Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Open accessAbstract
Damage to mitochondria can lead to the depolarization of the inner mitochondrial membrane, thereby sensitizing impaired mitochondria for selective elimination by autophagy. However, fusion of uncoupled mitochondria with polarized mitochondria can compensate for damage, reverse membrane depolarization, and obviate mitophagy. Parkin, an E3 ubiquitin ligase that is mutated in monogenic forms of Parkinson’s disease, was recently found to induce selective autophagy of damaged mitochondria. Here we show that ubiquitination of mitofusins Mfn1 and Mfn2, large GTPases that mediate mitochondrial fusion, is induced by Parkin upon membrane depolarization and leads to their degradation in a proteasome- and p97-dependent manner. p97, a AAA+ ATPase, accumulates on mitochondria upon uncoupling of Parkin-expressing cells, and both p97 and proteasome activity are required for Parkin-mediated mitophagy. After mitochondrial fission upon depolarization, Parkin prevents or delays refusion of mitochondria, likely by the elimination of mitofusins. Inhibition of Drp1-mediated mitochondrial fission, the proteasome, or p97 prevents Parkin-induced mitophagy.
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
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?
p97 provides the driving force to extract Mfn1, Mfn2, and MCL1 from the OMM and chaperone them to the proteasome.
“p97 provides the driving force to extract Mfn1, Mfn2, and the anti-apoptotic protein MCL1 from the OMM and chaperone them to the proteasome [49, 50].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [49]
p97/VCP is critical in the retrotranslocation and degradation of endoplasmic reticulum-associated proteins (ERAD) and mitochondrial proteins (MAD).
“p97/VCP is critical in the retrotranslocation and degradation of endoplasmic reticulum-associated proteins (ERAD) [47] and mitochondrial proteins ( MAD) [49, 50].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [49]
Parkin inhibits refusion after mitochondrial fission upon depolarization by inducing the proteasomal degradation of mitofusins.
“Parkin inhibits refusion after mitochondrial fission upon depolarization by inducing the proteasomal degradation of mitofusins (97).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [97]
Latent Parkin in the cytosol is activated and relocalized to the outer mitochondrial membrane, ubiquitinating mitochondrial proteins such as Mitofusin and Miro.
“Latent Parkin, in the cytosol, is activated and relocalized to the outer mitochondrial membrane, ubiquitinating mitochondrial proteins such as Mitofusin and Miro (Liu et al., 2012, Tanaka et al., 2010, Wang et al., 2011).”
From A Cell-Based High-Throughput Screening Identified Two Compounds that Enhance PINK1-Parkin Signaling (2020) · cites this paper as Tanaka et al., 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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 · 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
Self-citationChronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R., Sherer, T., Mackenzie, G., Garcia-Osuna, M., Panov, A., & Greenamyre, J. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,797 · 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
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 · 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
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 · see citing works
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works
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
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · 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
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558 · see citing works
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 2× · see citing works
“potential, by shuffling materials from healthy to damaged mitochondria (Chen et al., 2005).”
BackgroundOPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
High mobility of proteins in the mammalian cell nucleus
Phair, R. D., & Misteli, T. (2000) · Nature · doi:10.1038/35007077 · Cited by 1,212 · see citing works
Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099 · see citing works
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066 · see citing works
Dagda, R. K., Cherra, S. J., Kulich, S. M., Tandon, A., Park, D., & Chu, C. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808515200 · Cited by 954 · see citing works
Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601184 · Cited by 899 · see citing works
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works
Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J.-W., Yang, L., Beal, M. F., Vogel, H., & Lu, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602493103 · Cited by 798 · see citing works
<i>Drosophila</i> Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735 · see citing works
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works
Role of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625 · see citing works
Self-citationFunction of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol
Ye, Y., Meyer, H. H., & Rapoport, T. A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302169 · Cited by 598 · see citing works
Complex I Is the Major Site of Mitochondrial Superoxide Production by Paraquat
Cochemé, H. M., & Murphy, M. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708597200 · Cited by 563 · see citing works
Rabinovich, E., Kerem, A., Fröhlich, K., Diamant, N., & Bar‐Nun, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.626-634.2002 · Cited by 546 · see citing works
Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, G. A., Vogel, H. S., & Lu, B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711845105 · Cited by 536 · see citing works
Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 517 · see citing works
Loss-of-Function of Human PINK1 Results in Mitochondrial Pathology and Can Be Rescued by Parkin
Exner, N., Treske, B., Paquet, D., Holmström, K. M., Schiesling, C., Gispert, S., Carballo‐Carbajal, I., Berg, D., Hoepken, H.-H., Gasser, T., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0719-07.2007 · Cited by 511 · see citing works
The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 474 · see citing works
Self-citationRegulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
Griparić, L., Kanazawa, T., & van der Bliek, A. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704112 · Cited by 467 · see citing works
The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway
Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440 · see citing works
Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437 · see citing works
Paraquat elicited neurobehavioral syndrome caused by dopaminergic neuron loss
Brooks, A. I., Chadwick, C. A., Gelbard, H. A., Cory‐Slechta, D. A., & Federoff, H. J. (1999) · Brain Research · doi:10.1016/s0006-8993(98)01192-5 · Cited by 425 · see citing works
Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation*
Lutz, A., Exner, N., Fett, M. E., Schlehe, J. S., Kloos, K., Lämmermann, K., Brunner, B., Kurz-Drexler, A., Vogel, F., Reichert, A., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035774 · Cited by 421 · see citing works
Staropoli, J. F., McDermott, C., Martinat, C., Schulman, B. A., Demireva, E. Y., & Abeliovich, A. (2003) · Neuron · doi:10.1016/s0896-6273(03)00084-9 · Cited by 378 · see citing works
Fallon, L., Bélanger, C., Corera, A. T., Kontogiannea, M., Regan‐Klapisz, E., Moreau, F., Voortman, J., Haber, M., Rouleau, G., Thorarinsdottir, T., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1441 · Cited by 357 · see citing works
Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
Büeler, H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.03.006 · Cited by 326 · see citing works
A Genomic Screen for Yeast Mutants Defective in Selective Mitochondria Autophagy
Kanki, T., Wang, K., Baba, M., Bartholomew, C. R., Lynch-Day, M. A., Du, Z., Geng, J., Mao, K., Yang, Z., Yen, W.-L., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0225 · Cited by 266 · see citing works
Nowikovsky, K., Reipert, S., Devenish, R. J., & Schweyen, R. J. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402167 · Cited by 230 · see citing works
Alterations in the common fragile site gene Parkin in ovarian and other cancers
Denison, S. R., Wang, F., Becker, N. A., Schüle, B., Kock, N., Phillips, L. A., Klein, C., & Smith, D. I. (2003) · Oncogene · doi:10.1038/sj.onc.1207072 · Cited by 224 · see citing works
