PINK1/Parkin-mediated mitophagy in mammalian cells

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

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

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

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

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

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

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835 · see citing works

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

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

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

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

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

Mitochondrial dynamics and inheritance during cell division, development and disease

Mishra, P., & Chan, D. C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3877 · Cited by 1,038 · 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

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

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

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 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 · cited 1× · 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

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

PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria

Okatsu, K., Oka, T., Iguchi, M., Imamura, K., Kosako, H., Tani, N., Kimura, M., Go, E., Koyano, F., Funayama, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms2016 · Cited by 602 · 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

Cytosolic p53 inhibits Parkin-mediated mitophagy and promotes mitochondrial dysfunction in the mouse heart

Hoshino, A., Mita, Y., Okawa, Y., Ariyoshi, M., Iwai-Kanai, E., Ueyama, T., Ikeda, K., Ogata, T., & Matoba, S. (2013) · Nature Communications · doi:10.1038/ncomms3308 · Cited by 536 · 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

Mitochondrial quality control: a matter of life and death for neurons

Rugarli, E. I., & Langer, T. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.38 · Cited by 419 · see citing works

The Protein Import Machinery of Mitochondria—A Regulatory Hub in Metabolism, Stress, and Disease

Harbauer, A. B., Zahedi, R. P., Sickmann, A., Pfanner, N., & Meisinger, C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.010 · 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

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

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

The Parkinson's disease–linked proteins Fbxo7 and Parkin interact to mediate mitophagy

Burchell, V., Nelson, D. E., Sánchez-Martínez, Á., Delgado-Camprubi, M., Ivatt, R. M., Pogson, J. H., Randle, S. J., Wray, S., Lewis, P. A., Houlden, H., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3489 · Cited by 334 · 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

Protecting the mitochondrial powerhouse

Scheibye‐Knudsen, M., Fang, E. F., Croteau, D. L., Wilson, D. M., & Bohr, V. A. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.11.002 · Cited by 330 · see citing works

Determinants and Functions of Mitochondrial Behavior

Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 315 · see citing works

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

Wauer, T., Swatek, K. N., Wagstaff, J. L., Gladkova, C., Pruneda, J. N., Michel, M. A., Gersch, M., Johnson, C. M., Freund, S. M. V., & Komander, D. (2014) · The EMBO Journal · doi:10.15252/embj.201489847 · Cited by 303 · see citing works

Phosphorylated ubiquitin chain is the genuine Parkin receptor

Okatsu, K., Koyano, F., Kimura, M., Kosako, H., Saeki, Y., Tanaka, K., & Matsuda, N. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201410050 · Cited by 261 · 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

PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy

Kawajiri, S., Saiki, S., Sato, S., Sato, F., Hatano, T., Eguchi, H., & Hattori, N. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.016 · Cited by 246 · 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

Organellophagy: Eliminating cellular building blocks via selective autophagy

Okamoto, K. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201402054 · Cited by 218 · 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

Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering

Shiba‐Fukushima, K., Arano, T., Matsumoto, G., Inoshita, T., Yoshida, S., Ishihama, Y., Ryu, K., Nukina, N., Hattori, N., & Imai, Y. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004861 · Cited by 186 · see citing works

Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease

Shi, G. W., Lee, J. R., Grimes, D. A., Racacho, L., Ye, D., Yang, H. H., Ross, O. A., Farrer, M. J., McQuibban, G. A., & Bulman, D. E. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr077 · Cited by 169 · 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

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

Unconventional PINK1 localization mechanism to the outer membrane of depolarized mitochondria drives Parkin recruitment

Okatsu, K., Kimura, M., Oka, T., Tanaka, K., & Matsuda, N. (2015) · Journal of Cell Science · doi:10.1242/jcs.161000 · Cited by 127 · see citing works

PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402

Aerts, L., Craessaerts, K., Strooper, B. D., & Morais, V. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620906 · Cited by 117 · 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

Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin

Caulfield, T. R., Fiesel, F. C., Moussaud-Lamodière, E. L., Dourado, D. F. A. R., Flores, S. C., & Springer, W. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003935 · Cited by 108 · see citing works

