The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy
Open accessAbstract
An increasing body of evidence points to mitochondrial dysfunction as a contributor to the molecular pathogenesis of neurodegenerative diseases such as Parkinson's disease. Recent studies of the Parkinson's disease associated genes PINK1 (ref. 2) and parkin (PARK2, ref. 3) indicate that they may act in a quality control pathway preventing the accumulation of dysfunctional mitochondria. Here we elucidate regulators that have an impact on parkin translocation to damaged mitochondria with genome-wide small interfering RNA (siRNA) screens coupled to high-content microscopy. Screening yielded gene candidates involved in diverse cellular processes that were subsequently validated in low-throughput assays. This led to characterization of TOMM7 as essential for stabilizing PINK1 on the outer mitochondrial membrane following mitochondrial damage. We also discovered that HSPA1L (HSP70 family member) and BAG4 have mutually opposing roles in the regulation of parkin translocation. The screens revealed that SIAH3, found to localize to mitochondria, inhibits PINK1 accumulation after mitochondrial insult, reducing parkin translocation. Overall, our screens provide a rich resource to understand mitochondrial quality control.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Multiple genome-wide siRNA/CRISPR-Cas9 screens have already identified mitophagy genes although with little overlap between studies [15–18].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [16]
Experimental — accuracy not yet measured
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
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
Self-citationHereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
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
Self-citationPINK1/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
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
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
Self-citationLandscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Sarraf, S. A., Raman, M., Guarani-Pereira, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,010
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993
Widespread siRNA “off-target” transcript silencing mediated by seed region sequence complementarity
Jackson, A. L., Burchard, J., Schelter, J. M., Chau, B. N., Cleary, M. A., Lim, L. P., & Linsley, P. S. (2006) · RNA · doi:10.1261/rna.25706 · Cited by 979
Cited by
Sorted by citations
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
Self-citationThe Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
Pickrell, A. M., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.007 · Cited by 2,310
Self-citationMitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
Self-citationMechanisms of mitophagy in cellular homeostasis, physiology and pathology
Palikaras, K., Lionaki, E., & Tavernarakis, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0176-2 · Cited by 1,556
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
Self-citationGenome-scale CRISPR-Cas9 Knockout and Transcriptional Activation Screening
Joung, J., Konermann, S., Gootenberg, J. S., Abudayyeh, O. O., Platt, R. J., Brigham, M. D., Sanjana, N. E., & Zhang, F. (2017) · Nature Protocols · doi:10.1038/nprot.2017.016 · Cited by 1,243
High-throughput functional genomics using CRISPR-Cas9
Shalem, O., Sanjana, N. E., & Zhang, F. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3899 · Cited by 1,233
Mitochondrial dynamics and mitochondrial quality control
Ni, H.-M., Williams, J. A., & Ding, W.-X. (2015) · Redox Biology · doi:10.1016/j.redox.2014.11.006 · Cited by 931
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 758
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 718
Wang, Y., Bryant, S. H., Cheng, T., Wang, J., Gindulytė, A., Shoemaker, B. A., Thiessen, P. A., He, S., & Zhang, J. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1118 · Cited by 675
PINK1/Parkin-mediated mitophagy in mammalian cells
Eiyama, A., & Okamoto, K. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.01.002 · Cited by 603
MitoFates: Improved Prediction of Mitochondrial Targeting Sequences and Their Cleavage Sites*
