S., Luo, H., Krigman, J., Zhao, Y., Xin, G., & Sun, N. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.816551 · Cited by 15
The adhesion G protein‐coupled receptor VLGR1/ADGRV1 controls autophagy
Linnert, J., Güler, B. E., Krzysko, J., & Wolfrum, U. (2023) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13869 · Cited by 15
The Application of Nucleic Acid Nanomaterials in the Treatment of Mitochondrial Dysfunction
Yao, L., Hai, Q., & Zhang, T. (2023) · Current Drug Metabolism · doi:10.2174/1389200224666230614115655 · Cited by 15
Mitophagy: A Bridge Linking HMGB1 and Parkinson’s Disease Using Adult Zebrafish as a Model Organism
Razali, K., Nasir, M. H. M., Kumar, J., & Mohamed, W. M. Y. (2023) · Brain Sciences · doi:10.3390/brainsci13071076 · Cited by 15
Garimella, S. V., Gampa, S. C., & Chaturvedi, P. (2023) · Stem Cells and Cloning Advances and Applications · doi:10.2147/sccaa.s417842 · Cited by 16
Muvhulawa, N., Mazibuko-Mbeje, S. E., Ndwandwe, D. E., Silvestri, S., Ziqubu, K., Moetlediwa, M. T., Mthembu, S. X. H., Marnewick, J. L., van der Westhuizen, F. H., Nkambule, B. B., et al. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.122125 · Cited by 16
The role of mitophagy in the development of chronic kidney disease
Yang, K., Li, T., Geng, Y., Zou, X., Peng, F., & Gao, W. (2024) · PeerJ · doi:10.7717/peerj.17260 · Cited by 16
Feng, W., Li, J., Xu, Y., Jiang, G., Su, S., Zhang, Z., Jia, R., & YongKai, T. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.742372 · Cited by 15
Selvakumar, G. P., Iyer, S. S., Kempuraj, D., Ahmed, M. E., Thangavel, R., Dubova, I., Raikwar, S. P., Zaheer, S. A., & Zaheer, A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1340-1 · Cited by 15
Lo, S., Blaszak, R. T., & Parajuli, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103506 · Cited by 15
Mitophagy of polarized sperm-derived mitochondria after fertilization
Rubio-Peña, K., Rawi, S. A., Husson, F., Lam, F., Merlet, J., & Galy, V. (2020) · iScience · doi:10.1016/j.isci.2020.102029 · Cited by 15
Kim, J. Y., Park, S., Park, H. J., Kim, S. H., Lew, H., & Kim, G. J. (2021) · Cells · doi:10.3390/cells10051117 · Cited by 15
Kostyuk, S. V., Proskurnina, E. V., Konkova, M. S., Abramova, M. S., Кальянов, А. А., Ershova, E. S., Izhevskaya, V. L., Kutsev, S. I., & Veiko, N. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010261 · Cited by 16
Exercise-Boosted Mitochondrial Remodeling in Parkinson’s Disease
Magaña, J. C., Deus, C. M., Giné‐Garriga, M., Montané, J., & Pereira, S. P. (2022) · Biomedicines · doi:10.3390/biomedicines10123228 · Cited by 15
Upregulation of the ERRγ–VDAC1 axis underlies the molecular pathogenesis of pancreatitis
Chanda, D., Thoudam, T., Sinam, I. S., Lim, C. W., Kim, M., Wang, J., Lee, K., Ma, J., Saxena, R., Choi, J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219644120 · Cited by 15
Ma, G., Liu, Y., Zhang, Q., Zhang, B.-G., Zhao, N. O., Wang, Q.-L., & Wang, X. (2014) · Hepatology International · doi:10.1007/s12072-014-9529-5 · Cited by 15
Drugs for Targeted Therapies of Alzheimer’s Disease
Tam, C., Wong, J. H., Ng, T. B., Tsui, S. K., & Zuo, T. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180430150940 · Cited by 15