S-nitrosylation regulates mitochondrial quality control via activation of parkin

Ozawa, K., Komatsubara, A. T., Nishimura, Y., Sawada, T., Kawafune, H., Tsumoto, H., Tsuji, Y., Zhao, J., Kyotani, Y., Tanaka, T., et al. (2013) · Scientific Reports · doi:10.1038/srep02202 · Cited by 96 · 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

SARM1 and TRAF6 bind to and stabilize PINK1 on depolarized mitochondria

Murata, H., Sakaguchi, M., Kataoka, K., & Huh, N.-H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-01-0016 · Cited by 82 · 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

Select E2 enzymes differentially regulate parkin activation and mitophagy

Fiesel, F. C., Moussaud-Lamodière, E. L., Ando, M., & Springer, W. (2014) · Journal of Cell Science · doi:10.1242/jcs.147520 · Cited by 72 · see citing works

Profiling of Parkin-Binding Partners Using Tandem Affinity Purification

Zanon, A., Raković, A., Blankenburg, H., Doncheva, N. T., Schwienbacher, C., Serafin, A., Alexa, A., Weichenberger, C. X., Albrecht, M., Klein, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078648 · Cited by 60 · see citing works

AF-6 is a positive modulator of the PINK1/parkin pathway and is deficient in Parkinson's disease

Haskin, J., Szargel, R., Shani, V., Mekies, L. N., Rott, R., Lim, G. G. Y., Lim, K., Bandopadhyay, R., Wolosker, H., & Engelender, S. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt058 · Cited by 29 · see citing works

Mitochondrial energetics in the kidney

Bhargava, P., & Schnellmann, R. G. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.107 · Cited by 1,363 · 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

Spermidine in health and disease

Madeo, F., Eisenberg, T., Pietrocola, F., & Kroemer, G. (2018) · Science · doi:10.1126/science.aan2788 · Cited by 1,154 · see citing works

Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances

Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works

Sirt1 and the Mitochondria

Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740 · see citing works

Caloric Restriction Mimetics against Age-Associated Disease: Targets, Mechanisms, and Therapeutic Potential

Madeo, F., Carmona-Gutierrez, D., Hofer, S. J., & Kroemer, G. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.018 · Cited by 630 · 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

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

Complex interplay between autophagy and oxidative stress in the development of pulmonary disease

Ornatowski, W., Lü, Q., Yegambaram, M., Flores, A. G., Zemskov, E. A., Maltepe, E., Fineman, J. R., Wang, T., & Black, S. M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101679 · Cited by 474 · see citing works

XBP1 deficiency promotes hepatocyte pyroptosis by impairing mitophagy to activate mtDNA-cGAS-STING signaling in macrophages during acute liver injury

Liu, Z., Wang, M., Wang, X., Bu, Q., Wang, Q., Su, W., Li, L., Zhou, H., & Lü, L. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102305 · Cited by 353 · see citing works

Selective autophagy as a potential therapeutic target for neurodegenerative disorders

Scrivo, A., Bourdenx, M., Pampliega, O., & Cuervo, A. M. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30238-2 · Cited by 355 · see citing works

The Role of Autophagy and Mitophagy in Bone Metabolic Disorders

Wang, S., Deng, Z.-T., Ma, Y.-C., Jin, J., Qi, F., Li, S., Liu, C., Lyu, F.-J., & Zheng, Q. (2020) · International Journal on Biological Sciences · doi:10.7150/ijbs.46627 · Cited by 305 · see citing works

BNIP3L/NIX and FUNDC1-mediated mitophagy is required for mitochondrial network remodeling during cardiac progenitor cell differentiation

Lampert, M. A., Orogo, A. M., Najor, R. H., Hammerling, B. C., Leon, L. J., Wang, B. J., Kim, T.-Y., Sussman, M. A., & Gustafsson, Å. B. (2019) · Autophagy · doi:10.1080/15548627.2019.1580095 · Cited by 314 · see citing works

Regulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control

Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 309 · see citing works

Aging and Parkinson's disease: Different sides of the same coin?

