Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

Hydroperoxide metabolism in mammalian organs.

Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works

Protein Oxidation in Aging, Disease, and Oxidative Stress

Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,339 · see citing works

Mitochondrial free radical generation, oxidative stress, and aging

Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · see citing works

Purification and properties

Cox, B. M., Opheim, K. E., Teschemacher, H., & D, A. G. M. (1975) · Life Sciences · doi:10.1016/0024-3205(75)90272-6 · Cited by 1,708 · see citing works

Gene expression profile of aging and its retardation by caloric restriction

Lee, C.-K., Klopp, R. G., Weindruch, R., & Prolla, T. A. (1999) · Science · doi:10.1126/science.285.5432.1390 · Cited by 1,473 · see citing works

Morpholino Antisense Oligomers: Design, Preparation, and Properties

Summerton, J. E., & Weller, D. D. (1997) · Antisense and Nucleic Acid Drug Development · doi:10.1089/oli.1.1997.7.187 · Cited by 1,115 · see citing works

Degradation of oxidized proteins in mammalian cells

Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835 · see citing works

Labeling of proteins by reductive methylation using sodium cyanoborohydride.

Jentoft, N., & Dearborn, D. G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30016-9 · Cited by 771 · see citing works

[42]Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines

Trounce, I. A., Kim, Y. L., Jun, A. S., & Wallace, D. C. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64044-0 · Cited by 749 · see citing works

The oxidative inactivation of mitochondrial electron transport chain components and ATPase.

Zhang, Y., Marcillat, O., Giulivi, C., Ernster, L., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46227-2 · Cited by 713 · see citing works

Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase.

Davies, K. J. A., & Doroshow, J. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35746-0 · Cited by 633 · see citing works

Oxidative damage during aging targets mitochondrial aconitase

Yan, L., Levine, R. L., & Sohal, R. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11168 · Cited by 620 · see citing works

Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical.

Doroshow, J. H., & Davies, K. J. A. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35747-2 · Cited by 542 · see citing works

Superoxide sensitivity of the Escherichia coli aconitase.

Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514 · see citing works

Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein.

Davies, K. J. A., Lin, S. W., & Pacifici, R. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48021-0 · Cited by 481 · see citing works

Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells

Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13399 · Cited by 471 · see citing works

Increased Oxidative Damage Is Correlated to Altered Mitochondrial Function in Heterozygous Manganese Superoxide Dismutase Knockout Mice

Williams, M. D., Remmen, H. V., Conrad, C. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28510 · Cited by 453 · see citing works

Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs.

Gardner, P. R., Nguyen, D., & White, C. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12248 · Cited by 414 · see citing works

Mitochondrial adenine nucleotide translocase is modified oxidatively during aging

Yan, L.-J., & Sohal, R. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.22.12896 · Cited by 414 · see citing works

Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis.

Levine, R. L., Oliver, C. N., Fulks, R. M., & Stadtman, E. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2120 · Cited by 346 · see citing works

Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia

Bradley, J. L. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.275 · Cited by 339 · see citing works

Intracellular proteolytic systems may function as secondary antioxidant defenses: An hypothesis

Davies, K. J. A. (1986) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/s0748-5514(86)80066-6 · Cited by 276 · see citing works

Mitochondrial oxidative damage, hydrogen peroxide release, and aging

Sohal, R. S., & Dubey, A. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90062-0 · Cited by 272 · see citing works

Requirement for the Yeast Gene LON in Intramitochondrial Proteolysis and Maintenance of Respiration

Suzuki, C. K., Suda, K., Wang, N., & Schatz, G. (1994) · Science · doi:10.1126/science.8146662 · Cited by 272 · see citing works

An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide

Kennedy, M. C., Antholine, W. E., & Beinert, H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20340 · Cited by 259 · see citing works

Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria

Lass, A., Sohal, B. H., Weindruch, R. H., Forster, M. J., & Sohal, R. S. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00144-0 · Cited by 251 · see citing works

Peroxynitrite Increases the Degradation of Aconitase and Other Cellular Proteins by Proteasome

Grune, T., Blasig, I. E., Sitte, N., Roloff, B., Haseloff, R., & Davies, K. J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10857 · Cited by 250 · see citing works

Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase.

