Mitochondrial quality control: An integrated network of pathways

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

ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis

D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works

Mechanisms of mitophagy

Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · 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

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

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

Mitochondrial fusion and fission in cell life and death

Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · see citing works

The Biologic Clock: The Mitochondria?

Harman, D. (1972) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1972.tb00787.x · Cited by 1,991 · see citing works

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969 · see citing works

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375 · see citing works

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 · see citing works

Regulation of autophagy by ROS: physiology and pathology

Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263 · see citing works

Mitochondria 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

The sites and topology of mitochondrial superoxide production

Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works

The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity

Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · see citing works

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 · see citing works

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress

Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works

The Machines that Divide and Fuse Mitochondria

Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790 · see citing works

Mitochondrial DNA mutations in disease and aging

Wallace, D. C. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20586 · Cited by 622 · see citing works

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 · see citing works

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

Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., & Ron, D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.016 · Cited by 595 · see citing works

Hydrogen peroxide: a Jekyll and Hyde signalling molecule

Gough, D. R., & Cotter, T. G. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.96 · Cited by 563 · see citing works

Somatic Mitochondrial DNA Mutations in Mammalian Aging

Larsson, N. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-093701 · Cited by 543 · see citing works

Quality control of mitochondria: protection against neurodegeneration and ageing

Tatsuta, T., & Langer, T. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601972 · Cited by 519 · see citing works

The mitochondrial UPR – protecting organelle protein homeostasis

Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works

The matrix peptide exporter HAF-1 signals a mitochondrial unfolded protein response by activating the transcription factor ZC376.7 in C. elegans

Haynes, C. M., Yang, Y., Blais, S., Neubert, T., & Ron, D. (2010) · Molecules and Cells · doi:10.1016/j.molcel.2010.01.015 · Cited by 480 · see citing works

Mitochondrial filaments and clusters as intracellular power-transmitting cables

Skulachev, V. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01735-7 · Cited by 477 · see citing works

Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H ₂ O ₂ , and Protein Chaperones

Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463 · see citing works

The m-AAA Protease Defective in Hereditary Spastic Paraplegia Controls Ribosome Assembly in Mitochondria

Nolden, M., Ehses, S., Koppen, M., Bernacchia, A., Rugarli, E. I., & Langer, T. (2005) · Cell · doi:10.1016/j.cell.2005.08.003 · Cited by 398 · see citing works

Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models

Scheckhuber, C. Q., Erjavec, N., Tinazli, A., Hamann, A., Nyström, T., & Osiewacz, H. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1524 · Cited by 344 · see citing works

Mitophagy in Yeast Occurs through a Selective Mechanism

Kanki, T., & Klionsky, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802403200 · Cited by 335 · see citing works

A Stress-Responsive System for Mitochondrial Protein Degradation

Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304 · see citing works

Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death

Moon, J. C., Hah, Y., Kim, W. Y., Jung, B. G., Jang, H. H., Lee, J. R., Kim, S. Y., Lee, Y., Jeon, M. G., Kim, C. W., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505362200 · Cited by 300 · see citing works

A mitochondrial etiology of Alzheimer and Parkinson disease

Coskun, P. E., Wyrembak, J., Schriner, S. E., Chen, H.-W., Marciniack, C., LaFerla, F. M., & Wallace, D. C. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.008 · Cited by 297 · see citing works

Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)

Matsushima, Y., Goto, Y.-I., & Kaguni, L. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008924107 · Cited by 294 · see citing works

When a theory of aging ages badly

Lapointe, J., & Hekimi, S. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0138-8 · Cited by 261 · see citing works

Protein Degradation within Mitochondria: Versatile Activities of AAA Proteases and Other Peptidases

Koppen, M., & Langer, T. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701380452 · Cited by 252 · see citing works

Molecular Machinery of Mitochondrial Fusion and Fission

Westermann, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800011200 · Cited by 251 · see citing works

Mitochondrial DNA repair pathways

Croteau, D. L., Stierum, R. H., & Bohr, V. A. (1999) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(99)00025-7 · Cited by 240 · see citing works

Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1

Glauser, L., Sonnay, S., Stafa, K., & Moore, D. J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07318.x · Cited by 230 · see citing works

Membrane Protein Degradation by AAA Proteases in Mitochondria

Leonhard, K., Guiard, B., Pellecchia, G., Tzagoloff, A., Neupert, W., & Langer, T. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80242-7 · Cited by 218 · see citing works

Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death

Bota, D. A., Ngo, J. K., & Davies, K. J. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.017 · Cited by 203 · see citing works

Mitophagy Selectively Degrades Individual Damaged Mitochondria After Photoirradiation

Kim, I., & Lemasters, J. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3768 · Cited by 193 · see citing works

Mitochondrial protein quality control during biogenesis and aging

Baker, B. M., & Haynes, C. M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.004 · Cited by 192 · see citing works