Collier, T. J., Kanaan, N. M., & Kordower, J. H. (2017) · Movement Disorders · doi:10.1002/mds.27037 · Cited by 271 · see citing works

Mitochondria-associated membranes in aging and senescence: structure, function, and dynamics

Janikiewicz, J., Szymański, J., Malińska, D., Patalas‐Krawczyk, P., Michalska, B., Duszyński, J., Giorgi, C., Bonora, M., Dobrzyń, A., & Wieckowski, M. R. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0105-5 · Cited by 248 · see citing works

SPLICS: a split green fluorescent protein-based contact site sensor for narrow and wide heterotypic organelle juxtaposition

Cieri, D., Vicario, M., Giacomello, M., Vallese, F., Filadi, R., Wagner, T., Pozzan, T., Pizzo, P., Scorrano, L., Brini, M., et al. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0033-z · Cited by 245 · see citing works

PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases

Martire, S., Mosca, L., & D’Erme, M. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.001 · Cited by 228 · see citing works

Mitochondrial Dysfunction as a Driver of Cognitive Impairment in Alzheimer’s Disease

Sharma, C., Kim, S., Nam, Y., Jung, U. J., & Kim, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094850 · Cited by 241 · see citing works

Insulin Resistance and Diabetes Mellitus in Alzheimer’s Disease

Burillo, J., Marqués, P., Jiménez, B., González-Blanco, C., Benito, M., & Guillén, C. (2021) · Cells · doi:10.3390/cells10051236 · Cited by 234 · see citing works

Mitophagy in Human Diseases

Doblado, L., Lueck, C., Rey, C., Samhan-Arias, A. K., Priéto, I., Stacchiotti, A., & Monsalve, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083903 · Cited by 229 · see citing works

Mitochondrial dysfunction in fibrotic diseases

Li, X., Zhang, W. Y., Cao, Q., Wang, Z., Zhao, M., Xu, L., & Zhuang, Q. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00316-9 · Cited by 226 · see citing works

Mechanisms and roles of mitophagy in neurodegenerative diseases

Wang, Y., Liu, N., & Lu, B. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13140 · Cited by 214 · see citing works

Mitochondria-associated membranes as hubs for neurodegeneration

Krols, M., Isterdael, G. V., Asselbergh, B., Kremer, A., Lippens, S., Timmerman, V., & Janssens, S. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1528-7 · Cited by 200 · see citing works

Ketoconazole exacerbates mitophagy to induce apoptosis by downregulating cyclooxygenase-2 in hepatocellular carcinoma

Chen, Y., Chen, H., Wang, K., Zhang, L., Huang, Z., Liu, J., Zhang, Z., Luo, M., Lei, Y., Peng, Y., et al. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.09.022 · Cited by 192 · see citing works

Targeting autophagy using metallic nanoparticles: a promising strategy for cancer treatment

Cordani, M., & Somoza, Á. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2973-y · Cited by 189 · see citing works

Molecular Mechanisms of Mitochondrial Quality Control in Ischemic Cardiomyopathy

Chang, X., Liu, R., Li, R., Peng, Y., Zhu, P., & Zhou, H. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.76223 · Cited by 190 · see citing works

Emerging role of mitophagy in human diseases and physiology

Um, J., & Yun, J. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.6.056 · Cited by 181 · see citing works

PTEN-L is a novel protein phosphatase for ubiquitin dephosphorylation to inhibit PINK1–Parkin-mediated mitophagy

Wang, L., Cho, Y.-L., Tang, Y., Wang, J., Park, J., Wu, Y., Wang, C., Tong, Y., Chawla, R., Zhang, J., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0056-0 · Cited by 179 · see citing works

Myocardial stress and autophagy: mechanisms and potential therapies

Delbridge, L. M. D., Mellor, K. M., TAYLOR, D. J., & Gottlieb, R. A. (2017) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2017.35 · Cited by 176 · see citing works

Role of the mitochondrial contact site and cristae organizing system in membrane architecture and dynamics

Rampelt, H., Zerbes, R. M., van der Laan, M., & Pfanner, N. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.05.020 · Cited by 174 · see citing works