Rivett, A. J. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38913-5 · Cited by 241 · see citing works

PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae.

van Dyck, L., Pearce, D. A., & Sherman, F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42340-4 · Cited by 233 · see citing works

Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones

Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., & Davies, K. J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6223 · Cited by 229 · see citing works

Age-Related Changes in Protein Oxidation and Proteolysis in Mammalian Cells

Grune, T., Shringarpure, R., Sitte, N., & Davies, K. J. A. (2001) · The Journals of Gerontology Series A · doi:10.1093/gerona/56.11.b459 · Cited by 193 · see citing works

Selectivity of protein oxidative damage during aging in Drosophila melanogaster

Nilanjana, D. A. S., Levine, R. L., Orr, W. C., & Sohal, R. S. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600209 · Cited by 186 · see citing works

A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.

Wang, N., Gottesman, S., Willingham, M. C., Gottesman, M. M., & Maurizi, M. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11247 · Cited by 186 · see citing works

Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part II—aging of nondividing cells

Sitte, N., Merker, K., von Zglinicki, T., Davies, K. J. A., & Grune, T. (2000) · The FASEB Journal · doi:10.1096/fj.00-0210com · Cited by 157 · see citing works

Exposure of Hydrophobic Moieties Promotes the Selective Degradation of Hydrogen Peroxide-Modified Hemoglobin by the Multicatalytic Proteinase Complex, Proteasome

Giulivi, C., Pacifici, R. E., & Davies, K. J. A. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1245 · Cited by 155 · see citing works

Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin

Marcillat, O., Zhang, Y., & Davies, K. J. A. (1989) · Biochemical Journal · doi:10.1042/bj2590181 · Cited by 150 · see citing works

Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria.

Desautels, M., & Goldberg, A. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33815-8 · Cited by 148 · see citing works

[4] Measuring nitric oxide and superoxide: Rate constants for aconitase reactivity

Hausladen, A., & Fridovich, I. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69007-7 · Cited by 137 · see citing works

Liver mitochondria contain an ATP-dependent, vanadate-sensitive pathway for the degradation of proteins.

Desautels, M., & Goldberg, A. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.6.1869 · Cited by 120 · see citing works

Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins

Marcillat, O., Zhang, Y., Lin, S. W., & Davies, K. J. A. (1988) · Biochemical Journal · doi:10.1042/bj2540677 · Cited by 120 · see citing works

Lactacystin, a Specific Inhibitor of the Proteasome, Inhibits Human Platelet Lysosomal Cathepsin A-like Enzyme

Ostrowska, H., Wójcik, C., Ōmura, S., & Worowski, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6434 · Cited by 113 · see citing works

The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondriaPreprint

van Dyck, L., Neupert, W., & Langer, T. (1998) · Genes & Development · doi:10.1101/gad.12.10.1515 · Cited by 102 · see citing works

Protein degradation in mitochondria: implications for oxidative stress, aging and disease:

Bota, D. A., & Davies, K. J. A. (2001) · Mitochondrion · doi:10.1016/s1567-7249(01)00005-8 · Cited by 99 · see citing works

Selectivity of protein oxidative damage during aging in Drosophila melanogaster

Nilanjana, D. A. S., Levine, R. L., Orr, W. C., et al. (2001) · Biochemical Journal · doi:10.1042/bj3600209 · Cited by 99 · see citing works

Oxidatively denaturated proteins are degraded by an ATP-independent proteolytic pathway in escherichia coli

Davies, K. J. A. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90016-0 · Cited by 89 · see citing works

Mitochondrial impairment in the cerebellum of the patients with progressive supranuclear palsy

Park, L. C. H., Albers, D. S., Xu, H., LINDSAY, J. G., Beal, M. F., & Gibson, G. E. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10062 · Cited by 83 · see citing works

Endogenous free radical generation may influence proteolysis in Mitochondria

Dean, R. T., & POLLAK, J. K. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90296-7 · Cited by 73 · see citing works

[5] Preparation of bovine heart mitochondria in high yield

AZZONE, G. F., Colonna, R., & Ziche, B. (1979) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(79)55007-1 · Cited by 60 · see citing works

ATP-dependent protease in bovine adrenal cortex. Tissue specificity, subcellular localization, and partial characterization.