SOD1 and Amyotrophic Lateral Sclerosis: Mutations and Oligomerization

Banci, L., Bertini, I., Boca, M., Girotto, S., Martinelli, M., Valentine, J. S., & Vieru, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001677 · Cited by 190 · see citing works

Mitochondrial mutational spectra in human cells and tissues

Khrapko, K., Coller, H. A., André, P. C., Li-Sucholeiki, X., Hanekamp, J. S., & Thilly, W. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.13798 · Cited by 182 · see citing works

Mitochondrial quality control by the ubiquitin–proteasome system

Taylor, E. B., & Rutter, J. P. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391509 · Cited by 181 · see citing works

Functions and evolution of selenoprotein methionine sulfoxide reductases

Lee, B. C., Dikiy, A., Kim, H.-Y., & Gladyshev, V. N. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.014 · Cited by 178 · see citing works

Ubiquitin–Proteasome-dependent Degradation of a Mitofusin, a Critical Regulator of Mitochondrial Fusion

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

DNA repair in organelles: Pathways, organization, regulation, relevance in disease and aging

Boesch, P., Weber‐Lotfi, F., Ibrahim, N., Тарасенко, В. И., Cosset, A., Paulus, F., Lightowlers, R. N., & Dietrich, A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.002 · Cited by 165 · see citing works

Nuclear mutations in Saccharomyces cerevisiae that affect the escape of DNA from mitochondria to the nucleus.

Thorsness, P. E., & Fox, T. D. (1993) · Genetics · doi:10.1093/genetics/134.1.21 · Cited by 163 · see citing works

Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2

Mendl, N., Occhipinti, A., Müller, M. M., Wild, P. S., Đikić, I., & Reichert, A. S. (2011) · Journal of Cell Science · doi:10.1242/jcs.076406 · Cited by 161 · see citing works

The Dual Functions of Thiol-Based Peroxidases in H 2 O 2 Scavenging and Signaling

Fourquet, S., Huang, M., D’Autréaux, B., & Tolédano, M. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2049 · Cited by 157 · see citing works

Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: the involvement of the oxidative stress response regulators Yap1 and Skn7

Costa, V., Amorim, M. A., Quintanilha, A. T., & Moradas‐Ferreira, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01086-9 · Cited by 153 · see citing works

Roles for the Human ATP-dependent Lon Protease in Mitochondrial DNA Maintenance

Lü, B., Yadav, S. S., Shah, P. G., Liu, T., Tian, B., Pukszta, S., Villaluna, N., Kutějová, E., Newlon, C. S., Santos, J. H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611540200 · Cited by 148 · see citing works

Apoptosis pathways in fungal growth, development and ageing

Hamann, A., Brust, D., & Osiewacz, H. D. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.03.003 · Cited by 143 · see citing works

Mitochondrial DNA repair and association with aging – An update

Gredilla, R., Bohr, V. A., & Stevnsner, T. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.017 · Cited by 141 · see citing works

Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress

Ugarte, N., Petropoulos, I., & Friguet, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2998 · Cited by 136 · see citing works

Increasing organismal healthspan by enhancing mitochondrial protein quality control

Luce, K., & Osiewacz, H. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1893 · Cited by 133 · see citing works

Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins

Cox, A. G., Pearson, A. G., Pullar, J. M., Jönsson, T. J., Lowther, W. T., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemical Journal · doi:10.1042/bj20090242 · Cited by 112 · see citing works

Impaired quality control of mitochondria: Aging from a new perspective

Weber, T. A., & Reichert, A. S. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.018 · Cited by 110 · see citing works

Mitochondrial dynamics in model organisms: What yeasts, worms and flies have taught us about fusion and fission of mitochondria

Westermann, B. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.12.003 · Cited by 98 · see citing works

Oxidant-specific Folding of Yap1p Regulates Both Transcriptional Activation and Nuclear Localization

Gulshan, K., Rovinsky, S. A., Coleman, S. T., & Moye-Rowley, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504716200 · Cited by 89 · see citing works

Presequence‐dependent folding ensures MrpL32 processing by the m‐AAA protease in mitochondria

Bonn, F., Tatsuta, T., Petrungaro, C., Riemer, J., & Langer, T. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.169 · Cited by 83 · see citing works

Methionine sulfoxide reductase A expression is regulated by the DAF‐16/FOXO pathway in Caenorhabditis elegans

Minniti, A. N., Cataldo, R., Trigo, C., Vásquez, L., Mujica, P. E., Leighton, F., Inestrosa, N. C., & Aldunate, R. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00521.x · Cited by 73 · see citing works

Mitochondrial functions and aging

Osiewacz, H. D. (2002) · Gene · doi:10.1016/s0378-1119(01)00804-6 · Cited by 70 · see citing works

Mitochondrial protein quality control: Implications in ageing

Friguet, B., Bulteau, A., & Petropoulos, I. (2008) · Biotechnology Journal · doi:10.1002/biot.200800041 · Cited by 70 · see citing works