Nargesi, A. A., Farah, M. C., Zhu, X.-Y., Zhang, L., Tang, H. J., Jordan, K. L., Saadiq, I. M., Lerman, A., Lerman, L. O., & Eirin, A. (2020) · American Journal of Hypertension · doi:10.1093/ajh/hpaa202 · Cited by 17
The Role of Mitochondria in Phytochemically Mediated Disease Amelioration
Koh, Y., Ho, C., & Pan, M. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c08921 · Cited by 14
Stauch, K. L., Totusek, S., Trease, A. J., Estrella, L. D., Emanuel, K. M., Fangmeier, A., & Fox, H. S. (2023) · Scientific Reports · doi:10.1038/s41598-023-38484-0 · Cited by 15
An Update on Nucleolar Stress: The Transcriptional Control of Autophagy
Pfister, A. S. (2023) · Cells · doi:10.3390/cells12162071 · Cited by 15
Host Subcellular Organelles: Targets of Viral Manipulation
Song, M. S., Lee, D., Lee, C.-Y., Park, S., & Yang, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031638 · Cited by 15
Watzlawik, J. O., Hou, X., Richardson, T., Lewicki, S. L., Siuda, J. S., Wszołek, Z. K., Cook, C. N., Petrucelli, L., Deture, M. A., Dickson, D. W., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2356490 · Cited by 14
Decoding molecular mechanisms: brain aging and Alzheimer’s disease
Hayat, M., Syed, R. A., Qaiser, H., Uzair, M., Al-Regaiey, K., Khallaf, R. A., Albassam, L. A. M., Kaleem, I., Wang, X., Wang, R., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01403 · Cited by 14
Qi, L. I. N., Yating, L. I. N., Xinyan, L. I. A. O., Ziyi, C. H. E. N., Mengmeng, D. E. N. G., & Zhong, Z. (2024) · Scientific Reports · doi:10.1038/s41598-024-78136-5 · Cited by 15
BNIP3 Downregulation Ameliorates Muscle Atrophy in Cancer Cachexia
Fornelli, C., Beltrà, M., Zorzano, A., Costelli, P., Sebastián, D., & Penna, F. (2024) · Cancers · doi:10.3390/cancers16244133 · Cited by 14
Ahmed, H. S. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04154-3 · Cited by 15
Lizama, B. N., Palubinsky, A. M., & McLaughlin, B. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.013 · Cited by 14
Loss of Peter Pan (PPAN) Affects Mitochondrial Homeostasis and Autophagic Flux
Dannheisig, D. P., Beck, E., Calzia, E., Walther, P., Behrends, C., & Pfister, A. S. (2019) · Cells · doi:10.3390/cells8080894 · Cited by 14
Sabán-Ruiz, J., & Ly-Pen, D. (2020) · The journal of nutrition health & aging · doi:10.1007/s12603-020-1385-5 · Cited by 14
Tiwari, S., & Singh, S. (2020) · The Neuroscientist · doi:10.1177/1073858420942211 · Cited by 14
Regulation of mitochondrial dynamics in 2-methoxyestradiol-mediated osteosarcoma cell death
Górska‐Ponikowska, M., Bastian, P., Zauszkiewicz–Pawlak, A., Płoska, A., Zubrzycki, A., Kuban‐Jankowska, A., Nußberger, S., Kalinowski, L., & Kmieć, Z. (2021) · Scientific Reports · doi:10.1038/s41598-020-80816-x · Cited by 14
Blignaut, M., Harries, S., Lochner, A., & Huisamen, B. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8850708 · Cited by 14
Autophagy activity in cholangiocarcinoma is associated with anatomical localization of the tumor
Lendvai, G., Szekerczés, T., Illyés, I., Csengeri, M., Schlachter, K., Szabó, E., Lotz, G., Kiss, A., Borka, K., & Schaff, Z. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253065 · Cited by 14
Ji, H., Wu, D., Kimberlee, O., Li, R., & Qian, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.700585 · Cited by 14