Watabe, S., & Kimura, T. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89052-4 · Cited by 57 · see citing works

Adrenal cortex mitochondrial enzyme with ATP-dependent protease and protein-dependent ATPase activities. Purification and properties.

Watabe, S., & Kimura, T. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38597-6 · Cited by 43 · see citing works

Characteristics of an ATP‐dependent proteolytic system of rat liver mitochondria

Rapoport, S. M., Dubiel, W., & Müller, M. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)81018-1 · Cited by 26 · see citing works

Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP‐dependent Lon proteases

Amerik, A. Y., Petukhova, G. V., Grigorenko, G. M., Lykov, I. P., Yarovoi, S. V., Lipkin, V. M., & Gorbalenya, A. E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80166-5 · Cited by 22 · see citing works

[26] Mitochondrial ATP-dependent protease from rat liver and yeast

Kuzela, S., & Goldberg, A. L. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)44028-x · Cited by 19 · see citing works

Increased activity of surviving locus ceruleus neurons in Alzheimer's disease

Moser (1999) · Pure Amsterdam UMC · doi:10.1002/1531-8249(199901)45:1

Oxidative stress and neurodegeneration: where are we now?

Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614 · see citing works

Sarcopenia: Aging-Related Loss of Muscle Mass and Function

Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works

Ionizing radiation-induced metabolic oxidative stress and prolonged cell injury

Azzam, E. I., Jay‐Gerin, J., & Pain, D. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.12.012 · Cited by 1,611 · see citing works

Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease

Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works

Oxidative stress response and Nrf2 signaling in aging

Zhang, H., Davies, K. J. A., & Forman, H. J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.036 · Cited by 804 · see citing works

Role of oxidative carbonylation in protein quality control and senescence

Nyström, T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600599 · Cited by 791 · see citing works

Oxygen Consumption and Usage During Physical Exercise: The Balance Between Oxidative Stress and ROS-Dependent Adaptive Signaling

Radak, Z. O., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4498 · Cited by 616 · see citing works

New roles for mitochondrial proteases in health, ageing and disease

Quirós, P. M., Langer, T., & López-Otı́n, C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3984 · Cited by 546 · see citing works

Oxidative stress and pulmonary fibrosis

Cheresh, P., Kim, S.-J., Tulasiram, S., & Kamp, D. W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.11.021 · Cited by 527 · 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

Quality control of the mitochondrial proteome

Song, J., Herrmann, J. M., & Becker, T. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00300-2 · Cited by 492 · see citing works

Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging

Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490 · see citing works

Integration of cellular bioenergetics with mitochondrial quality control and autophagy

Hill, B. G., Benavides, G. A., Lancaster, J. R., Ballinger, S. W., Dell’Italia, L., Zhang, J., & Darley-Usmar, V. M. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0198 · Cited by 481 · see citing works

Mitochondrial dysfunction and oxidative stress in Parkinson's disease and monogenic parkinsonism

Hauser, D. N., & Hastings, T. G. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.10.011 · Cited by 470 · see citing works

Mitochondrial quality control: a matter of life and death for neurons

Rugarli, E. I., & Langer, T. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.38 · Cited by 419 · see citing works

The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria

Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works

Stationary-Phase Physiology

Nyström, T. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123818 · Cited by 385 · see citing works

Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis

Dasuri, K., Zhang, L., & Keller, J. N. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.016 · Cited by 371 · see citing works

Cytochrome c oxidase dysfunction in oxidative stress

Srinivasan, S., & Avadhani, N. G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.021 · Cited by 371 · see citing works

Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104pPreprint

Erjavec, N., Larsson, L., Grantham, J., & Nyström, T. (2007) · Genes & Development · doi:10.1101/gad.439307 · Cited by 357 · see citing works

Reconstitution of Mitochondria Derived Vesicle Formation Demonstrates Selective Enrichment of Oxidized Cargo

Soubannier, V., Rippstein, P. U., Kaufman, B. A., Shoubridge, E. A., & McBride, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052830 · Cited by 346 · see citing works

Oxidative DNA damage & repair: An introduction

Cadet, J., & Davies, K. J. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.030 · Cited by 339 · see citing works