Modulation of mitochondrial function and morphology by interaction of Omi/HtrA2 with the mitochondrial fusion factor OPA1

Kieper, N., Holmström, K. M., Ciceri, D., Fiesel, F. C., Wolburg, H., Ziviani, E., Whitworth, A. J., Martins, L. M., Kahle, P. J., & Krüger, R. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.01.005 · Cited by 67 · see citing works

ROS leads to MnSOD upregulation through ERK2 translocation and p53 activation in selenite‐induced apoptosis of NB4 cells

Li, Z., Shi, K., Guan, L., Cao, T., Jiang, Q., Yang, Y., & Xu, C. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.040 · Cited by 65 · see citing works

Mitochondrial Protein Quality Control Systems in Aging and Disease

Luce, K., Weil, A. C., & Osiewacz, H. D. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_9 · Cited by 59 · see citing works

Genetic regulation of aging

Osiewacz, H. D. (1997) · Journal of Molecular Medicine · doi:10.1007/s001090050158 · Cited by 57 · see citing works

Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA

Chen, S., Suzuki, C. K., & Wu, S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1140 · Cited by 53 · see citing works

Dual Function of Protein Kinase C (PKC) in 12-O-Tetradecanoylphorbol-13-acetate (TPA)-induced Manganese Superoxide Dismutase (MnSOD) Expression

Chung, Y. W., Kim, H.-K., Kim, I. Y., Yim, M. B., & Chock, P. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264945 · Cited by 47 · see citing works

Fussy mitochondria fuse in response to stress

van der Bliek, A. M. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.130 · Cited by 46 · see citing works

On the timing and the extent of clonal expansion of mtDNA deletions: Evidence from single-molecule PCR

Nicholas, A., Kraytsberg, Y., Guo, X., & Khrapko, K. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.04.029 · Cited by 38 · see citing works

Protein Metabolism and Homeostasis in Aging

Tavernarakis, N. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2 · Cited by 35 · see citing works

Gene expression profiling implicates OXPHOS complexes in lifespan extension of flies over-expressing a small mitochondrial chaperone, Hsp22

Kim, H.-J., Morrow, G., Westwood, J. T., Michaud, S., & Tanguay, R. M. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.12.012 · Cited by 34 · see citing works

Unmasking a temperature-dependent effect of the P. anserina i-AAA protease on aging and development

Weil, A. C., Luce, K., Dröse, S., Wittig, I., Brandt, U., & Osiewacz, H. D. (2011) · Cell Cycle · doi:10.4161/cc.10.24.18560 · Cited by 34 · see citing works

MAP-1 and IAP-1, Two Novel AAA Proteases with Catalytic Sites on Opposite Membrane Surfaces in Mitochondrial Inner Membrane ofNeurospora crassa

Klanner, C., Prokisch, H., & Langer, T. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2858 · Cited by 27 · see citing works

Transcriptional and Cellular Responses to Defective Mitochondrial Proteolysis in Fission Yeast

Guha, S., López‐Maury, L., Shaw, M. K., Bähler, J., Norbury, C. J., & Agashe, V. R. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.044 · Cited by 18 · see citing works

DNA-Triggered Aggregation of Copper, Zinc Superoxide Dismutase in the Presence of Ascorbate

Yin, J., Hu, S., Jiang, W., Liu, L., Lan, S., Song, X., & Liu, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012328 · Cited by 11 · see citing works

Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.

Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274 · see citing works

Mitochondrial 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

Mitochondria as a Target of Environmental Toxicants

Meyer, J. N., Leung, M. C. K., Rooney, J. P., Sendoel, A., Hengartner, M. O., Kisby, G. E., & Bess, A. S. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft102 · Cited by 571 · 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

Drug-induced mitochondrial dysfunction and cardiotoxicity

Varga, Z. V., Ferdinandy, P., Liaudet, L., & Pacher, P. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00554.2015 · Cited by 535 · see citing works

Chronic inflammation and the hallmarks of aging

Baechle, J. J., Chen, N., Makhijani, P., Winer, S., Furman, D., & Winer, D. A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101755 · Cited by 471 · 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

Multidimensional proteomics for cell biology

Larance, M., & Lamond, A. I. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3970 · Cited by 408 · see citing works

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 · see citing works

Mitochondrial quality control mechanisms as molecular targets in cardiac ageing

Picca, A., Mankowski, R. T., Burman, J. L., Donisi, L., Js, K., Marzetti, E., & Leeuwenburgh, C. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0059-z · Cited by 393 · see citing works

Mitochondrial pathways in sarcopenia of aging and disuse muscle atrophy

Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works

Neurobiology, Clinical Presentation, and Treatment of Methamphetamine Use Disorder: A Review

Paulus, M. P., & Stewart, J. L. (2020) · JAMA Psychiatry · doi:10.1001/jamapsychiatry.2020.0246 · Cited by 310 · see citing works