RetractedWang, Y., Su, R., Liu, P., Yuan, Z., Han, Y., Zhang, H., & Weng, Q. (2021) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00105.2021 · Cited by 14
Mitophagy induced by classical swine fever virus nonstructural protein 5A promotes viral replication
Chengcheng, Z., Xiuling, W., Jiahao, S., Guo, M., Zhang, X., & Wu, Y. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198886 · Cited by 14
Aging: Epigenetic modifications
Mishra, S., Raval, M., Kachhawaha, A. S., Tiwari, B. S., & Tiwari, A. K. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.02.002 · Cited by 14
Etiopathogenesis of oncocytomas
Correia, M., Silva-Pinheiro, P., Batısta, R., Soares, P., Sobrinho-Simões, M. A., & Máximo, V. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.06.014 · Cited by 16
Rao, Q., Yang, M., Liu, G., Wang, J., Bu, Y., Zhang, J., Zhu, X., Chen, G., Zhu, W., & Zhou, H. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.127169 · Cited by 14
Min, H., Jung, Y., Park, K. H., & Lee, H. (2019) · Anticancer Research · doi:10.21873/anticanres.13956 · Cited by 14
Isolation, Characterization, and Autophagy Function of BECN1-Splicing Isoforms in Cancer Cells
Maheshwari, C., Vidoni, C., Titone, R., Castiglioni, A., Lora, C., Follo, C., & Isidoro, C. (2022) · Biomolecules · doi:10.3390/biom12081069 · Cited by 13
Mukkala, A. N., Petrut, R., Goldfarb, R., Beroncal, E. L., Leung, C. H., Khan, Z. R., Ailenberg, M., Jerkić, M., Andreazza, A. C., Rhind, S. G., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.03.002 · Cited by 14
Jian, L., Wu, H., Zeng, H., Quan, T., Xia, F., Xiang, S., & Zhou, B. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105770 · Cited by 13
An integral role of mitochondrial function in the pathophysiology of preeclampsia
Kobayashi, H., Yoshimoto, C., Matsubara, S., Shigetomi, H., & Imanaka, S. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09285-z · Cited by 14
Bhat, S. A., Vasi, Z., Jiang, L., Selvaraj, S., Ferguson, R., Salarvand, S., Gudur, A., Adhikari, R., Castillo, V., Ismail, H., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114783 · Cited by 13
Grx2 Regulates Skeletal Muscle Mitochondrial Structure and Autophagy
Liaghati, A., Pileggi, C. A., Parmar, G., Patten, D. A., Hadžimustafić, N., Cuillerier, A., Menzies, K. J., Burelle, Y., & Harper, M. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.604210 · Cited by 13
Zhao, M., Lian, A., Zhong, L., & Guo, R. (2022) · Acta Physiologica · doi:10.1111/apha.13757 · Cited by 14
Panda, S. P., Dhurandhar, Y., & Agrawal, M. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.07.002 · Cited by 13
Keeping the beat against time: Mitochondrial fitness in the aging heart
Mendoza, A., & Karch, J. M. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.951417 · Cited by 13
Dai, T., Lu, J., Tao, X., Zhang, X., Li, M., Jin, M., Sun, P., Liu, W., Jiao, L., & Zhou, Q. (2022) · Aquaculture Reports · doi:10.1016/j.aqrep.2022.101272 · Cited by 13
Strategies for imaging mitophagy in high-resolution and high-throughput
Indira, D., Varadarajan, S. N., Lupitha, S. S., Lekshmi, A., Mathew, K. A., Chandrasekharan, A., Pillai, P. R., Kadamberi, I. P., Ramachandran, I., Sekar, H., et al. (2017) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2017.10.003 · Cited by 13
Defective immunometabolism pathways in cystic fibrosis macrophages
