Quality control of the mitochondrion

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

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

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

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

Mechanism and medical implications of mammalian autophagy

Dikic, I., & Elazar, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0003-4 · Cited by 2,771

Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development

Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601

Mitofusin 2 tethers endoplasmic reticulum to mitochondria

de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442

ER Tubules Mark Sites of Mitochondrial Division

Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072

Nanotubular Highways for Intercellular Organelle Transport

Rustom, A., Saffrich, R., Markovic, I., Walther, P., & Gerdes, H.-H. (2004) · Science · doi:10.1126/science.1093133 · Cited by 2,038

The multifaceted contributions of mitochondria to cellular metabolism

Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935

Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells

Smirnova, E., Griparic, L., Shurland, D.-L., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,933

MitoCarta3.0: an updated mitochondrial proteome now with sub-organelle localization and pathway annotations

Rath, S., Sharma, R., Gupta, R., Ast, T., Chan, C., Durham, T. J., Goodman, R. P., Grabarek, Z., Haas, M. E., Hung, W. H. W., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1011 · Cited by 1,888

The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis

Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755

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

Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells

Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,684

Autophagosomes form at ER–mitochondria contact sites

Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683

OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion

Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673

The integrated stress response: From mechanism to disease

Costa-Mattioli, M., & Walter, P. (2020) · Science · doi:10.1126/science.aat5314 · Cited by 1,617

Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A

Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550

Hypoxia-Induced Autophagy Is Mediated through Hypoxia-Inducible Factor Induction of BNIP3 and BNIP3L via Their BH3 Domains

Bellot, G., Garcia-Medina, R., Gounon, P., Chiche, J., Roux, D., Pouysségur, J., & Mazure, N. M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00166-09 · Cited by 1,501

Translocation of Proteins into Mitochondria

Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,481

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 1,472

Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy

Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446

Transfer of mitochondria from astrocytes to neurons after stroke

Hayakawa, K., Esposito, E., Wang, X., Terasaki, Y., Liu, Y., Xing, C., Ji, X., & Lo, E. H. (2016) · Nature · doi:10.1038/nature18928 · Cited by 1,423

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

Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin

Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369

Selective Mitochondrial Autophagy, or Mitophagy, as a Targeted Defense Against Oxidative Stress, Mitochondrial Dysfunction, and Aging

Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,340

PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria

Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323

OPA1 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

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

Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission

Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235

Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations

Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211

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

Essential role for Nix in autophagic maturation of erythroid cells

Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185

Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis

Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168

Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation

Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott-Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,156

ExoCarta 2012: database of exosomal proteins, RNA and lipids

Mathivanan, S., Fahner, C. J., Reid, G. E., & Simpson, R. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr828 · Cited by 1,094

AMP-activated protein kinase mediates mitochondrial fission in response to energy stress

Toyama, E. Q., Herzig, S., Courchet, J., Lewis, T. L., Losón, O. C., Hellberg, K., Young, N. P., Chen, H., Polleux, F., Chan, D. C., et al. (2016) · Science · doi:10.1126/science.aab4138 · Cited by 1,085

Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells

Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083

Mitochondrial Import Efficiency of ATFS-1 Regulates Mitochondrial UPR Activation

Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M., & Haynes, C. M. (2012) · Science · doi:10.1126/science.1223560 · Cited by 1,059

Reversible phosphorylation of Drp1 by cyclic AMP‐dependent protein kinase and calcineurin regulates mitochondrial fission and cell death

Cribbs, J. T., & Strack, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,020

Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice

Sundaresan, N. R., Gupta, M., Kim, G., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 995

PARIS (ZNF746) Repression of PGC-1α Contributes to Neurodegeneration in Parkinson's Disease

Shin, J.-H., Ko, H. S., Kang, H., Lee, Y., Lee, Y.-I., Pletinkova, O., Troconso, J. C., Dawson, V. L., & Dawson, T. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.010 · Cited by 953

The Mitochondrial Phosphatase PGAM5 Functions at the Convergence Point of Multiple Necrotic Death Pathways

Wang, Z., Jiang, H., Chen, S., Du, F., & Wang, X. (2012) · Cell · doi:10.1016/j.cell.2011.11.030 · Cited by 949

Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy

Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910

Autophagy maintains the metabolism and function of young and old stem cells

Ho, T. T., Warr, M. R., Adelman, E. R., Lansinger, O. M., Flach, J., Verovskaya, E. V., Figueroa, M. E., & Passegué, E. (2017) · Nature · doi:10.1038/nature21388 · Cited by 896

Mitochondrial Machineries for Protein Import and Assembly

Wiedemann, N., & Pfanner, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014352 · Cited by 890

Mitochondria–lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis

Wong, Y. C., Ysselstein, D., & Krainc, D. (2018) · Nature · doi:10.1038/nature25486 · Cited by 876

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

Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor

Wei, Y., Chiang, W.-C., Sumpter, R., Mishra, P., & Levine, B. (2017) · Cell · doi:10.1016/j.cell.2016.11.042 · Cited by 842

Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals

Quirós, P. M., Prado, M. A., Zamboni, N., D’Amico, D., Williams, R. W., Finley, D., Gygi, S. P., & Auwerx, J. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201702058 · Cited by 832

Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease

Casari, G., De Fusco, M., Ciarmatori, S., Zeviani, M., Mora, M., Fernandez, P., De Michele, G., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 830

OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L

Song, Z., Chen, H., Fiket, M., Alexander, C., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704110 · Cited by 828

An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2

Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817

Mito-Morphosis: Mitochondrial Fusion, Fission, and Cristae Remodeling as Key Mediators of Cellular Function

Pernas, L., & Scorrano, L. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 817

The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy

Kwon, Y. T., & Ciechanover, A. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.09.002 · Cited by 817

Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation

Wong, Y. C., & Holzbaur, E. L. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405752111 · Cited by 812

The i -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission

Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812

Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy

Okamoto, K., Kondo-Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 797

SLP‐2 is required for stress‐induced mitochondrial hyperfusion

Tondera, D., Grandemange, S., Jourdain, A., Karbowski, M., Mattenberger, Y., Herzig, S., Da Cruz, S., Clerc, P., Raschke, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 779

The Novel Tail-anchored Membrane Protein Mff Controls Mitochondrial and Peroxisomal Fission in Mammalian Cells

Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769

A Network of Macrophages Supports Mitochondrial Homeostasis in the Heart

Nicolás-Ávila, J. A., Lechuga-Vieco, A. V., Esteban-Martínez, L., Sánchez-Díaz, M., Díaz-García, E., Santiago, D. J., Rubio-Ponce, A., Li, J. L., Balachander, A., Quintana, J. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.031 · Cited by 762

A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes

Soubannier, V., McLelland, G.-L., Zunino, R., Braschi, E., Rippstein, P., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 761

A Lethal Defect of Mitochondrial and Peroxisomal Fission

Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749

Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control

McLelland, G., Soubannier, V., Chen, C. X., McBride, H. M., & Fon, E. A. (2014) · The EMBO Journal · doi:10.1002/embj.201385902 · Cited by 743

Mitochondrial Rhomboid PARL Regulates Cytochrome c Release during Apoptosis via OPA1-Dependent Cristae Remodeling

Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W., D'Adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 741

Mitochondrial disorders as windows into an ancient organelle

Vafai, S. B., & Mootha, V. K. (2012) · Nature · doi:10.1038/nature11707 · Cited by 737

Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity

Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731

Chronic enrichment of hepatic endoplasmic reticulum–mitochondria contact leads to mitochondrial dysfunction in obesity

Arruda, A. P., Pers, B. M., Parlakgül, G., Güney, E., Inouye, K., & Hotamisligil, G. S. (2014) · Nature Medicine · doi:10.1038/nm.3735 · Cited by 720

Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors

Johansen, T., & Lamark, T. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.07.016 · Cited by 717

The mitochondrial UPR: mechanisms, physiological functions and implications in ageing

Shpilka, T., & Haynes, C. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.110 · Cited by 714

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

Platelets release mitochondria serving as substrate for bactericidal group IIA-secreted phospholipase A2 to promote inflammation