The PINK1–Parkin pathway is involved in the regulation of mitochondrial remodeling process
Park, J., Lee, G., & Chung, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.11.086 · Cited by 181 · see citing works
Diverse Effects of Pathogenic Mutations of Parkin That Catalyze Multiple Monoubiquitylation in Vitro
Matsuda, N., Kitami, T., Suzuki, T., Mizuno, Y., Hattori, N., & Tanaka, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510393200 · Cited by 180 · see citing works
Matton, A., Craig, K. J. T., Beilina, A. G., van der Brug, M., Harwig, M. C., Ahmad, R., Miller, D. W., Zambrano, I., Cowburn, R. F., Behbahani, H., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005701 · Cited by 176 · see citing works
Cohen, M. M., Leboucher, G. P., Livnat‐Levanon, N., Glickman, M. H., & Weissman, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0227 · Cited by 170 · see citing works
Novel Monoclonal Antibodies Demonstrate Biochemical Variation of Brain Parkin with Age
Pawlyk, A. C., Giasson, B. I., Sampathu, D. M., Perez, F. A., Lim, K. L., Dawson, V. L., Dawson, T. M., Palmiter, R. D., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306889200 · Cited by 149 · see citing works
Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8
Krick, R., Bremer, S., Welter, E., Schlotterhose, P., Mühe, Y., Eskelinen, E., & Thumm, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002075 · Cited by 139 · see citing works
Escobar‐Henriques, M., Westermann, B., & Langer, T. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512079 · Cited by 119 · see citing works
Neutzner, A., & Youle, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500807200 · Cited by 89 · see citing works
Self-citationMatsuda, N., & Tanaka, K. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1231 · Cited by 87 · see citing works
Dürr, M., Escobar‐Henriques, M., Merz, S., Geimer, S., Langer, T., & Westermann, B. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-01-0053 · Cited by 73 · see citing works
Outer Mitochondrial Membrane Protein Degradation by the Proteasome
Neutzner, A., Youle, R. J., & Karbowski, M. (2007) · Novartis Foundation symposium · doi:10.1002/9780470725207.ch2 · Cited by 72 · see citing works
Self-citationAmiott, E. A., Cohen, M. M., Saint-Georges, Y., Weissman, A. M., & Shaw, J. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0622 · Cited by 45 · see citing works
Protein degradation in Parkinson disease revisited: it’s complex
Li, H., & Guo, M. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38619 · Cited by 25 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,467 · see citing works
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Guidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Self-citationMitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Self-citationThe Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978 · see citing works
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
The 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 · see citing works
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 · see citing works
Self-citationThe pathways of mitophagy for quality control and clearance of mitochondria
Ashrafi, G., & Schwarz, T. L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.81 · Cited by 1,900 · see citing works
Synaptic Energy Use and Supply
Harris, J. J., Jolivet, R., & Attwell, D. (2012) · Neuron · doi:10.1016/j.neuron.2012.08.019 · Cited by 1,747 · see citing works
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803 · see citing works
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735 · see citing works
Mechanisms 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 1,505 · see citing works
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416 · see citing works
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works
Molecular mechanisms and physiological functions of mitophagy
Onishi, M., Yamano, K., Sato, M., Matsuda, N., & Okamoto, K. (2021) · The EMBO Journal · doi:10.15252/embj.2020104705 · Cited by 1,429 · see citing works
Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure
Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341 · 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
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
Self-citationMitochondria and the Autophagy–Inflammation–Cell Death Axis in Organismal Aging
Green, D. R., Galluzzi, L., & Kroemer, G. (2011) · Science · doi:10.1126/science.1201940 · Cited by 1,245 · see citing works
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · see citing works