Hamilton, K., Krause, K., Badr, A., Daily, K. P., Estfanous, S. Z. K., Eltobgy, M. M., Khweek, A. A., Anne, M. N. K., Carafice, C., Baetzhold, D., et al. (2020) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2020.10.006 · Cited by 13
Sopha, P., Phutubtim, N., Chantrathonkul, B., Ploypradith, P., Ruchirawat, S., & Chittchang, M. (2021) · Toxicology · doi:10.1016/j.tox.2021.152963 · Cited by 13
Maddalena, L. A., Ghelfi, M. D., Atkinson, J., & Stuart, J. A. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.11.005 · Cited by 13
Lewis, L., Valvi, D., Gedaly, R., & Martí, F. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1621759 · Cited by 12
McCaffrey, J. M., & Ibdah, J. A. (2025) · Nutrients · doi:10.3390/nu17182972 · Cited by 14
Determination of mitophagy by electron microscope
Li, Z., Wu, Q., Le, L., Sun, S., Sun, S., Wang, Z., & Li, J. (2020) · Methods in cell biology · doi:10.1016/bs.mcb.2020.10.015 · Cited by 12
Transmembrane Parkinson’s disease mutation of PINK1 leads to altered mitochondrial anchoring
Brassard, R., Arutyunova, E. I., Takyi, E., Espinoza‐Fonseca, L. M., Young, H. S., Touret, N., & Lemieux, M. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108253 · Cited by 13
Chen, X., Li, L., Jiang, J., Li, K., Su, Z., Zhang, F., Zhang, W., & Zhao, G. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197934 · Cited by 12
Xu, S., Zheng, G., & Zhou, K. (2022) · Analytical Biochemistry · doi:10.1016/j.ab.2021.114545 · Cited by 13
Jeong, Y., Davis, C.-H. O., Muscarella, A. M., Navarro, H. H., Deshpande, V. A., Moore, L. G., Keun-young Kim, A., Ellisman, M. H., & Marsh‐Armstrong, N. (2025) · eLife · doi:10.7554/elife.103844 · Cited by 12
Zha, C., Xiao, H., Song, B., Zheng, C., Yang, X., Wang, W., & Wang, L. (2020) · Journal of Applied Microbiology · doi:10.1111/jam.14747 · Cited by 12
Wu, M., Chen, P., Liu, F., Lv, B., Ge, M., Jiang, P., Xu, W., Liu, X., & Yang, D. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.02.037 · Cited by 12
Suárez, V. T., Gallet, B., Chevallet, M., Jouneau, P., Tucoulou, R., Veronesi, G., & Deniaud, A. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2021.107766 · Cited by 12
Teodoro, J. S., Machado, I. F., Castela, A. C., Amorim, J. A., Jarak, I., Carvalho, R. A., Palmeira, C. M., & Rolo, A. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111738 · Cited by 12
Lijie, G., Yueyue, Z., Zhu, N., Ling, W., Xuan, W., & Weijie, Y. (2019) · Cell Biology International · doi:10.1002/cbin.11097 · Cited by 12
Whole-genome resequencing identifies candidate genes associated with heat adaptation in chickens
Bai, H., Zhao, N., Li, X., Ding, Y., Guo, Q., Chen, G., & Chang, G. (2024) · Poultry Science · doi:10.1016/j.psj.2024.104139 · Cited by 11
Liang, J., Wei, X., Hou, W., Wang, H., Ma, R., Gao, Y., Du, Y., & Zhang, Q. (2023) · Chinese Medicine · doi:10.1186/s13020-023-00858-x · Cited by 11
Sun, L., Hong, X., Wang, D., & Li, Y. (2023) · European Journal of Neuroscience · doi:10.1111/ejn.16218 · Cited by 11
Liu, S., Yang, T., Wang, Y., Ma, X., Shi, Y., Zhao, Y., & Li, J. (2024) · Journal of Pineal Research · doi:10.1111/jpi.70014 · Cited by 11
Pharmacological Progress of Mitophagy Regulation