AMPK, Mitochondrial Function, and Cardiovascular Disease

Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · see citing works

Mitochondrial dysfunction and damage associated molecular patterns (DAMPs) in chronic inflammatory diseases

Dela Cruz, C. S., & Kang, M.-J. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.12.001 · Cited by 255 · see citing works

Oxidative stress and ageing

Birch-Machin, M. A., & Bowman, A. (2016) · British Journal of Dermatology · doi:10.1111/bjd.14906 · Cited by 225 · see citing works

Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis

Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 219 · see citing works

The Role of Mitochondria in the Mechanisms of Cardiac Ischemia-Reperfusion Injury

Kuznetsov, A. V., Javadov, S. A., Margreiter, R., Grimm, M. F., Hagenbuchner, J., & Ausserlechner, M. J. (2019) · Antioxidants · doi:10.3390/antiox8100454 · Cited by 199 · see citing works

Mitochondria, Oxidative Stress and the Kynurenine System, with a Focus on Ageing and Neuroprotection

Sas, K., Szabó, E., & Vécsei, L. (2018) · Molecules · doi:10.3390/molecules23010191 · Cited by 199 · see citing works

Sestrin-2 and BNIP3 regulate autophagy and mitophagy in renal tubular cells in acute kidney injury

Ishihara, M., Urushido, M., Hamada, K., Matsumoto, T., Shimamura, Y., Ogata, K., Inoue, K., Taniguchi, Y., Horino, T., Fujieda, M., et al. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00642.2012 · Cited by 195 · see citing works

Mitochondrial Energy and Redox Signaling in Plants

Schwarzländer, M., & Finkemeier, I. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5104 · Cited by 192 · see citing works

Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors

Gispert, S., Parganlija, D., Klinkenberg, M., Dröse, S., Wittig, I., Mittelbronn, M. G. A., Grzmil, P., Koob, S., Hamann, A., Walter, M. J., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt338 · Cited by 188 · see citing works

Dysregulation of mitochondrial dynamics, mitophagy and apoptosis in major depressive disorder: Does inflammation play a role?

Scaini, G., Mason, B. L., Díaz, A. P., Jha, M. K., Soares, J. C., Trivedi, M. H., & Quevedo, J. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01312-w · Cited by 184 · see citing works

The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion

Venditti, P., & Meo, S. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062173 · Cited by 170 · see citing works

The Complex Interplay between Mitochondria, ROS and Entire Cellular Metabolism

Kuznetsov, A. V., Margreiter, R., Ausserlechner, M. J., & Hagenbuchner, J. (2022) · Antioxidants · doi:10.3390/antiox11101995 · Cited by 168 · see citing works

Why size matters – balancing mitochondrial dynamics in Alzheimer's disease

DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 164 · see citing works

What is the function of mitochondrial networks? A theoretical assessment of hypotheses and proposal for future research

Hoitzing, H., Johnston, I. G., & Jones, N. S. (2015) · BioEssays · doi:10.1002/bies.201400188 · Cited by 159 · see citing works

Targeting AMPK Signaling as a Neuroprotective Strategy in Parkinson’s Disease

Curry, D. W., Stutz, B., Andrews, Z. B., & Elsworth, J. D. (2018) · Journal of Parkinson s Disease · doi:10.3233/jpd-171296 · Cited by 159 · see citing works

The Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases

Bhandari, V., Wong, K. S., Zhou, J. L., Mabanglo, M. F., Batey, R. A., & Houry, W. A. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00124 · Cited by 157 · see citing works

Mitochondrial ClpP serine protease-biological function and emerging target for cancer therapy

Nouri, K., Feng, Y., & Schimmer, A. D. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03062-z · Cited by 156 · see citing works

Huntington’s Disease and Mitochondria

Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 148 · see citing works

The role of mitochondria in mood disorders: from physiology to pathophysiology and to treatment

Giménez-Palomo, A., Dodd, S., Anmella, G., Carvalho, A. F., Scaini, G., Quevedo, J., Pacchiarotti, I., Vieta, E., & Berk, M. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.546801 · Cited by 140 · see citing works

Mitochondria—hubs for regulating cellular biochemistry: emerging concepts and networks

Anderson, A. J., Jackson, T. D., Stroud, D. A., & Stojanovski, D. (2019) · Open Biology · doi:10.1098/rsob.190126 · Cited by 130 · see citing works

Mitochondrial Dysfunction in Neural Injury

Zhao, X., Lu, M., Yuan, D., Xu, D.-E., Yao, P.-P., Ji, W., Chen, H., Liu, W., Yan, C.-X., Xia, Y., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00030 · Cited by 126 · see citing works

Simultaneous impairment of mitochondrial fission and fusion reduces mitophagy and shortens replicative lifespan

Bernhardt, D., Müller, M., Reichert, A. S., & Osiewacz, H. D. (2015) · Scientific Reports · doi:10.1038/srep07885 · Cited by 125 · see citing works