Boudreau, L. H., Duchez, A.-C., Cloutier, N., Soulet, D., Martin, N., Bollinger, J., Paré, A., Rousseau, M., Naika, G. S., Lévesque, T., et al. (2014) · Blood · doi:10.1182/blood-2014-05-573543 · Cited by 703

Maintenance and Expression of Mammalian Mitochondrial DNA

Gustafsson, C. M., Falkenberg, M., & Larsson, N.-G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014402 · Cited by 700

3D tomography reveals connections between the phagophore and endoplasmic reticulum

Ylä-Anttila, P., Vihinen, H., Jokitalo, E., & Eskelinen, E.-L. (2009) · Autophagy · doi:10.4161/auto.5.8.10274 · Cited by 675

Mitochondrial stress is relayed to the cytosol by an OMA1–DELE1–HRI pathway

Guo, X., Aviles, G., Liu, Y., Tian, R., Unger, B. A., Lin, Y.-H. T., Wiita, A. P., Xu, K., Correia, M. A., & Kampmann, M. (2020) · Nature · doi:10.1038/s41586-020-2078-2 · Cited by 674

Transcellular degradation of axonal mitochondria

Davis, C.-H. O., Kim, K.-Y., Bushong, E. A., Mills, E. A., Boassa, D., Shih, T., Kinebuchi, M., Phan, S., Zhou, Y., Bihlmeyer, N. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404651111 · Cited by 673

ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells

Lewis, S. C., Uchiyama, L. F., & Nunnari, J. (2016) · Science · doi:10.1126/science.aaf5549 · Cited by 673

PINK1 is degraded through the N-end rule pathway

Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 672

C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane

Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670

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

Atg8 family LC3/GABARAP proteins are crucial for autophagosome–lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation

Nguyen, T. N., Padman, B. S., Usher, J., Oorschot, V., Ramm, G., & Lazarou, M. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201607039 · Cited by 668

The Transcription Factor ATF5 Mediates a Mammalian Mitochondrial UPR

Fiorese, C. J., Schulz, A. M., Lin, Y.-F., Rosin, N., Pellegrino, M. W., & Haynes, C. M. (2016) · Current Biology · doi:10.1016/j.cub.2016.06.002 · Cited by 667

EMRE Is an Essential Component of the Mitochondrial Calcium Uniporter Complex

Sancak, Y., Markhard, A. L., Kitami, T., Kovács-Bogdán, E., Kamer, K. J., Udeshi, N. D., Carr, S. A., Chaudhuri, D., Clapham, D. E., Li, A. A., et al. (2013) · Science · doi:10.1126/science.1242993 · Cited by 663

MiD49 and MiD51, new components of the mitochondrial fission machinery

Palmer, C. S., Osellame, L. D., Laine, D., Koutsopoulos, O. S., Frazier, A. E., & Ryan, M. T. (2011) · The EMBO Reports · doi:10.1038/embor.2011.54 · Cited by 649

A Ribosome-Bound Quality Control Complex Triggers Degradation of Nascent Peptides and Signals Translation Stress

Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A., Williams, C. C., Li, G.-W., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 646

PGC-1 α, Inflammation, and Oxidative Stress: An Integrative View in Metabolism

Rius-Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á. L., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 642

Parkin Mediates Proteasome-dependent Protein Degradation and Rupture of the Outer Mitochondrial Membrane

Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612

A Regulatory Signaling Loop Comprising the PGAM5 Phosphatase and CK2 Controls Receptor-Mediated Mitophagy

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ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans

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Early ERK1/2 activation promotes DRP1-dependent mitochondrial fission necessary for cell reprogramming

Prieto, J., León, M., Ponsoda, X., Sendra, R., Bort, R., Ferrer-Lorente, R., Raya, A., López-García, C., & Torres, J. (2016) · Nature Communications · doi:10.1038/ncomms11124 · Cited by 273

The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria

Griffin, E. E., Graumann, J., & Chan, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503148 · Cited by 265

Phosphorylated ubiquitin chain is the genuine Parkin receptor

Okatsu, K., Koyano, F., Kimura, M., Kosako, H., Saeki, Y., Tanaka, K., & Matsuda, N. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201410050 · Cited by 263

SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin μ gene expression

Dobreva, G., Dambacher, J., & Grosschedl, R. (2003) · Genes & Development · doi:10.1101/gad.1153003 · Cited by 255

Human Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery

Yu, R., Jin, S., Lendahl, U., Nistér, M., & Zhao, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899748 · Cited by 251

Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system

McLelland, G.-L., Lee, S. A., McBride, H. M., & Fon, E. A. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201603105 · Cited by 250

The Scaffold Protein Atg11 Recruits Fission Machinery to Drive Selective Mitochondria Degradation by Autophagy

Mao, K., Wang, K., Liu, X., & Klionsky, D. J. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.024 · Cited by 249

Cdc48-associated complex bound to 60S particles is required for the clearance of aberrant translation products

Defenouillère, Q., Yao, Y., Mouaikel, J., Namane, A., Galopier, A., Decourty, L., Doyen, A., Malabat, C., Saveanu, C., Jacquier, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221724110 · Cited by 248

Mitochondrial Proteases: Multifaceted Regulators of Mitochondrial Plasticity

Deshwal, S., Fiedler, K. U., & Langer, T. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012739 · Cited by 246

Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1

Park, Y.-Y., Lee, S., Karbowski, M., Neutzner, A., Youle, R. J., & Cho, H. (2010) · Journal of Cell Science · doi:10.1242/jcs.061481 · Cited by 244

Extracellular Regulated Kinase Phosphorylates Mitofusin 1 to Control Mitochondrial Morphology and Apoptosis

Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244

The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover

Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0748 · Cited by 243

Reciprocal Regulation of Mitochondrial Fission and Fusion

Sabouny, R., & Shutt, T. E. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.03.009 · Cited by 241

Perrault Syndrome Is Caused by Recessive Mutations in CLPP, Encoding a Mitochondrial ATP-Dependent Chambered Protease

Jenkinson, E. M., Rehman, A. U., Walsh, T., Clayton-Smith, J., Lee, K., Morell, R. J., Drummond, M. C., Khan, S. N., Naeem, M. A., Rauf, B., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.02.013 · Cited by 240

The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells

Tondera, D., Czauderna, F., Paulick, K., Schwarzer, R., Kaufmann, J., & Santel, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02415 · Cited by 239

Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore

Quinsay, M. N., Thomas, R. L., Lee, Y., & Gustafsson, Å. B. (2010) · Autophagy · doi:10.4161/auto.6.7.13005 · Cited by 238

Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome

Verma, R., Oania, R. S., Kolawa, N. J., & Deshaies, R. J. (2013) · eLife · doi:10.7554/elife.00308 · Cited by 238

OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution

Elachouri, G., Vidoni, S., Zanna, C., Pattyn, A., Boukhaddaoui, H., Gaget, K., Yu-Wai-Man, P., Gasparre, G., Sarzi, E., Delettre, C., et al. (2011) · Genome Research · doi:10.1101/gr.108696.110 · Cited by 238

Mitocellular communication: Shaping health and disease

Mottis, A., Herzig, S., & Auwerx, J. (2019) · Science · doi:10.1126/science.aax3768 · Cited by 238

CHOP induces activating transcription factor 5 (ATF5) to trigger apoptosis in response to perturbations in protein homeostasis

Teske, B. F., Fusakio, M. E., Zhou, D., Shan, J., McClintick, J. N., Kilberg, M. S., & Wek, R. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-01-0067 · Cited by 237

ATP-Dependent Lon Protease Controls Tumor Bioenergetics by Reprogramming Mitochondrial Activity

Quirós, P. M., Español, Y., Acín-Pérez, R., Rodríguez, F., Bárcena, C., Watanabe, K., Calvo, E., Loureiro, M., Fernández-García, M. S., Fueyo, A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.018 · Cited by 233

Mitophagy in the pathogenesis and management of disease

Wang, Q., Sun, Y., Li, T. Y., & Auwerx, J. (2026) · Cell Research · doi:10.1038/s41422-025-01203-7 · Cited by 103