Sehgal, S. A., Wu, H., Sajid, M., Sohail, S., Ahsan, M., Parveen, G., Riaz, M., Khan, M. S., Iqbal, M. N., & Malik, A. (2023) · Current Neuropharmacology · doi:10.2174/1570159x21666230314140528 · Cited by 11
Wang, Q., Yang, J., Pan, R., & Zha, Z. (2024) · Immunobiology · doi:10.1016/j.imbio.2024.152799 · Cited by 11
Mechanistic Role of Kinases in the Regulation of Mitochondrial Fitness
Sorriento, D., Gambardella, J., Fiordelisi, A., Trimarco, B., Ciccarelli, M., Iaccarino, G., & Santulli, G. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_26 · Cited by 11
Maturation of White Adipose Tissue Function in C57BL/6j Mice From Weaning to Young Adulthood
Kodde, A., Engels, E., Oosting, A., van Limpt, K., van der Beek, E. M., & Keijer, J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00836 · Cited by 11
Implications of intracellular protein degradation pathways in Parkinson's disease and therapeutics
Amrutha, K., Mishra, A., & Singh, S. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25101 · Cited by 11
Divergent Signaling Pathways May Lead to Convergence in Cancer Therapy - A Review
Qayum, A., Shah, S. M., & Singh, S. K. (2022) · Cellular Physiology and Biochemistry · doi:10.33594/000000512 · Cited by 10
Heat and mitochondrial bioenergetics
Schulze, A. T. V., & Geiger, P. C. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100553 · Cited by 10
Mitochondrial damage and clearance in retinal pigment epithelial cells
Gurubaran, I. S. (2024) · Acta Ophthalmologica · doi:10.1111/aos.16661 · Cited by 11
Glycation in the cardiomyocyte
Delligatti, C. E., & Kirk, J. A. (2024) · Vitamins and hormones · doi:10.1016/bs.vh.2024.04.005 · Cited by 10
Zhou, X., Lu, Q., Wang, Q., Chu, W., Huang, J., Yu, J.-M., Nong, Y., & Lu, W. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s493037 · Cited by 11
Peng, F., Ai, X., Hao, B., Bu, X., Zhao, Z., Yang, L., & Gao, B. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c00464 · Cited by 10
TNFα enhances trovafloxacin-induced in vitro hepatotoxicity by inhibiting protective autophagy
Ahn, J., Jegal, H., Choi, M., Kim, S., Park, S., Ahn, J.-H., Han, H., Cho, H., Yoon, S., & Oh, J. (2021) · Toxicology Letters · doi:10.1016/j.toxlet.2021.02.009 · Cited by 10
Dai, H., Ma, B., Dai, X., Pang, J., Wang, J., Zhao, Y., Wang, M., Zhang, H., Gao, H., Qian, S., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.585286 · Cited by 10
Kingnate, C., Charoenkwan, K., Kumfu, S., Apaijai, N., Jaiwongkam, T., Khunamornpong, S., Chattipakorn, N., & Chattipakorn, S. C. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114587 · Cited by 10
Bioimaging tools reveal copper processing in fish cells by mitophagy
Xia, Y., & Wang, W. (2023) · Aquatic Toxicology · doi:10.1016/j.aquatox.2023.106633 · Cited by 10
Han, W., Li, H., Jiang, H., Xu, H., Lin, Y., Chen, J., Bi, C., & Liu, Z. (2023) · PeerJ · doi:10.7717/peerj.15977 · Cited by 10
He, Y.-J., Liu, J., Zhang, L., & Yan, J. (2023) · Talanta · doi:10.1016/j.talanta.2023.125362 · Cited by 10
Mitophagy and spermatogenesis: Role and mechanisms
Rotimi, D. E., Iyobhebhe, M. E., Oluwayemi, E. T., Evbuomwan, I. O., Asaleye, R. M., Ojo, O. A., & Adeyemı, O. S. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101698 · Cited by 11
Mechanisms of programmed cell death: structural and functional pathways. A narrative review.