Fukasawa, Y., Tsuji, J., Fu, S.-C., Tomii, K., Horton, P., & Imai, K. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.043083 · Cited by 573
The Role of Autophagy in the Heart
Sciarretta, S., Maejima, Y., Zablocki, D., & Sadoshima, J. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021317-121427 · Cited by 547
Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System
Kocatürk, N. M., & Gözüaçık, D. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00128 · Cited by 442
PHB2 (prohibitin 2) promotes PINK1-PRKN/Parkin-dependent mitophagy by the PARL-PGAM5-PINK1 axis
Yan, C., Gong, L., Chen, L., Xu, M., Hamdan, H. A., Tang, M., Désaubry, L., & Song, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1628520 · Cited by 431
The three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications
Durcan, T. M., & Fon, E. A. (2015) · Genes & Development · doi:10.1101/gad.262758.115 · Cited by 400
AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1
Strappazzon, F., Nazio, F., Corrado, M., Cianfanelli, V, Romagnoli, A., Fimia, G. M., Campello, S., Nardacci, R., Piacentini, M., Campanella, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.139 · Cited by 399
Parkin and PINK1: much more than mitophagy
Scarffe, L. A., Stevens, D. A., Dawson, V. L., & Dawson, T. M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.004 · Cited by 392
PINK1/Parkin-mediated mitophagy in neurodegenerative diseases
Li, J., Yang, D., Li, Z., Zhao, M., Wang, D., Sun, Z., Wen, P., Dai, Y., Gou, F., Ji, Y., et al. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101817 · Cited by 406
Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
Bingol, B., & Sheng, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.015 · Cited by 340
USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria
Cunningham, C. N., Baughman, J. M., Phu, L., Tea, J. S., Yu, C., Coons, M. M., Kirkpatrick, D. S., Bingol, B., & Corn, J. E. (2015) · Nature Cell Biology · doi:10.1038/ncb3097 · Cited by 344
PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol
Sekine, S., & Youle, R. J. (2018) · BMC Biology · doi:10.1186/s12915-017-0470-7 · Cited by 320
Self-citationRegulation 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 310
Mitochondrial quality control in health and in Parkinson’s disease
Eldeeb, M. A., Thomas, R. A., Ragheb, M. A., Fallahi, A., & Fon, E. A. (2022) · Physiological Reviews · doi:10.1152/physrev.00041.2021 · Cited by 281
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 272
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 253
Self-citationThe ADP/ATP translocase drives mitophagy independent of nucleotide exchange
Hoshino, A., Wang, W.-J., Wada, S., McDermott-Roe, C., Evans, C. S., Gosis, B., Morley, M. P., Rathi, K. S., Li, J., Li, K., et al. (2019) · Nature · doi:10.1038/s41586-019-1667-4 · Cited by 228
Organellophagy: Eliminating cellular building blocks via selective autophagy
Okamoto, K. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201402054 · Cited by 225
Macdonald, R., Barnes, K., Hastings, C., & Mortiboys, H. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170501 · Cited by 223
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 217
Gan, Z. Y., Callegari, S., Cobbold, S. A., Cotton, T. R., Mlodzianoski, M. J., Schubert, A. F., Geoghegan, N. D., Rogers, K. L., Leis, A. P., Dewson, G., et al. (2021) · Nature · doi:10.1038/s41586-021-04340-2 · Cited by 212
Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy
Yamano, K., Kikuchi, R., Kojima, W., Hayashida, R., Koyano, F., Kawawaki, J., Shoda, T., Demizu, Y., Naito, M., Tanaka, K., et al. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201912144 · Cited by 205
Self-citationThe multifaceted regulation of mitophagy by endogenous metabolites
Zhang, T., Liu, Q., Gao, W., Sehgal, S. A., & Wu, H. (2021) · Autophagy · doi:10.1080/15548627.2021.1975914 · Cited by 209
Truban, D., Hou, X., Caulfield, T. R., Fiesel, F. C., & Springer, W. (2016) · Journal of Parkinson’s Disease · doi:10.3233/jpd-160989 · Cited by 237
Mitochondrial proteostasis in the context of cellular and organismal health and aging
Moehle, E. A., Shen, K., & Dillin, A. G. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000893 · Cited by 200
Autophagy Assays for Biological Discovery and Therapeutic Development
