Lipofuscin: mechanisms of age-related accumulation and influence on cell function12 1Guest Editor: Rajindar S. Sohal 2This article is part of a series of reviews on “Oxidative Stress and Aging.” The full list of papers may be found on the homepage of the journal.

Aging: a theory based on free radical and radiation chemistry

Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567

The Free Radical Theory of Aging Matures

BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879

Autophagy as a Regulated Pathway of Cellular Degradation

Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630

Functions of Lysosomes

de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033

Chain Migration of Neuronal Precursors

Lois, C., García-Verdugo, J.-M., & Alvarez-Buylla, A. (1996) · Science · doi:10.1126/science.271.5251.978 · Cited by 1,331

LYSOSOMAL STORAGE DISEASES

Neufeld, E. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.001353 · Cited by 924

The mitochondrial‐lysosomal axis theory of aging

Brunk, U. T., & Terman, A. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02869.x · Cited by 729

Lysosomal Storage Diseases

Pastores, G. M. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4377-0435-8.00036-6 · Cited by 641

The lipofuscin fluorophore A2E mediates blue light-induced damage to retinal pigmented epithelial cells.

Sparrow, J. R., Nakanishi, K., & Parish, C. A. (2000) · PubMed · Cited by 566

Retinal age pigments generated by self-assembling lysosomotropic detergents

Eldred, G., & Lasky, M. R. (1993) · Nature · doi:10.1038/361724a0 · Cited by 489

The Aging of Iron Man

Ashraf, A., Clark, M., & So, P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00065 · Cited by 163

In Caenorhabditis elegans Nanoparticle-Bio-Interactions Become Transparent: Silica-Nanoparticles Induce Reproductive Senescence

Pluskota, A., Horzowski, E., Bossinger, O., & von Mikecz, A. H. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006622 · Cited by 156

Tearful relations: oxidative stress, inflammation and eye diseases

Wakamatsu, T. H., Doğru, M., & Tsubota, K. (2008) · Arquivos Brasileiros de Oftalmologia · doi:10.1590/s0004-27492008000700015 · Cited by 157

Autophagic and lysosomal reactions to stress in the hepatopancreas of blue mussels

Moore, M. N., Viarengo, A., Donkin, P., & Hawkins, A. J. S. (2007) · Aquatic Toxicology · doi:10.1016/j.aquatox.2007.06.007 · Cited by 154

Autofluorescence as a measure of senescence in C. elegans: look to red, not blue or green

Pincus, Z., Mazer, T. C., & Slack, F. J. (2016) · Aging · doi:10.18632/aging.100936 · Cited by 153

Cellular biomarkers for monitoring estuarine environments: Transplanted versus native mussels

Nigro, M., Falleni, A., Barga, I. D., Scarcelli, V., Lucchesi, P., Regoli, F., & Frenzilli, G. (2006) · Aquatic Toxicology · doi:10.1016/j.aquatox.2005.12.013 · Cited by 151

Microglial degeneration in the aging brain - bad news for neurons?

Streit, W. (2008) · Frontiers in Bioscience · doi:10.2741/2937 · Cited by 150

Oxidative Stress and Autophagy in the Regulation of Lysosome-Dependent Neuron Death

Pivtoraiko, V. N., Stone, S. L., Roth, K. A., & Shacka, J. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2263 · Cited by 154

Oxidative stress and mitochondrial impairment can be separated from lipofuscin accumulation in aged human skeletal muscle

Hütter, E., Skovbro, M., Lener, B., Prats, C., Rabøl, R., Dela, F., & Jansen‐Dürr, P. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00282.x · Cited by 149

Characterization of mussel gill cells in vivo and in vitro

Gómez-Mendikute, A., Elizondo, M., Venier, P., & Cajaraville, M. P. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-1093-9 · Cited by 149

The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases

Nixon, R. A. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140443 · Cited by 149

Iron homeostasis and organismal aging

Zeidan, R. S., Han, S. M., Leeuwenburgh, C., & Xiao, R. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101510 · Cited by 155