PGRN acts as a novel regulator of mitochondrial homeostasis by facilitating mitophagy and mitochondrial biogenesis to prevent podocyte injury in diabetic nephropathy

Zhou, D., Zhou, M., Wang, Z., Fu, Y., Jia, M., Wang, X., Liu, M., Zhang, Y., Sun, Y., Lu, Y., et al. (2019) · Cell Death &amp; Disease · doi:10.1038/s41419-019-1754-3 · Cited by 162 · see citing works

The interplay of autophagy and oxidative stress in the pathogenesis and therapy of retinal degenerative diseases

Chang, K., Liu, P., Chang, C., Lin, Y., Chen, Y., & Shu, C. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00736-9 · Cited by 168 · see citing works

Mitochondrial‐Endoplasmic Reticulum Communication‐Mediated Oxidative Stress and Autophagy

Liu, X., Hussain, R., Mehmood, K., Tang, Z., Zhang, H., & Li, Y. (2022) · BioMed Research International · doi:10.1155/2022/6459585 · Cited by 164 · see citing works

Protective effects of metformin against osteoarthritis through upregulation of SIRT3-mediated PINK1/Parkin-dependent mitophagy in primary chondrocytes

Wang, C., Yang, Y., Zhang, Y., Liu, J., Yao, Z., & Zhang, C. (2018) · BioScience Trends · doi:10.5582/bst.2018.01263 · Cited by 161 · see citing works

Fisetin induces autophagy in pancreatic cancer cells via endoplasmic reticulum stress- and mitochondrial stress-dependent pathways

Jia, S., Xu, X., Zhou, S., Chen, Y., Ding, G., & Cao, L. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1366-y · Cited by 157 · see citing works

Mitochondrial dynamics and cell death in heart failure

Marı́n-Garcı́a, J., & Akhmedov, A. T. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9530-2 · Cited by 154 · see citing works

Supplementing Glycine and N-Acetylcysteine (GlyNAC) in Older Adults Improves Glutathione Deficiency, Oxidative Stress, Mitochondrial Dysfunction, Inflammation, Physical Function, and Aging Hallmarks: A Randomized Clinical Trial

Kumar, P., Liu, C., Suliburk, J. W., Hsu, J. W.-C., Muthupillai, R., Jahoor, F., Minard, C. G., Taffet, G. E., & Sekhar, R. V. (2022) · The Journals of Gerontology Series A · doi:10.1093/gerona/glac135 · Cited by 161 · see citing works

Mitochondrial dynamics, transport, and quality control: A bottleneck for retinal ganglion cell viability in optic neuropathies

Ito, Y. A., & Di Polo, A. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.08.014 · Cited by 142 · see citing works

Shaping the mitochondrial inner membrane in health and disease

Colina-Tenorio, L., Horten, P., Pfanner, N., & Rampelt, H. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13031 · Cited by 151 · see citing works

Optineurin-mediated mitophagy protects renal tubular epithelial cells against accelerated senescence in diabetic nephropathy

Chen, K., Dai, H., Yuan, J., Chen, J., Lin, L., Zhang, W., Wang, L., Zhang, J., Li, K., & He, Y. (2018) · Cell Death &amp; Disease · doi:10.1038/s41419-017-0127-z · Cited by 150 · see citing works

Mitophagy links oxidative stress conditions and neurodegenerative diseases

Jung, J., Huh, Y., Shefa, U., Jeong, N., Song, I., Chung, H.-J., & Kim, D. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.249218 · Cited by 152 · see citing works

Autophagy in kidney disease and aging: lessons from rodent models

Lenoir, O., Tharaux, P., & Huber, T. B. (2016) · Kidney International · doi:10.1016/j.kint.2016.04.014 · Cited by 150 · see citing works

RING-Between-RING E3 Ligases: Emerging Themes amid the Variations

Dove, K. K., & Klevit, R. E. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.08.008 · Cited by 140 · see citing works

Impaired mitophagy links mitochondrial disease to epithelial stress in methylmalonyl-CoA mutase deficiency