Mizushima, N., & Murphy, L. O. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.07.006 · Cited by 197
The Mitochondrial Dynamism-Mitophagy-Cell Death Interactome
Dorn, G. W., & Kitsis, R. N. (2014) · Circulation Research · doi:10.1161/circresaha.116.303554 · Cited by 193
Pink1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy
Pryde, K. R., Smith, H. L., Chau, K.-Y., & Schapira, A. H. V. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201509003 · Cited by 185
Visualizing and Modulating Mitophagy for Therapeutic Studies of Neurodegeneration
Katayama, H., Hama, H., Nagasawa, K., Kurokawa, H., Sugiyama, M., Ando, R., Funata, M., Yoshida, N., Homma, M., Nishimura, T., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.025 · Cited by 185
Genetics and genomics of Parkinson’s disease
Lin, M. K., & Farrer, M. J. (2014) · Genome Medicine · doi:10.1186/gm566 · Cited by 183
Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1
Sekine, S., Wang, C., Sideris, D. P., Bunker, E. N., Zhang, Z., & Youle, R. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.002 · Cited by 160
Self-citationMitochondrial pathology: stress signals from the energy factory
Raimundo, N. (2014) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2014.01.005 · Cited by 165
Guo, S., Liang, Y., Murphy, S. F., Huang, A., Shen, H., Kelly, D. F., Sobrado, P., & Sheng, Z. (2015) · Autophagy · doi:10.1080/15548627.2015.1017181 · Cited by 148
Mohanty, A., Tiwari-Pandey, R., & Pandey, N. R. (2019) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-019-00507-9 · Cited by 164
Leonard, A. P., Cameron, R. B., Speiser, J. L., Wolf, B. J., Peterson, Y. K., Schnellmann, R. G., Beeson, C. C., & Rohrer, B. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.002 · Cited by 150
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 153
Wilson, E. L., & Metzakopian, E. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00705-8 · Cited by 158
Li, J., Zhu, S., Kozono, D., Ng, K., Futalan, D., Shen, Y. H., Akers, J. C., Steed, T., Kushwaha, D. S., Schlabach, M. R., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.1801 · Cited by 147
AMPK protects against alcohol-induced liver injury through UQCRC2 to up-regulate mitophagy
Lü, X., Xuan, W., Li, J., Yao, H., Huang, C., & Li, J. (2021) · Autophagy · doi:10.1080/15548627.2021.1886829 · Cited by 143
Self-citationROCK inhibitors upregulate the neuroprotective Parkin-mediated mitophagy pathway
Moskal, N., Riccio, V., Bashkurov, M., Taddese, R., Datti, A., Lewis, P. N., & Angus McQuibban, G. (2020) · Nature Communications · doi:10.1038/s41467-019-13781-3 · Cited by 142
Feng, S., Wang, Z., Yuan, Y., Wang, X., Sun, H., Chen, N., & Zhang, Y. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104553 · Cited by 146
Autophagy in neurodegeneration: New insights underpinning therapy for neurological diseases
Corti, O., Blomgren, K., Poletti, A., & Beart, P. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15002 · Cited by 141
PINK1 Is a Negative Regulator of Growth and the Warburg Effect in Glioblastoma
Agnihotri, S., Golbourn, B. J., Huang, X., Remke, M., Younger, S. H., Cairns, R. A., Chalil, A., Smith, C. A., Krumholtz, S.-L., Mackenzie, D., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3079 · Cited by 142
Madhu, V., Boneski, P. K., Silagi, E. S., Qiu, Y., Kurland, I. J., Guntur, A. R., Shapiro, I. M., & Risbud, M. V. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4019 · Cited by 137
Mitochondrial genome maintenance in health and disease
Copeland, W. C., & Longley, M. J. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.03.010 · Cited by 147
Mitophagy mechanisms and role in human diseases
Redmann, M., Dodson, M. B., Boyer‐Guittaut, M., Darley-Usmar, V. M., & Zhang, J. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.010 · Cited by 138
Zhang, J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.003 · Cited by 141
Okatsu, K., Kimura, M., Oka, T., Tanaka, K., & Matsuda, N. (2015) · Journal of Cell Science · doi:10.1242/jcs.161000 · Cited by 133
Miller, S., & Muqit, M. M. K. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.029 · Cited by 133
Xie, X., Yang, Y., Wang, Q., Liu, H.-F., Fang, X., Li, C., Jiang, Y., Wang, S., Zhao, H., Miao, J., et al. (2023) · Cell Research · doi:10.1038/s41422-022-00766-z · Cited by 130