A mitochondrial FUNDC1/HSC70 interaction organizes the proteostatic stress response at the risk of cell morbidity

Li, Y., Xue, Y., Xu, X., Wang, G., Liu, Y., Wu, H., Li, W., Wang, Y., Chen, Z., Zhang, W., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798786 · Cited by 117 · see citing works

Muscle-generated BDNF (brain derived neurotrophic factor) maintains mitochondrial quality control in female mice

Ahuja, P., Ng, C. F., Pang, B. P. S., Chan, W. S., Tse, M. C. L., Bi, X., Kwan, H.-L. R., Brobst, D., Herlea-Pana, O., Yang, X., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.1985257 · Cited by 116 · see citing works

Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death

Wong, K. S., Mabanglo, M. F., Seraphim, T. V., Mollica, A., Mao, Y.-Q., Rizzolo, K., Leung, E., Moutaoufik, M. T., Hoell, L., Phanse, S., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.05.014 · Cited by 116 · see citing works

Mitochondrial hyperpolarization during chronic complex I inhibition is sustained by low activity of complex II, III, IV and V

Forkink, M., Manjeri, G. R., Liemburg-Apers, D. C., Nibbeling, E. A. R., Blanchard, M. G., Wojtala, A., Smeitink, J. A. M., Wieckowski, M. R., Willems, P. H. G. M., & Koopman, W. J. H. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.04.008 · Cited by 106 · see citing works

Mitochondrial Dysfunction in Primary Ovarian Insufficiency

Tiosano, D., Mears, J. A., & Buchner, D. A. (2019) · Endocrinology · doi:10.1210/en.2019-00441 · Cited by 105 · see citing works

Oxidative stress-a key emerging impact factor in health, ageing, lifestyle and aesthetics

Kandola, K., Bowman, A., & Birch‐Machin, M. A. (2015) · International Journal of Cosmetic Science · doi:10.1111/ics.12287 · Cited by 103 · see citing works

Mitochondrial and Nuclear DNA Damage and Repair in Age-Related Macular Degeneration

Błasiak, J., Głowacki, S., Kauppinen, A., & Kaarniranta, K. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14022996 · Cited by 98 · see citing works

PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control

Zhuang, N., Li, L., Chen, S., & Wang, T. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.396 · Cited by 92 · see citing works

Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism

Fischer, F., Langer, J. D., & Osiewacz, H. D. (2015) · Scientific Reports · doi:10.1038/srep18375 · Cited by 96 · see citing works

Mitochondria and Aging—The Role of Exercise as a Countermeasure

Nilsson, M. I., & Tarnopolsky, M. A. (2019) · Biology · doi:10.3390/biology8020040 · Cited by 92 · see citing works

The disruption of mitochondrial axonal transport is an early event in neuroinflammation

Errea, O., Moreno, B., González-Franquesa, A., García-Rovés, P. M., & Villoslada, P. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0375-8 · Cited by 90 · see citing works

Irisin exhibits neuroprotection by preventing mitochondrial damage in Parkinson’s disease

Zhang, X., Xu, S., Hu, Y. H., Liu, Q., Liu, C., Chai, H., Luo, Y., Jin, L., & Li, S. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00453-9 · Cited by 87 · see citing works

The Mitochondrial Rhomboid Protease PARL Is Regulated by PDK2 to Integrate Mitochondrial Quality Control and Metabolism

Shi, G., & McQuibban, G. A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.029 · Cited by 82 · see citing works

Chaperone-Independent Peripheral Quality Control of CFTR by RFFL E3 Ligase

Okiyoneda, T., Veit, G., Sakai, R., Aki, M., Fujihara, T., Higashi, M., Susuki-Miyata, S., Miyata, M., Fukuda, N., Yoshida, A., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.02.001 · Cited by 83 · see citing works

AMPK activation serves a critical role in mitochondria quality control via modulating mitophagy in the heart under chronic hypoxia

Zhang, H., Liu, B., Li, T., Zhu, Y. K., Luo, G.-P., Jiang, Y., Tang, F., Zhao, J., & Xiao, Y. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3213 · Cited by 80 · see citing works

Mitochondrial transfer between cell crosstalk – An emerging role in mitochondrial quality control

Liu, Y., Fu, T., Li, G., Li, B., Luo, G., Li, N., & Geng, Q. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102038 · Cited by 78 · see citing works

Redox signalling and mitochondrial stress responses; lessons from inborn errors of metabolism

Olsen, R. K. J., Cornelius, N., & Gregersen, N. (2015) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-015-9861-5 · Cited by 78 · see citing works

Mitochondrial dysfunction as a critical event in the pathophysiology of bipolar disorder

Scaini, G., Andrews, T., Lima, C. N. D. C., Benevenuto, D., STRECK, E. L., & Quevedo, J. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.002 · Cited by 77 · see citing works