Luciani, A., Schumann, A., Berquez, M., Chen, Z., Nieri, D., Failli, M., Debaix, H., Festa, B. P., Tokonami, N., Raimondi, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14729-8 · Cited by 131 · see citing works

Hydrogen-rich saline alleviates inflammation and apoptosis in myocardial I/R�injury via PINK-mediated autophagy

Li, Y., Chen, H., Wu, Q., & Xie, K. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4264 · Cited by 135 · see citing works

PINK1/Parkin‐mediated mitophagy promotes apelin‐13‐induced vascular smooth muscle cell proliferation by AMPKα and exacerbates atherosclerotic lesions

He, L., Zhou, Q., Huang, Z., Xu, J., Zhou, H., Lv, D., Lu, L., Huang, S., Tang, M., Zhong, J., et al. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27527 · Cited by 133 · see citing works

Diquat-induced oxidative stress increases intestinal permeability, impairs mitochondrial function, and triggers mitophagy in piglets1

Cao, S., Wu, H. C., Wang, C., Zhang, Q., Jiao, L., Lin, F., & Hu, C. (2018) · Journal of Animal Science · doi:10.1093/jas/sky104 · Cited by 130 · see citing works

Molecular Interactions Between Reactive Oxygen Species and Autophagy in Kidney Disease

Kaushal, G. P., Chandrashekar, K., & Juncos, L. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153791 · Cited by 129 · see citing works

Pharmacological Targeting of Mitochondria in Diabetic Kidney Disease

Cleveland, K. H., & Schnellmann, R. G. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000560 · Cited by 130 · see citing works

The bile acid TUDCA and neurodegenerative disorders: An overview

Zangerolamo, L., Vettorazzi, J. F., Rosa, L. R. D. O., Carneiro, E. M., & Barbosa, H. C. L. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119252 · Cited by 127 · see citing works

ATM mediates spermidine-induced mitophagy via PINK1 and Parkin regulation in human fibroblasts

Qi, Y., Qiu, Q., Gu, X., Tian, Y., & Zhang, Y. (2016) · Scientific Reports · doi:10.1038/srep24700 · Cited by 122 · see citing works

Mitochondrial Function and Mitophagy in the Elderly: Effects of Exercise

Moreira, O. C., Estébanez, B., Martínez‐Flórez, S., Fernández, J. A. D. P., Cuevas, M. J., & González‐Gallego, J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2012798 · Cited by 120 · see citing works

Loss of conserved Gsdma3 self-regulation causes autophagy and cell death

Shi, P., Tang, A., Xian, L., Hou, S., Zou, D., Lv, Y.-S., Huang, Z., Wang, Q., Song, A., Lin, Z., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150204 · Cited by 115 · see citing works

Autophagy-related proteins are functionally active in human spermatozoa and may be involved in the regulation of cell survival and motility

Aparicio, I. M., Espino, J., Bejarano, I., Gallardo, A., Campo, M. L., Salido, G. M., Pariente, J. A., Peña, F. J., & Tapia, J. A. (2016) · Scientific Reports · doi:10.1038/srep33647 · Cited by 119 · see citing works

Autophagy Activator Drugs: A New Opportunity in Neuroprotection from Misfolded Protein Toxicity

Thellung, S., Corsaro, A., Nizzari, M., Barbieri, F., & Florio, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040901 · Cited by 105 · see citing works

Resveratrol improves intestinal barrier function, alleviates mitochondrial dysfunction and induces mitophagy in diquat challenged piglets 1

Cao, S., Shen, Z., Wang, C., Zhang, Q., Hong, Q., He, Y., & Hu, C. (2018) · Food & Function · doi:10.1039/c8fo02091d · Cited by 118 · see citing works

Modulation of Mitochondrial Membrane Potential and ROS Generation by Nicotinamide in a Manner Independent of SIRT1 and Mitophagy

Song, S. B., Jang, S.-Y., Kang, H. T., Wei, B., Jeoun, U.-W., Yoon, G. S., & Hwang, E. S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0081 · Cited by 114 · see citing works

A novel small-molecule activator of Sirtuin-1 induces autophagic cell death/mitophagy as a potential therapeutic strategy in glioblastoma