Defects in calcium homeostasis and mitochondria can be reversed in Pompe disease
Lim, J., Li, L., Kakhlon, O., Myerowitz, R., & Raben, N. (2015) · Autophagy · doi:10.1080/15548627.2015.1009779 · Cited by 131
Khurana, V., Peng, J., Chung, C. Y., Auluck, P. K., Fanning, S., Tardiff, D. F., Bartels, T., Koeva, M., Eichhorn, S. W., Benyamini, H., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2016.12.011 · Cited by 121
Hypoxia Activation of Mitophagy and Its Role in Disease Pathogenesis
Wu, H., & Chen, Q. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6204 · Cited by 119
Mitophagy for cardioprotection
Titus, A. S., Sung, E., Zablocki, D., & Sadoshima, J. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01009-x · Cited by 128
Palmer, C. S., Anderson, A. J., & Stojanovski, D. (2020) · FEBS Letters · doi:10.1002/1873-3468.14022 · Cited by 126
Iron loss triggers mitophagy through induction of mitochondrial ferritin
Hara, Y., Yanatori, I., Tanaka, A., Kishi, F., Lemasters, J. J., Nishina, S., Sasaki, K., & Hino, K. (2020) · EMBO Reports · doi:10.15252/embr.202050202 · Cited by 117
BRCA1 and S phase DNA repair pathways restrict LINE-1 retrotransposition in human cells
Mita, P., Sun, X., Fenyö, D., Kahler, D. J., Li, D., Agmon, N., Wudzinska, A., Keegan, S., Bader, J. S., Yun, C., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0374-z · Cited by 113
Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex
Rasool, S., Veyron, S., Soya, N., Eldeeb, M. A., Lukács, G. L., Fon, E. A., & Trempe, J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.012 · Cited by 116
Meißner, C., Lorenz, H., Hehn, B., & Lemberg, M. K. (2015) · Autophagy · doi:10.1080/15548627.2015.1063763 · Cited by 117
PINK1 deficiency sustains cell proliferation by reprogramming glucose metabolism through HIF1
Requejo-Aguilar, R., López-Fabuel, I., Fernández, E., Martins, L. M., Almeida, Á., & Bolaños, J. P. (2014) · Nature Communications · doi:10.1038/ncomms5514 · Cited by 114
Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond
Bayne, A. N., & Trempe, J. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03203-4 · Cited by 121
Henstridge, D. C., Whitham, M., & Febbraio, M. A. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.08.003 · Cited by 112
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 109
High-Throughput Imaging for the Discovery of Cellular Mechanisms of Disease
Pegoraro, G., & Misteli, T. (2017) · Trends in Genetics · doi:10.1016/j.tig.2017.06.005 · Cited by 106
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 106
Mitophagy in Cardiovascular Diseases
Morciano, G., Patergnani, S., Bonora, M., Pedriali, G., Tarocco, A., Bouhamida, E., Marchi, S., Ancora, G., Anania, G., Wieckowski, M. R., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030892 · Cited by 110
The role of mitochondrial dynamics in oocyte and early embryo development
Yildirim, R. M., & Seli, E. U. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.01.007 · Cited by 109
Mitochondrial protein translocases for survival and wellbeing
Sokòl, A. M., Sztolsztener, M. E., Wasilewski, M., Heinz, E., & Chacińska, A. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.028 · Cited by 108
Potting, C., Crochemore, C., Moretti, F., Nigsch, F., Schmidt, I., Manneville, C., Carbone, W., Knehr, J., DeJesus, R., Lindeman, A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711023115 · Cited by 93
Madhu, V., Hernandez-Meadows, M., Boneski, P. K., Qiu, Y., Guntur, A. R., Kurland, I. J., Barve, R. A., & Risbud, M. V. (2023) · Autophagy · doi:10.1080/15548627.2022.2162245 · Cited by 97
The mitochondrial kinase PINK 1: functions beyond mitophagy
Voigt, A., Berlemann, L. A., & Winklhofer, K. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13655 · Cited by 100
Lee, J. H., Yoon, Y. M., Song, K., Noh, H., & Lee, S. H. (2020) · Aging Cell · doi:10.1111/acel.13111 · Cited by 97
Cherok, E., Xu, S., Li, S., Das, S., Meltzer, W. A., Zalzman, M., Wang, C., & Karbowski, M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-04-0208 · Cited by 94
Self-citationPellegrino, M. W., & Haynes, C. M. (2015) · BMC Biology · doi:10.1186/s12915-015-0129-1 · Cited by 99