Adaptive homeostasis

Davies, K. J. A. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.04.007 · Cited by 330 · see citing works

Phosphorylation of Human TFAM in Mitochondria Impairs DNA Binding and Promotes Degradation by the AAA+ Lon Protease

Lü, B., Lee, J., Nie, X., Li, M., Morozov, Y. I., Venkatesh, S., Bogenhagen, D. F., Temiakov, D., & Suzuki, C. K. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.023 · Cited by 320 · see citing works

The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes

Pickering, A. M., Koop, A. L., Teoh, C., Ermak, G., Grune, T., & Davies, K. J. A. (2010) · Biochemical Journal · doi:10.1042/bj20100878 · Cited by 319 · see citing works

Signaling the mitochondrial unfolded protein response

Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359 · see citing works

Mitochondrial Management of Reactive Oxygen Species

Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 296 · 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

Skeletal muscle mitochondrial remodeling in exercise and diseases

Gan, Z., Fu, T., Kelly, D. P., & Vega, R. B. (2018) · Cell Research · doi:10.1038/s41422-018-0078-7 · Cited by 287 · see citing works

Imaging dynamics of endogenous mitochondrial RNA in single living cells

Ozawa, T., Natori, Y., Sato, M., & Umezawa, Y. (2007) · Nature Methods · doi:10.1038/nmeth1030 · Cited by 282 · see citing works

Nrf2-dependent Induction of Proteasome and Pa28αβ Regulator Are Required for Adaptation to Oxidative Stress

Pickering, A. M., Linder, R. A., Zhang, H., Forman, H. J., & Davies, K. J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277145 · Cited by 280 · see citing works

Quality Control of Mitochondrial ProteostasisPreprint

Baker, M. J., Tatsuta, T., & Langer, T. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007559 · Cited by 260 · see citing works

Protein damage, repair and proteolysis

Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 254 · 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

Redox crosstalk at endoplasmic reticulum (ER) membrane contact sites (MCS) uses toxic waste to deliver messages

Yoboue, E. D., Sitia, R., & Simmen, T. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0033-4 · Cited by 238 · see citing works

The role of oxidative stress in anxiety disorder: cause or consequence?

Fedoce, A. G., Ferreira, F. R., Bota, R. G., Bonet-Costa, V., Sun, P. Y., & Davies, K. J. A. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1475733 · Cited by 235 · see citing works

Radical medicine: treating ageing to cure disease

Finkel, T. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1763 · Cited by 234 · see citing works

Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress

Bota, D. A., Van Remmen, H., & Davies, K. J. A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03638-4 · Cited by 233 · see citing works

Skeletal muscle aging and the mitochondrion

Johnson, M. L., Robinson, M. M., & Nair, K. S. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.12.003 · Cited by 233 · see citing works

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 · see citing works

Redox regulation of antioxidants, autophagy, and the response to stress: Implications for electrophile therapeutics

Levonen, A., Hill, B. G., Kansanen, E., Zhang, J., & Darley-Usmar, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.025 · Cited by 232 · see citing works

Adaptive homeostasis and the free radical theory of ageing

Pomatto, L. C. D., & Davies, K. J. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.016 · Cited by 224 · see citing works

Oxidized protein degradation and repair in ageing and oxidative stress

Friguet, B. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.028 · Cited by 222 · see citing works

Chaperone–protease networks in mitochondrial protein homeostasis

Voos, W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.06.005 · Cited by 221 · see citing works

A switch in metabolism precedes increased mitochondrial biogenesis in respiratory chain-deficient mouse hearts

Hansson, A., Hance, N., Dufour, E., Rantanen, A., Hultenby, K., Clayton, D. A., Wibom, R., & Larsson, N.-G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308710100 · Cited by 220 · see citing works

Molecular basis of asbestos-induced lung disease

Liu, G., Cheresh, P., & Kamp, D. W. (2013) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163942 · Cited by 213 · see citing works

Normoxic Resuscitation after Cardiac Arrest Protects against Hippocampal Oxidative Stress, Metabolic Dysfunction, and Neuronal Death

Vereczki, V., Martin, E., Rosenthal, R. E., Hof, P. R., Hoffman, G. E., & Fiskum, G. M. (2005) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600234 · Cited by 213 · see citing works