Fernández‐Lázaro, D., Sanz, B., & Seco‐Calvo, J. (2024) · Investigación Clínica · doi:10.54817/ic.v65n2a09 · Cited by 10
Synthesis of resveratrol sulfates: turning a nightmare into a dream
Mattarei, A., Biasutto, L., Romio, M., Zoratti, M., & Paradisi, C. (2014) · Tetrahedron · doi:10.1016/j.tet.2014.09.063 · Cited by 10
Albumin Overload and PINK1/Parkin Signaling-Related Mitophagy in Renal Tubular Epithelial Cells
Tan, J., Xie, Q., Song, S., Miao, Y., & Zhang, Q. (2018) · Medical Science Monitor · doi:10.12659/msm.907718 · Cited by 10
Ouyang, S., Chen, W., Zeng, G., Lei, C., Tian, G.-P., Zhu, M., Liu, Y., & Yang, M. (2019) · Gene · doi:10.1016/j.gene.2019.144136 · Cited by 10
Quality control of mitochondria involves lysosomes in multiple definitive ways
Ma, X., & Ding, W.-X. (2024) · Autophagy · doi:10.1080/15548627.2024.2408712 · Cited by 10
Self-citationSarabhai, T., Kahl, S., Gancheva, S., Mastrototaro, L., Dewidar, B., Pesta, D., Ratter-Rieck, J. M., Bobrov, P., Jeruschke, K., Esposito, I., et al. (2024) · Metabolism · doi:10.1016/j.metabol.2023.155762 · Cited by 9
RetractedShi, P., Liu, Y., Sha, Y., Wang, J., Zhou, J., Liu, K., Cao, Y., Zhang, Q., Wang, X., & Sun, H. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107760 · Cited by 9
Sultana, O. F., Bandaru, M., Bushra, M. A., Reddy, P. H., & Reddy, A. P. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102957 · Cited by 11
A Metal-containing Nucleoside That Possesses Both Therapeutic and Diagnostic Activity against Cancer
Choi, J.-S., Maity, A., Gray, T., & Berdis, A. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620294 · Cited by 9
Unraveling and targeting RAS-driven metabolic signaling for therapeutic gain
DeLiberty, J. M., Robb, R. N., Gates, C. E., & Bryant, K. L. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.010 · Cited by 10
Metadata
- Authors
- Ding, W.-X., & Yin, X.-M.
- Affiliations
- University of Kansas Medical Center (US)
- Indiana University School of Medicine (US)
- Venue
- bchm
- Publisher
- Walter de Gruyter GmbH
- Published
- 2012-07-01
- Volume
- 393
- Issue
- 7
- Pages
- 547-564
- ISSN
- 1431-6730 (ISSN-L)
- 1437-4315
- PMC
- PMC3630798
- OpenAlex
- W2076769172
- Cited by
- 1,032
- References
- 166
- Citations by year
- 2026: 47 · 2025: 77 · 2024: 83 · 2023: 99 · 2022: 90 · 2021: 115 · 2020: 111 · 2019: 98 · 2018: 67 · 2017: 64 · 2016: 59 · 2015: 44 · 2014: 50 · 2013: 25 · 2012: 1
- FWCI
- 4.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biological Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- Funders
- National Institutes of Health (AA020518, RR016475)
- National Institute on Alcohol Abuse and Alcoholism (R01AA020518, R21AA017421, R37AA020518)
- National Cancer Institute (R01CA83817, R01CA083817)
- National Institute of General Medical Sciences (P20GM103418)
- National Center for Research Resources (P20RR021940, RR016475, P20RR016475)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitophagy, PINK1/Parkin pathway, Nix, BNIP3, mitochondrial priming, selective autophagy, neurodegenerative diseases, ischemia, energy homeostasis, cell death
- MeSH terms
- Aging, Animals, Disease, Humans, Mitochondria, Signal Transduction, Mitochondrial Proteins, 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