Proteasomal and Autophagic Degradation Systems
Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,165 · see citing works
Mitochondrial Dynamics — Mitochondrial Fission and Fusion in Human Diseases
Archer, S. L. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1215233 · Cited by 1,103 · 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
Mitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032 · 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
The mechanisms and roles of selective autophagy in mammals
Vargas, J. N. S., Hamasaki, M., Kawabata, T., Youle, R. J., & Yoshimori, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00542-2 · Cited by 1,030 · see citing works
Self-citationBroad 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 · see citing works
The mitophagy pathway and its implications in human diseases
Wang, S., Long, H., Hou, L., Feng, B., Ma, Z., Wu, Y., Zeng, Y., Cai, J., Zhang, D., & Zhao, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01503-7 · Cited by 938 · see citing works
Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration
Sheng, Z., & Cai, Q. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3156 · Cited by 906 · see citing works
Mechanisms of Mitochondrial Fission and FusionPreprint
van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 861 · see citing works
Mitochondrial Cristae: Where Beauty Meets Functionality
Cogliati, S., Enriquez, J. A., & Scorrano, L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.01.001 · Cited by 816 · see citing works
A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
Sugiura, A., McLelland, G., Fon, E. A., & McBride, H. M. (2014) · The EMBO Journal · doi:10.15252/embj.201488104 · Cited by 862 · see citing works
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812 · see citing works
Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
Meyer, H. H., Bug, M., & Bremer, S. (2012) · Nature Cell Biology · doi:10.1038/ncb2407 · Cited by 803 · see citing works
Ubiquitination and selective autophagy
Shaid, S., Brandts, C. H., Serve, H., & Dikic, I. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.72 · Cited by 800 · see citing works
Kubli, D. A., & Gustafsson, Å. B. (2012) · Circulation Research · doi:10.1161/circresaha.112.265819 · Cited by 792 · see citing works
The Interplay Between Mitochondrial Dynamics and Mitophagy
Twig, G., & Shirihai, O. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3779 · Cited by 778 · see citing works
Jiang, P., & Mizushima, N. (2013) · Cell Research · doi:10.1038/cr.2013.161 · Cited by 767 · 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
Ubiquitin-Dependent And Independent Signals In Selective Autophagy
Khaminets, A., Behl, C., & Đikić, I. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.010 · Cited by 716 · see citing works
Exner, N., Lutz, A. K., Haass, C., & Winklhofer, K. F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.170 · Cited by 652 · see citing works
PINK1- and Parkin-mediated mitophagy at a glance
Jin, S. M., & Youle, R. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.093849 · Cited by 631 · see citing works
Self-citationMitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 625 · see citing works
Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612 · see citing works
What Genetics Tells us About the Causes and Mechanisms of Parkinson's Disease
Corti, O., Lesage, S., & Brice, A. (2011) · Physiological Reviews · doi:10.1152/physrev.00022.2010 · Cited by 610 · see citing works
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
Mitophagy, Mitochondrial Homeostasis, and Cell Fate
Ma, K., Chen, G., Li, W., Kepp, O., Zhu, Y., & Chen, Q. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00467 · Cited by 609 · see citing works
Understanding Dopaminergic Cell Death Pathways in Parkinson Disease
Michel, P. P., Hirsch, É. C., & Hunot, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.038 · Cited by 594 · see citing works
Autophagy balances inflammation in innate immunity
Deretic, V., & Levine, B. (2018) · Autophagy · doi:10.1080/15548627.2017.1402992 · Cited by 563 · see citing works
Endogenous Drp1 Mediates Mitochondrial Autophagy and Protects the Heart Against Energy Stress
Ikeda, Y., Shirakabe, A., Maejima, Y., Zhai, P., Sciarretta, S., Toli, J., Nomura, M., Mihara, K., Egashira, K., Ohishi, M., et al. (2015) · Circulation Research · doi:10.1161/circresaha.116.303356 · Cited by 571 · see citing works
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
The role of mitochondria in amyotrophic lateral sclerosis
Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.052 · Cited by 556 · see citing works
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 · see citing works
Mitochondrial Trafficking in Neurons
Schwarz, T. L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011304 · Cited by 525 · see citing works
The role of PINK1–Parkin in mitochondrial quality control
Narendra, D. P., & Youle, R. J. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01513-9 · Cited by 580 · see citing works
Self-citationLoss of iron triggers PINK1/Parkin‐independent mitophagy
Allen, G. F. G., Toth, R. L., James, J. L., & Ganley, I. G. (2013) · EMBO Reports · doi:10.1038/embor.2013.168 · Cited by 540 · see citing works
Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment
Golpich, M., Amini, E., Mohamed, Z., Raymond, A. A., Ibrahim, N. M., & Ahmadiani, A. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12655 · Cited by 540 · see citing works
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
Mitochondria: The Next (Neurode)Generation
Schon, E. A., & Przedborski, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.003 · Cited by 568 · see citing works
Emerging views of mitophagy in immunity and autoimmune diseases
Xu, Y., Shen, J., & Ran, Z. (2019) · Autophagy · doi:10.1080/15548627.2019.1603547 · Cited by 521 · see citing works
Ge, P., Dawson, V. L., & Dawson, T. M. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00367-7 · Cited by 514 · see citing works
A pathway coordinated by DELE1 relays mitochondrial stress to the cytosol
Fessler, E., Eckl, E.-M., Schmitt, S., Mancilla, I. A., Meyer-Bender, M., Hanf, M., Philippou‐Massier, J., Krebs, S., Zischka, H., & Jae, L. T. (2020) · Nature · doi:10.1038/s41586-020-2076-4 · Cited by 514 · see citing works
Zhang, X., Yan, H., Yuan, Y., Gao, J., Shen, Z., Cheng, Y., Shen, Y., Wang, R.-R., Wang, X., Hu, W.-W., et al. (2013) · Autophagy · doi:10.4161/auto.25132 · Cited by 510 · see citing works
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 490 · see citing works
Amm, I., Sommer, T., & Wolf, D. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493 · see citing works
Integration of cellular bioenergetics with mitochondrial quality control and autophagy
Hill, B. G., Benavides, G. A., Lancaster, J. R., Ballinger, S. W., Dell’Italia, L., Zhang, J., & Darley-Usmar, V. M. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0198 · Cited by 481 · see citing works
Quality control of the mitochondrial proteome
Song, J., Herrmann, J. M., & Becker, T. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00300-2 · Cited by 492 · see citing works
New insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 476 · see citing works
Mitochondrial fission facilitates the selective mitophagy of protein aggregates
Burman, J. L., Pickles, S., Wang, C., Sekine, S., Vargas, J. N. S., Zhang, Z., Youle, A. M., Nezich, C. L., Wu, X., Hammer, J. A., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612106 · Cited by 479 · see citing works
Self-citationMitochondria and cell signalling
Tait, S. W. G., & Green, D. R. (2012) · Journal of Cell Science · doi:10.1242/jcs.099234 · Cited by 453 · see citing works
Kubli, D. A., Zhang, X., Lee, Y., Hanna, R. A., Quinsay, M. N., Nguyen, C. K., Jimenez, R., Petrosyan, S., Murphy, A. N., & Gustafsson, Å. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411363 · Cited by 476 · see citing works
Mitochondrial dysfunction and oxidative stress in Parkinson's disease and monogenic parkinsonism
Hauser, D. N., & Hastings, T. G. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.10.011 · Cited by 470 · see citing works
Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy
Vargas, J. N. S., Wang, C., Bunker, E. N., Hao, L., Maric, D., Schiavo, G., Randow, F., & Youle, R. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.010 · Cited by 469 · see citing works
Self-citationMitochondrial dynamics in neurodegeneration
Itoh, K., Nakamura, K., Iijima, M., & Sesaki, H. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.006 · Cited by 464 · see citing works
Mitophagy in degenerative joint diseases
Sun, K., Jing, X., Guo, J., Yao, X., & Guo, F. (2020) · Autophagy · doi:10.1080/15548627.2020.1822097 · Cited by 464 · see citing works
Hsieh, C.-H., Shaltouki, A., Gonzalez, A. E., da Cruz, A. B., Burbulla, L. F., Lawrence, E. S., Schüle, B., Krainc, D., Palmer, T. D., & Wang, X. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.08.002 · Cited by 459 · see citing works
Quality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 453 · see citing works
A Molecular Approach to Mitophagy and Mitochondrial Dynamics.