Mitochondrial quality control and communications with the nucleus are important in maintaining mitochondrial function and cell health

Kotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 212 · see citing works

The Mitochondrial Lon Protease Is Required for Age-Specific and Sex-Specific Adaptation to Oxidative Stress

Pomatto, L. C. D., Carney, C., Shen, B., Wong, S., Halaszynski, K., Salomon, M. P., Davies, K. J. A., & Tower, J. (2016) · Current Biology · doi:10.1016/j.cub.2016.10.044 · Cited by 211 · see citing works

Oxygen-sensitive mitochondrial accumulation of cystathionine β-synthase mediated by Lon protease

Teng, H., Wu, B., Zhao, K., Yang, G., Wu, L., & Wang, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308487110 · Cited by 210 · see citing works

Biological roles of the Lon ATP-dependent protease

Tsilibaris, V., Maenhaut-Michel, G., & Melderen, L. V. (2006) · Research in Microbiology · doi:10.1016/j.resmic.2006.05.004 · Cited by 207 · 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

Aconitase post-translational modification as a key in linkage between Krebs cycle, iron homeostasis, redox signaling, and metabolism of reactive oxygen species

Lushchak, O. V., Piroddi, M., Galli, F., & Lushchak, V. I. (2013) · Redox Report · doi:10.1179/1351000213y.0000000073 · Cited by 195 · 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

Protein Homeostasis in Models of Aging and Age-Related Conformational Disease

Kikis, E. A., Gidalevitz, T., & Morimoto, R. I. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_11 · Cited by 187 · see citing works

Accumulation of altered proteins and ageing: Causes and effects☆

Hipkiss, A. R. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.03.004 · Cited by 185 · see citing works

Stress-responsive regulation of mitochondria through the ER unfolded protein response

Rainbolt, T. K., Saunders, J. M., & Wiseman, R. L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.06.007 · Cited by 183 · see citing works

Disruption of mitochondrial redox circuitry in oxidative stress

Jones, D. P. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.008 · Cited by 176 · see citing works

Cell penetrating peptide conjugates of steric block oligonucleotides

Lebleu, B., Moulton, H. M., Abes, R., Ivanova, G. D., Abes, S., Stein, D. A., Iversen, P. L., Arzumanov, A. A., & Gait, M. J. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.09.002 · Cited by 175 · see citing works

Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress

Poppek, D., Keck, S., Ermak, G., Jung, T., Stolzing, A., Ullrich, O., Davies, K. J. A., & Grune, T. (2006) · Biochemical Journal · doi:10.1042/bj20060463 · Cited by 174 · see citing works

Rapid and Selective Oxygen-regulated Protein Tyrosine Denitration and Nitration in Mitochondria

Koeck, T., Fu, X., Hazen, S. L., Crabb, J. W., Stuehr, D. J., & Aulak, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401586200 · Cited by 172 · 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

Roles of mitochondria in human disease

Duchen, M. R., & Szabadkai, G. (2010) · Essays in Biochemistry · doi:10.1042/bse0470115 · Cited by 167 · see citing works

DNA and RNA Binding by the Mitochondrial Lon Protease Is Regulated by Nucleotide and Protein Substrate

Liu, T., Lü, B., Lee, I., Ondrovičová, G., Kutějová, E., & Suzuki, C. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309642200 · Cited by 166 · see citing works

The ageing neuromuscular system and sarcopenia: A mitochondrial perspective

Rygiel, K. A., Picard, M., & Turnbull, D. M. (2016) · The Journal of Physiology · doi:10.1113/jp271212 · Cited by 165 · see citing works

CODAS Syndrome Is Associated with Mutations of LONP1, Encoding Mitochondrial AAA+ Lon Protease

Strauss, K. A., Jinks, R. N., Puffenberger, E. G., Venkatesh, S., Singh, K., Cheng, I., Mikita, N., Thilagavathi, J., Lee, J., Sarafianos, S. G., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.12.003 · Cited by 163 · see citing works

Multitasking in the mitochondrion by the ATP-dependent Lon protease

Venkatesh, S., Lee, J., Singh, K., Lee, I., & Suzuki, C. K. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.003 · Cited by 160 · see citing works