Degradation Rate of Mitochondrial Proteins in Arabidopsis thaliana Cells

Nelson, C. J., Li, L., Jacoby, R. P., & Millar, A. H. (2013) · Journal of Proteome Research · doi:10.1021/pr400304r · Cited by 76 · see citing works

Morphological and bioenergetic demands underlying the mitophagy in post-mitotic neurons: the pink–parkin pathway

Amadoro, G., Corsetti, V., Florenzano, F., Atlante, A., Bobba, A., Nicolin, V., Nori, S., & Calissano, P. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00018 · Cited by 80 · see citing works

Calcineurin suppresses AMPK-dependent cytoprotective autophagy in cardiomyocytes under oxidative stress

He, H., Liu, X., Lv, L., Liang, H., Leng, B., Zhao, D., Zhang, Y., Du, Z., Chen, X., Li, S., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.533 · Cited by 75 · see citing works

Astragaloside IV ameliorates diabetic nephropathy by modulating the mitochondrial quality control network

Liu, X., Wang, W., Song, G., Wei, X., Zeng, Y., Han, P., Wang, D., Shao, M., Wu, J., Sun, H., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182558 · Cited by 74 · see citing works

Multi-target-directed therapeutic strategies for Alzheimer's disease: controlling amyloid-β aggregation, metal ion homeostasis, and enzyme inhibition

Yoo, J., Lee, J., Ahn, B., Han, J., & Lim, M. H. (2025) · Chemical Science · doi:10.1039/d4sc06762b · Cited by 74 · see citing works

Mitochondria: key players in the neurotoxic effects of amphetamines

Barbosa, D. J., Capela, J. P., Feio‐Azevedo, R., Gomes, A., Bastos, M. D. L., & Carvalho, F. D. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1478-9 · Cited by 69 · see citing works

Adiponectin modulates oxidative stress-induced mitophagy and protects C2C12 myoblasts against apoptosis

Ren, Y., Li, Y., Yan, J., Ma, M., Zhou, D., Xue, Z., Zhang, Z., Liu, H., Yang, H., Jia, L., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-03319-2 · Cited by 68 · see citing works

The mitochondrial unfolded protein response in mammalian physiology

Mottis, A., Jovaisaite, V., & Auwerx, J. H. (2014) · Mammalian Genome · doi:10.1007/s00335-014-9525-z · Cited by 68 · see citing works

Mitochondrial MsrB2 serves as a switch and transducer for mitophagy

Lee, S. H., Lee, S., Du, J., Jain, K., Ding, M., Kadado, A. J., Atteya, G. A., Jaji, Z., Tyagi, T., Kim, W., et al. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201910409 · Cited by 67 · see citing works

Mitophagy and Its Contribution to Metabolic and Aging-Associated Disorders

Liu, L., Liao, X., Wu, H., Li, Y., Zhu, Y., & Chen, Q. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.8013 · Cited by 68 · see citing works

Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain

Fischer, F., Weil, A. C., Hamann, A., & Osiewacz, H. D. (2013) · Nature Communications · doi:10.1038/ncomms2397 · Cited by 67 · see citing works

Emerging role of transcription factor EB in mitochondrial quality control

Wang, S., Chen, Y., Li, X., Zhang, W., Liu, Z., Wu, M., Pan, Q., & Liu, H. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110272 · Cited by 62 · see citing works

Mitochondrial Quality Control: Its Role in Metabolic Dysfunction-Associated Steatotic Liver Disease (MASLD)

Shin, S., Kim, J., Lee, J., Kim, J., & Oh, C. (2023) · Journal of Obesity & Metabolic Syndrome · doi:10.7570/jomes23054 · Cited by 66 · see citing works

The Tricky Connection between Extracellular Vesicles and Mitochondria in Inflammatory-Related Diseases

Mambro, T. D., Pellielo, G., Agyapong, E. D., Carinci, M., Chianese, D., Giorgi, C., Morciano, G., Patergnani, S., Pinton, P., & Rimessi, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098181 · Cited by 65 · see citing works

Tom70 Is Essential for PINK1 Import into Mitochondria

Kato, H., Lu, Q.-P., Rapaport, D., & Kozjak-Pavlovic, V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058435 · Cited by 64 · see citing works

Defective insulin signaling and mitochondrial dynamics in diabetic cardiomyopathy

Westermeier, F., Navarro-Márquez, M., López‐Crisosto, C., Bravo-Sagua, R., Quiroga, C., Bustamante, M., Verdejo, H., Ricardo Zalaquett, S., Ibacache, M. E., Parra, V., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.02.005 · Cited by 63 · see citing works

Control of mitochondrial integrity in ageing and disease

Szklarczyk, R., Nooteboom, M., & Osiewacz, H. D. (2014) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2013.0439 · Cited by 61 · see citing works

Mutation or knock-down of 17β-hydroxysteroid dehydrogenase type 10 cause loss of MRPP1 and impaired processing of mitochondrial heavy strand transcripts