Yoo, S., & Jung, Y. (2018) · PubMed Central · doi:10.14348/molcells.2018.2277 · Cited by 447 · see citing works
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
The VCP/p97 system at a glance: connecting cellular function to disease pathogenesis
Meyer, H. H., & Weihl, C. C. (2014) · Journal of Cell Science · doi:10.1242/jcs.093831 · Cited by 423 · see citing works
Metformin Improves Mitochondrial Respiratory Activity through Activation of AMPK
Wang, Y., An, H., Liu, T., Qin, C., Sesaki, H., Guo, S., Radovick, S., Hussain, M., Maheshwari, A., Wondisford, F. E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.070 · Cited by 432 · see citing works
Parkin‐independent mitophagy requires Drp1 and maintains the integrity of mammalian heart and brain
Kageyama, Y., Hoshijima, M., Seo, K., Bedja, D., Sysa‐Shah, P., Andrabi, S. A., Chen, W., Höke, A., Dawson, V. L., Dawson, T. M., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488658 · Cited by 420 · see citing works
Mitochondria: from cell death executioners to regulators of cell differentiation
Kasahara, A., & Scorrano, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.005 · Cited by 420 · see citing works
VCP/p97-Mediated Unfolding as a Principle in Protein Homeostasis and Signaling
van den Boom, J., & Meyer, H. H. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.028 · Cited by 408 · see citing works
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 · see citing works
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 388 · see citing works
RALA and RALBP1 regulate mitochondrial fission at mitosis
Kashatus, D. F., Lim, K.-H., Brady, D. C., Pershing, N. L. K., Cox, A. D., & Counter, C. M. (2011) · Nature Cell Biology · doi:10.1038/ncb2310 · Cited by 380 · see citing works
McLelland, G., Goiran, T., Yi, W., Dorval, G., Chen, C. X., Lauinger, N. D., Krahn, A. I., Valimehr, S., Raković, A., Rouiller, I., et al. (2018) · eLife · doi:10.7554/elife.32866 · Cited by 386 · see citing works
Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · 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
Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002537 · Cited by 371 · see citing works
Mitophagy: An Emerging Role in Aging and Age-Associated Diseases
Chen, G., Kroemer, G., & Kepp, O. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00200 · Cited by 359 · see citing works
The spatial and temporal organization of ubiquitin networks
Grabbe, C., Husnjak, K., & Đikić, I. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3099 · Cited by 368 · see citing works
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363 · see citing works
Mitofusin 2: from functions to disease
Filadi, R., Pendin, D., & Pizzo, P. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0023-6 · Cited by 359 · see citing works
- Authors
- Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892 1
- University of Maryland, Baltimore (US)
- Corresponding author
- Karbowski, Mariusz
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2010-12-20
- Volume
- 191
- Issue
- 7
- Pages
- 1367-1380
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3010068
- OpenAlex
- W2104412320
- Cited by
- 1,369
- References
- 57
- Citations by year
- 2026: 48 · 2025: 58 · 2024: 68 · 2023: 68 · 2022: 84 · 2021: 108 · 2020: 111 · 2019: 101 · 2018: 78 · 2017: 85 · 2016: 99 · 2015: 85 · 2014: 111 · 2013: 110 · 2012: 97
- FWCI
- 60.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Japan Society for the Promotion of Science
- National Institute of General Medical Sciences (R01GM083131)
- National Institute of Neurological Disorders and Stroke
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- mitophagy, Parkin, mitofusins, Mfn1, mitofusin 2, proteasome, VCP, AAA+ ATPase, mitochondrial fusion, mitochondrial fission, Drp1, mitochondrial depolarization, ubiquitination, selective autophagy, Parkinson's disease, ubiquitin-proteasome system
- MeSH terms
- PTEN-Induced Putative Kinase, Adenosine Triphosphatases, Animals, Autophagy, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Fibroblasts, HeLa Cells, Humans, Leupeptins, Membrane Fusion, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Models, Biological, Nuclear Proteins, Protein Binding, Protein Kinases, Mice, Knockout, GTP Phosphohydrolases, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Dynamins, RNA, Small Interfering, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, HCT116 Cells, Cell Line, Tumor, Proteasome Endopeptidase Complex, Mice, Membrane Potential, Mitochondrial, Ubiquitination, Proteasome Inhibitors
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