Yao, Z., Zhang, X., Zhen, Y., He, X., Zhao, S., Li, X., Yang, B., Gao, F., Guo, F., Fu, L., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0799-z · Cited by 115 · see citing works

Involvement of mitochondrial dynamics and mitophagy in diabetic endothelial dysfunction and cardiac microvascular injury

Zhang, X., Zhou, H., & Chang, X. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03599-w · Cited by 114 · see citing works

PGC-1α protects RPE cells of the aging retina against oxidative stress-induced degeneration through the regulation of senescence and mitochondrial quality control. The significance for AMD pathogenesis

Kaarniranta, K., Kajdanek, J., Morawiec, J., Pawlowska, E., & Blasiak, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082317 · Cited by 112 · see citing works

Metformin modulates mitochondrial function and mitophagy in peripheral blood mononuclear cells from type 2 diabetic patients

Marañón, A., Díaz-Pozo, P., Canet, F., Díaz‐Morales, N., Abad‐Jiménez, Z., López‐Domènech, S., Vezza, T., Apostolova, N., Morillas, C., Rocha, M., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102342 · Cited by 112 · see citing works

‘Hints’ in the killer protein gasdermin D: unveiling the secrets of gasdermins driving cell death

Qiu, S., Liu, J., & Xing, F. (2017) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2017.24 · Cited by 111 · see citing works

Regulation of the NLRP3 inflammasome by autophagy and mitophagy

Gupta, S., Cassel, S. L., Sutterwala, F. S., & Dagvadorj, J. (2024) · Immunological Reviews · doi:10.1111/imr.13410 · Cited by 112 · see citing works

Mitochondrial Quality Control in Cerebral Ischemia–Reperfusion Injury

Wu, M., Gu, X., & Ma, Z.-L. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02494-8 · Cited by 111 · see citing works

Targeting CRL4 suppresses chemoresistant ovarian cancer growth by inducing mitophagy

Meng, Y., Qiu, L., Zeng, X., Hu, X., Zhang, Y., Wan, X., Mao, X., Wu, J., Xu, Y., Xiong, Q., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01253-y · Cited by 113 · see citing works

Amyotrophic lateral sclerosis-associated mutant SOD1 inhibits anterograde axonal transport of mitochondria by reducing Miro1 levels

Möller, A., Bauer, C. S., Cohen, R. N., Webster, C. P., & Vos, K. J. D. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx348 · Cited by 109 · see citing works

Weaning disrupts intestinal antioxidant status, impairs intestinal barrier and mitochondrial function, and triggers mitophagy in piglets1

Cao, S., Wang, C. C., Wu, H. C., Zhang, Q. H., Jiao, L., & Hu, C. (2018) · Journal of Animal Science · doi:10.1093/jas/skx062 · Cited by 109 · see citing works

LPS challenge increased intestinal permeability, disrupted mitochondrial function and triggered mitophagy of piglets

Cao, S., Zhang, Q., Wang, C., Wu, H. C., Jiao, L., Hong, Q., & Hu, C. (2018) · Innate Immunity · doi:10.1177/1753425918769372 · Cited by 108 · see citing works

Berberine Promotes Cardiac Function by Upregulating PINK1/Parkin-Mediated Mitophagy in Heart Failure

Abudureyimu, M., Yu, W., Cao, R. Y., Zhang, Y., Liu, H., & Zheng, H. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.565751 · Cited by 108 · see citing works

Ubiquitin and Receptor-Dependent Mitophagy Pathways and Their Implication in Neurodegeneration

Fritsch, L. E., Moore, M. E., Sarraf, S. A., & Pickrell, A. M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.015 · Cited by 104 · see citing works

MICOS and the mitochondrial inner membrane morphology – when things get out of shape

Mukherjee, I., Ghosh, M., & Meinecke, M. (2021) · FEBS Letters · doi:10.1002/1873-3468.14089 · Cited by 104 · see citing works

Mitophagy in neurodegenerative diseases

Rodolfo, C., Campello, S., & Cecconi, F. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.004 · Cited by 100 · see citing works