Deutschmann, A. J., Amberger, A., Zavadil, C., Steinbeißer, H., Mayr, J. A., Feichtinger, R. G., Oerum, S., Yue, W. W., & Zschocke, J. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu072 · Cited by 61 · see citing works

Antagonistic functions of LMNA isoforms in energy expenditure and lifespan

López‐Mejía, I. C., de Toledo, M., Chavey, C., Lapasset, L., Cavelier, P., Herrera, C. L., Chébli, K., Fort, P., Béranger, G. E., Fajas, L., et al. (2014) · EMBO Reports · doi:10.1002/embr.201338126 · Cited by 59 · see citing works

The interplay between mitochondria and autophagy and its role in the aging process

Schiavi, A., & Ventura, N. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.02.015 · Cited by 59 · see citing works

Genetic and cellular modifiers of oxidative stress: What can we learn from fatty acid oxidation defects?

Olsen, R. K. J., Cornelius, N., & Gregersen, N. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.10.007 · Cited by 58 · see citing works

Mitophagy receptors sense stress signals and couple mitochondrial dynamic machinery for mitochondrial quality control

Wu, H., Wei, H., Sehgal, S. A., Liu, L., & Chen, Q. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.030 · Cited by 57 · see citing works

Mitochondrial Quality Control: A Pathophysiological Mechanism and Therapeutic Target for Stroke

Yang, M., He, Y. T., Deng, S., Xiao, L., Tian, M., Xin, Y., Lu, C., Zhao, F., & Gong, Y. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.786099 · Cited by 56 · see citing works

What are the 100 most cited fungal genera?

Bhunjun, C. S., Chen, Y. J., Phukhamsakda, C., Boekhout, T., Groenewald, J. Z., McKenzi, E. H. C., Francisco, E. C., Frisvad, J. C., Groenewald, M., Hurdeal, V. G., et al. (2024) · Studies in Mycology · doi:10.3114/sim.2024.108.01 · Cited by 57 · see citing works

A-Kinase Anchoring Protein 1: Emerging Roles in Regulating Mitochondrial Form and Function in Health and Disease

Liu, Y., Merrill, R. A., & Strack, S. (2020) · Cells · doi:10.3390/cells9020298 · Cited by 55 · see citing works

Mitochondrial protein quality control in health and disease

Baker, M. J., Palmer, C. S., & Stojanovski, D. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12430 · Cited by 55 · see citing works

Identification of autophagy as a longevity-assurance mechanism in the aging modelPodospora anserina

Knuppertz, L., Hamann, A., Pampaloni, F., Stelzer, E. H. K., & Osiewacz, H. D. (2014) · Autophagy · doi:10.4161/auto.28148 · Cited by 55 · see citing works

Lack of FTSH4 Protease Affects Protein Carbonylation, Mitochondrial Morphology, and Phospholipid Content in Mitochondria of Arabidopsis: New Insights into a Complex Interplay

Smakowska, E., Skibior, R., Czarna, M., Kołodziejczak, M., Kwaśniak-Owczarek, M., Parys, K., Funk, C., & Jańska, H. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00370 · Cited by 51 · see citing works

Disturbed mitochondrial quality control involved in hepatocytotoxicity induced by silica nanoparticles.

Qi, Y., Ma, R., Li, X., Lv, S., Liu, X.-Y., Abulikemu, A., Zhao, X., Li, Y.-B., Guo, C.-X., & Sun, Z. (2020) · Nanoscale · doi:10.1039/d0nr01893g · Cited by 40 · see citing works

Mitophagy: Basic Mechanism and Potential Role in Kidney Diseases

Tang, C., He, L., Liu, J., & Dong, Z. (2015) · Kidney Diseases · doi:10.1159/000381510 · Cited by 50 · see citing works

Short‐chain acyl‐CoA dehydrogenase deficiency: from gene to cell pathology and possible disease mechanisms

Nochi, Z., Olsen, R. K. J., & Gregersen, N. (2017) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-017-0047-1 · Cited by 49 · see citing works

Inhibition of PI3K/mTOR increased the sensitivity of hepatocellular carcinoma cells to cisplatin via interference with mitochondrial‐lysosomal crosstalk

Sheng, J., Shen, L., Sun, L., Zhang, X., Cui, R., & Wang, L. (2019) · Cell Proliferation · doi:10.1111/cpr.12609 · Cited by 49 · see citing works

Mitochondrial translation and dynamics synergistically extend lifespan in C. elegans through HLH-30

Liu, Y. J., McIntyre, R. L., Janssens, G. E., Williams, E. G., Lan, J., van Weeghel, M., Schomakers, B. V., van Veen, H. A., van der Wel, N. N., Yao, P., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201907067 · Cited by 48 · see citing works

Protein Homeostasis at the Plasma Membrane

Apaja, P. M., & Lukács, G. L. (2014) · Physiology · doi:10.1152/physiol.00058.2013 · Cited by 46 · see citing works