Staying cool in difficult times: Mitochondrial dynamics, quality control and the stress response

Shutt, T. E., & McBride, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.024 · Cited by 160 · see citing works

Mitochondrial protein oxidation and degradation in response to oxidative stress and aging

Bulteau, A., Szweda, L. I., & Friguet, B. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.03.013 · Cited by 159 · see citing works

Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis

Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 158 · see citing works

Tissue-specific changes of mitochondrial functions in aged rats: Effect of a long-term dietary treatment with N-acetylcysteine

Cocco, T., Sgobbo, P., Clemente, M. T., Lopriore, B., Grattagliano, I., Paola, M. D., & Villani, G. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.034 · Cited by 157 · see citing works

Age-Associated declines in mitochondrial biogenesis and protein quality control factors are minimized by exercise training

Koltai, E., Hart, N., Taylor, A. W., Goto, S., Ngo, J. K., Davies, K. J. A., & Radak, Z. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00337.2011 · Cited by 152 · see citing works

Oxidative stress adaptation with acute, chronic, and repeated stress

Pickering, A. M., Vojtovich, L., Tower, J., & Davies, K. J. A. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.001 · Cited by 152 · see citing works

Artemisinins ameliorate polycystic ovarian syndrome by mediating LONP1-CYP11A1 interaction

Liu, Y., Jiang, J., Du, S.-Y., Mu, L., Fan, J., Hu, J., Yao, Y., Ding, M., Zhou, W.-Y., Yu, Q., et al. (2024) · Science · doi:10.1126/science.adk5382 · Cited by 151 · see citing works

Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease

Bender, T., Lewrenz, I., Franken, S., Baitzel, C., & Voos, W. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0718 · Cited by 150 · see citing works

Mitochondrial contribution to lipofuscin formation

König, J., Ott, C., Hugo, M., Jung, T., Bulteau, A., Grune, T., & Höhn, A. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.017 · Cited by 150 · 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

Mitochondrial Lon protease in human disease and aging: Including an etiologic classification of Lon-related diseases and disorders

Bota, D. A., & Davies, K. J. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.031 · Cited by 148 · see citing works

Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins

Pickering, A. M., & Davies, K. J. A. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.04.018 · Cited by 147 · see citing works

Elimination of damaged proteins during differentiation of embryonic stem cells

Hernebring, M., Brolén, G., Aguilaniu, H., Semb, H., & Nyström, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510944103 · Cited by 146 · see citing works

Rules Governing Selective Protein Carbonylation

Maisonneuve, E., Ducret, A., Khoueiry, P., Lignon, S., Longhi, S., Talla, E., & Dukan, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007269 · Cited by 145 · see citing works

Redox Regulation of Homeostasis and Proteostasis in Peroxisomes

Walker, C. L., Pomatto, L. C. D., Tripathi, D. N., & Davies, K. J. A. (2017) · Physiological Reviews · doi:10.1152/physrev.00033.2016 · Cited by 145 · see citing works

Reactive Oxygen Species–Mediated Mitochondria-to-Nucleus Signaling: A Key to Aging and Radical-Caused Diseases

Störz, P. (2006) · Science s STKE · doi:10.1126/stke.3322006re3 · Cited by 144 · see citing works

Overexpression of Lon contributes to survival and aggressive phenotype of cancer cells through mitochondrial complex I-mediated generation of reactive oxygen species

Cheng, C.-W., Kuo, C.-Y., Fan, C.-C., Fang, W.-C., Jiang, S. S., Yk, L., Wang, T.-Y., Kao, M.-C., & Lee, A. Y.-L. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.204 · Cited by 141 · see citing works

Turnover of Mitochondrial Steroidogenic Acute Regulatory (StAR) Protein by Lon Protease: The Unexpected Effect of Proteasome Inhibitors

Granot, Z., Kobiler, O., Melamed‐Book, N., Eimerl, S., Bahat, A., Lü, B., Braun, S., Maurizi, M. R., Suzuki, C. K., Oppenheim, A. B., et al. (2007) · Molecular Endocrinology · doi:10.1210/me.2005-0458 · Cited by 139 · see citing works

Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging

Ngo, J. K., Pomatto, L. C. D., & Davies, K. J. A. (2013) · Redox Biology · doi:10.1016/j.redox.2013.01.015 · Cited by 138 · see citing works

The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives

Bernstein, S. H., Venkatesh, S., Li, M., Lee, J., Lü, B., Hilchey, S. P., Morse, K. M., Metcalfe, H. M., Skalska, J., Andreeff, M., et al. (2012) · Blood · doi:10.1182/blood-2011-02-340075 · Cited by 137 · see citing works

The ATPase Inhibitory Factor 1 (IF1): A master regulator of energy metabolism and of cell survival

García-Bermúdez, J., & Cuezva, J. M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.004 · Cited by 137 · 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

Ubiquitin-Dependent Degradation of Mitochondrial Proteins Regulates Energy Metabolism

Lavie, J., Belvalet, H. D., Sonon, S., Ion, A. M., Dumon, E., Melser, S., Lacombe, D., Dupuy, J., Lalou, C., & Bénard, G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.013 · Cited by 136 · see citing works

LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding

Shin, C.-S., Meng, S., Garbis, S. D., Moradian, A., Taylor, R. W., Sweredoski, M. J., Lomenick, B., & Chan, D. C. (2021) · Nature Communications · doi:10.1038/s41467-020-20597-z · Cited by 135 · 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

Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion

Bulteau, A., Lundberg, K. C., Ikeda‐Saito, M., Isaya, G., & Szweda, L. I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501519102 · Cited by 131 · see citing works

Mitochondrial AAA proteases — Towards a molecular understanding of membrane-bound proteolytic machines

Gerdes, F., Tatsuta, T., & Langer, T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.015 · Cited by 128 · see citing works

Cleavage Site Selection within a Folded Substrate by the ATP-dependent Lon Protease

Ondrovičová, G., Liu, T., Singh, K., Tian, B., Hong Li, A., Gakh, O., Perečko, D., Janata, J., Granot, Z., Orly, J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502796200 · Cited by 123 · see citing works

Changes in rat liver mitochondria with aging

Bakala, H., Delaval, E., Hamelin, M., Bismuth, J., Borot, C., Corman, B., & Friguet, B. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03598.x · Cited by 122 · see citing works

Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates

Lee, I., & Suzuki, C. K. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.02.010 · Cited by 119 · see citing works

Novel Mechanisms for Heme-dependent Degradation of ALAS1 Protein as a Component of Negative Feedback Regulation of Heme Biosynthesis

Kubota, Y., Nomura, K., Katoh, Y., Yamashita, R., Kaneko, K., & Furuyama, K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.719161 · Cited by 118 · see citing works

Effects of polystyrene nanoplastics on Ctenopharyngodon idella (grass carp) after individual and combined exposure with zinc oxide nanoparticles

Estrela, F. N., Guimarães, A. T. B., Silva, F. G., da Luz, T. M., Silva, A. M., Pereira, P. S., & Malafaia, G. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.123879 · Cited by 118 · see citing works

Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer

Pinti, M., Gibellini, L., Liu, Y., Xu, S., Lü, B., & Cossarizza, A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2039-3 · Cited by 117 · see citing works

Importance of the Lon Protease in Mitochondrial Maintenance and the Significance of Declining Lon in Aging

Ngo, J. K., & Davies, K. J. A. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1404.015 · Cited by 104 · see citing works

Determination of Aconitase Activity: A Substrate of the Mitochondrial Lon Protease

Quirós, P. M. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7595-2_5 · Cited by 16 · see citing works

The human Lon protease in mitochondrial stress protection and aging

Ngo, J. K. (2015) · University of Southern California Digital Library · doi:10.25549/usctheses-m1314

Age‐related impairment of mitochondrial matrix aconitase and ATP‐stimulated protease in rat liver and heart

Delaval, E., Perichon, M., & Friguet, B. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04422.x · Cited by 82 · see citing works

Effects of Lon protease down-regulation on the mitochondrial function and proteome

Hamon, M., Bayot, A., Gareil, M., Chavatte, L., Lombès, A., Friguet, B., & Bulteau, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.767 · Cited by 2 · see citing works