Melatonin induced suppression of ER stress and mitochondrial dysfunction inhibited NLRP3 inflammasome activation in COPD mice

Mahalanobish, S., Dutta, S., Saha, S., & Sil, P. C. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111588 · Cited by 96 · see citing works

Lycopene mitigates DEHP-induced hepatic mitochondrial quality control disorder via regulating SIRT1/PINK1/mitophagy axis and mitochondrial unfolded protein response

Zhao, Y., Li, H., Luo, Y., Cui, J.-G., Talukder, M., & Li, J. (2021) · Environmental Pollution · doi:10.1016/j.envpol.2021.118390 · Cited by 96 · see citing works

Arsenic induces hepatic insulin resistance via mtROS-NLRP3 inflammasome pathway

Jia, X., Qiu, T., Yao, X., Jiang, L., Wang, N., Wei, S., Tao, Y., Pei, P., Wang, Z., Zhāng, J., et al. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.123034 · Cited by 95 · see citing works

Inflammasome and Mitophagy Connection in Health and Disease

Yuk, J., Silwal, P., & Jo, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134714 · Cited by 95 · see citing works

Disruption of Mitochondrial Homeostasis: The Role of PINK1 in Parkinson’s Disease

Vizziello, M., Borellini, L., Franco, G., & Ardolino, G. (2021) · Cells · doi:10.3390/cells10113022 · Cited by 98 · see citing works

The mitochondrial unfolded protein response: A multitasking giant in the fight against human diseases

Zhou, Z., Fan, Y., Zong, R., & Tan, K. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101702 · Cited by 95 · see citing works

The reproductive and transgenerational toxicity of microplastics and nanoplastics: A threat to mammalian fertility in both sexes

He, Y., & Yin, R. (2023) · Journal of Applied Toxicology · doi:10.1002/jat.4510 · Cited by 98 · see citing works

The role of lipotoxicity in kidney disease: From molecular mechanisms to therapeutic prospects

Ren, L., Cui, H., Wang, Y., Ju, F., Cai, Y., Gang, X., & Wang, G. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114465 · Cited by 99 · see citing works

The mitochondrial permeability transition: Nexus of aging, disease and longevity

Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works

Mitophagy in the Pathogenesis of Liver Diseases

Ke, P. (2020) · Cells · doi:10.3390/cells9040831 · Cited by 89 · see citing works

Mitochondria: Potential Targets for Osteoarthritis

Mao, X.-J., Fu, P., Wang, L.-L., & Xiang, C. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.581402 · Cited by 89 · see citing works

The diabetic microenvironment causes mitochondrial oxidative stress in glomerular endothelial cells and pathological crosstalk with podocytes

Casalena, G., Yu, L., Gil, R., Rodriguez, S., Sosa, S., Janssen, W. G. M., Azeloglu, E. U., Leventhal, J. S., & Daehn, I. S. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00605-x · Cited by 91 · see citing works

LDHB inhibition induces mitophagy and facilitates the progression of CSFV infection

Fan, S., Wu, K., Zhao, M., Yuan, J., Ma, S., Zhu, E., Chen, Y., Ding, H., Yi, L., & Chen, J. (2020) · Autophagy · doi:10.1080/15548627.2020.1823123 · Cited by 88 · see citing works

PINK1/Parkin-mediated mitophagy in cardiovascular disease: From pathogenesis to novel therapy

Wu, Y., Jiang, T., Hua, J., Xiong, Z., Dai, K., Chen, H., Li, L., Peng, J., Peng, X., Zheng, Z., et al. (2022) · International Journal of Cardiology · doi:10.1016/j.ijcard.2022.05.025 · Cited by 91 · see citing works

Mitophagy-driven mitochondrial rejuvenation regulates stem cell fate

Vázquez‐Martín, A., den Haute, C. V., Cufí, S., Corominas-Faja, B., Cuyàs, E., López‐Bonet, E., Rodríguez‐Gallego, E., Fernández‐Arroyo, S., Joven, J., Baekelandt, V., et al. (2016) · Aging · doi:10.18632/aging.100976 · Cited by 88 · see citing works