Live imaging of alterations in cellular morphology and organelles during cornification using an epidermal equivalent model

Ipponjima, S., Umino, Y., Nagayama, M., & Denda, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-62240-3 · Cited by 46 · see citing works

Orchestrating the network of molecular pathways affecting aging: Role of nonselective autophagy and mitophagy

Knuppertz, L., & Osiewacz, H. D. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.01.003 · Cited by 44 · see citing works

Alcohol induces mitochondrial redox imbalance in alveolar macrophages

Liang, Y., Harris, F. L., Jones, D. P., & Brown, L. A. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.010 · Cited by 44 · see citing works

Epigenetic signature: implications for mitochondrial quality control in human aging

D’Aquila, P., Montesanto, A., Rango, F. D., Guarasci, F., Passarino, G., & Bellizzi, D. (2019) · Aging · doi:10.18632/aging.101832 · Cited by 43 · see citing works

Inhibition of the mitochondria-shaping protein Opa1 restores sensitivity to Gefitinib in a lung adenocarcinomaresistant cell line

Noguchi, M., Kohno, S., Pellattiero, A., Machida, Y., Shibata, K., Shintani, N., Kohno, T., Gotoh, N., Takahashi, C., Hirao, A., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05768-2 · Cited by 43 · see citing works

Mitochondrial‐targeted nitroxides disrupt mitochondrial architecture and inhibit expression of peroxiredoxin 3 and FOXM1 in malignant mesothelioma cells

Cunniff, B., Benson, K., Stumpff, J. K., Newick, K., Held, P., Taatjes, D. J., Joseph, J., Kalyanaraman, B., & Heintz, N. H. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24232 · Cited by 43 · see citing works

Cellular consequences of oxidative stress in riboflavin responsive multiple acyl-CoA dehydrogenation deficiency patient fibroblasts

Cornelius, N., Corydon, T. J., Gregersen, N. V., & Olsen, R. K. J. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu146 · Cited by 43 · see citing works

Mitochondrion-mediated cell death: dissecting yeast apoptosis for a better understanding of neurodegeneration

Braun, R. J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00182 · Cited by 42 · see citing works

Mitochondrial Determinants of Anti-Cancer Drug-Induced Cardiotoxicity

Rocca, C., Francesco, E. M. D., Pasqua, T., Granieri, M. C., Bartolo, A. D., Cantafio, M. E. G., Muoio, M. G., Gentile, M., Neri, A., Angelone, T., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10030520 · Cited by 42 · see citing works

LONP1-mediated mitochondrial quality control safeguards metabolic shifts in heart development

Zhao, K., Huang, X., Zhao, W., Lü, B., & Yang, Z. (2022) · Development · doi:10.1242/dev.200458 · Cited by 40 · see citing works

Tauroursodeoxycholic Acid Enhances Mitochondrial Biogenesis, Neural Stem Cell Pool, and Early Neurogenesis in Adult Rats

Soares, R., Ribeiro, F. F., Xapelli, S., Genebra, T., Ribeiro, M. F., Sebastião, A. M., Rodrigues, C. M. P., & Solá, S. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0592-5 · Cited by 40 · see citing works

Plant mitochondrial retrograde signaling: post-translational modifications enter the stage

Hartl, M., & Finkemeier, I. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00253 · Cited by 40 · see citing works

Regulation and Quantification of Cellular Mitochondrial Morphology and Content

Tronstad, K. J., Nooteboom, M., Nilsson, L. I. H., Nikolaisen, J., Sokolewicz, M., Grefte, S., Pettersen, I. K. N., Dyrstad, S. E., Hoel, F., Willems, P. H. G. M., et al. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305230546 · Cited by 39 · see citing works

Role of Mitochondria-Cytoskeleton Interactions in the Regulation of Mitochondrial Structure and Function in Cancer Stem Cells

Kim, J., & Cheong, J. (2020) · Cells · doi:10.3390/cells9071691 · Cited by 40 · see citing works

Mitochondrial quality control pathways as determinants of metabolic health

Held, N. M., & Houtkooper, R. H. (2015) · BioEssays · doi:10.1002/bies.201500013 · Cited by 128 · see citing works

The mechanism of mammalian mitochondrial quality control system

Khan, S. U., & Khan, M. U. (2021) · Journal of Chemistry and Nutritional Biochemistry · doi:10.48185/jcnb.v2i2.387 · Cited by 6 · see citing works

Impaired quality control of mitochondria: Aging from a new perspective

Weber, T. A., & Reichert, A. S. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.018 · Cited by 110 · see citing works

Mitochondria as a Key Player in Aging

Banerjee, R., & Rath, P. C. (2020) · Springer eBooks · doi:10.1007/978-981-32-9005-1_10

Autophagic responses compensate mitochondrial impairments

Henkel, V., Warnsmann, V., & Osiewacz, H. D. (2017) · Aging · doi:10.18632/aging.101292 · Cited by 2 · see citing works