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

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

Mechanisms of mitophagy

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

Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

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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

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

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 2,026

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

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

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

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

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

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

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

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

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

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

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

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

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

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

Mitochondrial DNA mutations in disease and aging

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

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

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

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 570

Somatic Mitochondrial DNA Mutations in Mammalian Aging

Larsson, N. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-093701 · Cited by 561

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 525

The mitochondrial UPR – protecting organelle protein homeostasis

Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 506

The Matrix Peptide Exporter HAF-1 Signals a Mitochondrial UPR by Activating the Transcription Factor ZC376.7 in C. elegans

Haynes, C. M., Yang, Y., Blais, S. P., Neubert, T. A., & Ron, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.015 · Cited by 504

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

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

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

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

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

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

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 303

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

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

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 274

Molecular Machinery of Mitochondrial Fusion and Fission

Westermann, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800011200 · Cited by 258

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

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 245

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

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

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

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 198

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 195

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 194

Mitochondrial quality control by the ubiquitin–proteasome system

Taylor, E. B., & Rutter, J. P. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391509 · Cited by 188

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

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

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 176

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 171

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 167

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 166

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

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

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

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 147

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

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

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

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 116

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 112

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 105

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

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

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 72

Mitochondrial functions and aging

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

Mitochondrial protein quality control: Implications in ageing

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

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

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 66

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 61

Genetic regulation of aging

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

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

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

Fussy mitochondria fuse in response to stress

van der Bliek, A. M. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.130 · Cited by 47

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

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

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 35

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

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

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

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

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

Mitochondrial dynamics, mitophagy and cardiovascular disease

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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 587

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 555

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 547

Mitochondrial quality control pathways as determinants of metabolic health

Held, N. M., & Houtkooper, R. H. (2015) · BioEssays · doi:10.1002/bies.201500013 · Cited by 133

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

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 112

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