Protein quality control at the mitochondrion

Voos, W., Jaworek, W., Wilkening, A., & Bruderek, M. (2016) · Essays in Biochemistry · doi:10.1042/ebc20160009 · Cited by 88 · see citing works

Bone Marrow-Derived Mesenchymal Stem Cells Ameliorate Sepsis-Induced Acute Kidney Injury by Promoting Mitophagy of Renal Tubular Epithelial Cells via the SIRT1/Parkin Axis

Guo, J. X., Wang, R., & Liu, D. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.639165 · Cited by 89 · see citing works

FUNDC1: A Promising Mitophagy Regulator at the Mitochondria-Associated Membrane for Cardiovascular Diseases

Li, G., Li, J., Shao, R., Zhao, J., & Chen, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.788634 · Cited by 88 · see citing works

Mitochondria in endothelial cells angiogenesis and function: current understanding and future perspectives

Luo, Z., Yao, J., Wang, Z., & Xu, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04286-1 · Cited by 87 · see citing works

GlyNAC (Glycine and N-Acetylcysteine) Supplementation in Mice Increases Length of Life by Correcting Glutathione Deficiency, Oxidative Stress, Mitochondrial Dysfunction, Abnormalities in Mitophagy and Nutrient Sensing, and Genomic Damage

Kumar, P., Osahon, O. W., & Sekhar, R. V. (2022) · Nutrients · doi:10.3390/nu14051114 · Cited by 83 · see citing works

circARF3 Alleviates Mitophagy-Mediated Inflammation by Targeting miR-103/TRAF3 in Mouse Adipose Tissue

Zhang, Z., Zhang, T., Feng, R., Huang, H., Xia, T., & Sun, C. (2018) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2018.11.014 · Cited by 82 · see citing works

PINK1 deficiency impairs osteoblast differentiation through aberrant mitochondrial homeostasis

Lee, S.-Y., An, H., Kim, J. M., Sung, M.-J., Kim, H. K., Kim, H. K., Oh, J., Jeong, H. Y., Lee, Y. H., Yang, T., et al. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02656-4 · Cited by 84 · see citing works

Receptor-mediated mitophagy

Yamaguchi, O., Murakawa, T., Nishida, K., & Otsu, K. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.03.010 · Cited by 84 · see citing works

Quantitative proteomic analysis of Parkin substrates in Drosophila neurons

Martinez, A., Lectez, B. L. P., Ramírez, J., Popp, O., Sutherland, J. D., Urbé, S., Dittmar, G., Clague, M. J., & Mayor, U. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0170-3 · Cited by 83 · see citing works

MIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology

Tang, B. L. (2015) · Cells · doi:10.3390/cells5010001 · Cited by 82 · see citing works

The role of FUNDC1 in mitophagy, mitochondrial dynamics and human diseases

Liu, H., Zang, C., Yuan, F., Ju, C., Shang, M., Ning, J., Yang, Y., Ma, J., Li, G. L., Bao, X., et al. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114891 · Cited by 81 · see citing works

The protective effect of selenoprotein M on non-alcoholic fatty liver disease: the role of the AMPKα1–MFN2 pathway and Parkin mitophagy

Cai, J., Huang, J., Yang, J., Chen, X., Zhang, H., Zhu, Y., Liu, Q., & Zhang, Z. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04385-0 · Cited by 83 · 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

The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation

Yamano, K., Matsuda, N., & Tanaka, K. (2016) · EMBO Reports · doi:10.15252/embr.201541486 · Cited by 239 · see citing works

Ubiquitin signaling in PINK1/Parkin-dependent mitophagy

Okatsu, K., & Fukai, S. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf079 · Cited by 19 · see citing works

PINK1 and Parkin: team players in stress-induced mitophagy

Bader, V., & Winklhofer, K. F. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0135 · Cited by 56 · see citing works

PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: Implications for Parkinson disease pathogenesis

Gegg, M. E., & Schapira, A. H. V. (2011) · Autophagy · doi:10.4161/auto.7.2.14332 · Cited by 106 · see citing works