A novel role of KEAP1/PGAM5 complex: ROS sensor for inducing mitophagy
Zeb, A., Choubey, V., Gupta, R., Kuum, M., Safiulina, D., Vaarmann, A., Gogichaishvili, N., Liiv, M., Ilves, I., Tämm, K., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102186 · Cited by 91
Keeping the immune system in check: a role for mitophagy
Lazarou, M. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.75 · Cited by 92
Protein trafficking at the crossroads to mitochondria
Wasilewski, M., Chojnacka, K., & Chacińska, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.019 · Cited by 95
Ito, H., Tanaka, S., Akiyama, Y., Shimada, S., Adikrisna, R., Matsumura, S., Aihara, A., Mitsunori, Y., Ban, D., Ochiai, T., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146564 · Cited by 82
Dynamic changes of muscle insulin sensitivity after metabolic surgery
Gancheva, S., Ouni, M., Jeleník, T., Koliaki, C. C., Szendroedi, J., Toledo, F. G. S., Markgraf, D. F., Pesta, D. H., Mastrototaro, L., Filippo, E. D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12081-0 · Cited by 78
Selective autophagy as a therapeutic target for neurological diseases
Xu, W., Ocak, U., Gao, L., Tu, S., Lenahan, C., Zhang, J., & Shao, A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03667-9 · Cited by 84
Heman-Ackah, S. M., Bassett, A. R., & Wood, M. J. A. (2016) · Scientific Reports · doi:10.1038/srep28420 · Cited by 77
Self-citationEldeeb, M. A., Bayne, A. N., Fallahi, A., Goiran, T., MacDougall, E. J., Soumbasis, A., Zorca, C. E., Jones-Tabah, J., Thomas, R. A., Karpilovsky, N. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313540121 · Cited by 81
Application guide for omics approaches to cell signaling
Yao, Z., Petschnigg, J., Ketteler, R., & Štagljar, I. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1809 · Cited by 77
Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75
PubChem applications in drug discovery: a bibliometric analysis
Cheng, T., Pan, Y., Hao, M., Wang, Y., & Bryant, S. H. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.08.008 · Cited by 74
PTENα regulates mitophagy and maintains mitochondrial quality control
Li, G., Yang, J., Yang, C., Zhu, M., Jin, Y., McNutt, M. A., & Yin, Y. (2018) · Autophagy · doi:10.1080/15548627.2018.1489477 · Cited by 77
Heo, J., Harper, N. J., Paulo, J. A., Li, M. Z., Xu, Q., Coughlin, M. L., Elledge, S. J., & Harper, J. W. (2019) · Science Advances · doi:10.1126/sciadv.aay4624 · Cited by 76
Toward stem cell-based phenotypic screens for neurodegenerative diseases
Khurana, V., Tardiff, D. F., Chung, C. Y., & Lindquist, S. L. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.79 · Cited by 72
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
Metadata
- Authors
- 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., Martin, S. E., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Youle, Richard J.
- ORCID
- Venue
- Nature
- Published
- 2013-11-24
- Volume
- 504
- Issue
- 7479
- Pages
- 291-295
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5841086
- OpenAlex
- W2091264505
- Cited by
- 365
- References
- 30
- Citations by year
- 2026: 15 · 2025: 19 · 2024: 25 · 2023: 16 · 2022: 27 · 2021: 36 · 2020: 32 · 2019: 38 · 2018: 27 · 2017: 27 · 2016: 31 · 2015: 36 · 2014: 36
- FWCI
- 21.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, public-domain)
- Funders
- National Institutes of Health (Z99 NS999999)
- National Institute of General Medical Sciences
- National Institute of Neurological Disorders and Stroke
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- mitophagy, Parkin, PINK1, mitochondrial quality control, HSPA1L, mitochondrial outer membrane, Parkinson's disease, mitochondrial dysfunction, autophagy, ubiquitin ligase
- MeSH terms
- Mitochondrial Precursor Protein Import Complex Proteins, PTEN-Induced Putative Kinase, Multigene Family, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Parkinson Disease, Protein Kinases, Reproducibility of Results, Genome, Human, HSP70 Heat-Shock Proteins, Protein Transport, Mitochondrial Proteins, RNA Interference, RNA, Small Interfering, Ubiquitin-Protein Ligases, HCT116 Cells, Adaptor Proteins, Signal Transducing, Mitochondrial Membranes, HEK293 Cells, 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