Multigenerational Study of Gold Nanoparticles inCaenorhabditis elegans: Transgenerational Effect of Maternal Exposure

Kim, S. W., Kwak, J. I., & An, Y. (2013) · Environmental Science & Technology · doi:10.1021/es304511z · Cited by 147

Mitochondrial recycling and aging of cardiac myocytes: the role of autophagocytosis

Terman, A., Dalen, H., Eaton, J. W., Neužil, J., & Brunk, U. T. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00114-1 · Cited by 147

Autophagy as a second level protective process in conferring resistance to environmentally-induced oxidative stress

Moore, M. N. (2008) · Autophagy · doi:10.4161/auto.5528 · Cited by 147

Hepatic lipid metabolism and non-alcoholic fatty liver disease in aging

Gong, Z., Tas, E., Yakar, S., & Muzumdar, R. H. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.12.022 · Cited by 153

Increased Oxidative Stress and Cardiomyocyte Myofibrillar Degeneration in Patients With Chronic Isolated Mitral Regurgitation and Ejection Fraction >60%

Ahmed, M. I., Gladden, J. D., Litovsky, S. H., Lloyd, S. G., Gupta, H., Inusah, S., Denney, T. S., Powell, P. C., McGiffin, D. C., & Dell’Italia, L. J. (2010) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2009.08.074 · Cited by 141

Autophagy as a cell-repair mechanism: Activation of chaperone-mediated autophagy during oxidative stress

Kaushik, S., & Cuervo, A. M. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.007 · Cited by 145

New aspects of altitude adaptation in Tibetans: a proteomic approach

Gelfi, C., Palma, S. D., Ripamonti, M., Wait, R., Eberini, I., Bajracharya, A., Marconi, C., Schneider, A., Hoppeler, H. H., & Cerretelli, P. (2004) · The FASEB Journal · doi:10.1096/fj.03-1077fje · Cited by 143

Neovascular Macular Degeneration: A Review of Etiology, Risk Factors, and Recent Advances in Research and Therapy

Pugazhendhi, A., Hubbell, M., Jairam, M. P., & Ambati, B. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031170 · Cited by 148

Anthranilate Fluorescence Marks a Calcium-Propagated Necrotic Wave That Promotes Organismal Death in C. elegans

Coburn, C., Allman, E. L., Mahanti, P., Benedetto, A., Cabreiro, F., Pincus, Z., Matthijssens, F., Araiz, C., Mandel, A., Vlachos, M., et al. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001613 · Cited by 154

Oxidative modifications, mitochondrial dysfunction, and impaired protein degradation in Parkinson's disease: how neurons are lost in the Bermuda triangle

Malkus, K. A., Tsika, E., & Ischiropoulos, H. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-24 · Cited by 144

Lipids and lipid peroxidation products in the pathogenesis of age-related macular degeneration

Kopitz, J., Holz, F. G., Kaemmerer, E., & Schütt, F. (2004) · Biochimie · doi:10.1016/j.biochi.2004.09.029 · Cited by 140

Forced turnover of aged microglia induces an intermediate phenotype but does not rebalance CNS environmental cues driving priming to immune challenge

O’Neil, S. M., Witcher, K. G., McKim, D. B., & Godbout, J. P. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0636-8 · Cited by 138

The role of oxidative damage in mitochondria during aging: a review

Huang, H. (2004) · Frontiers in bioscience · doi:10.2741/1298 · Cited by 136

The Role of Osteocytes in Age-Related Bone Loss

Jilka, R. L., & O’Brien, C. A. (2016) · Current Osteoporosis Reports · doi:10.1007/s11914-016-0297-0 · Cited by 141

Lipid-laden cells differentially distributed in the aging brain are functionally active and correspond to distinct phenotypes

Shimabukuro, M. K., Langhi, L. G. P., Cordeiro, I., Brito, J. M., Batista, C. M. D. C., Mattson, M. P., & de Mello Coelho, V. (2016) · Scientific Reports · doi:10.1038/srep23795 · Cited by 136

Role of the inflammation-autophagy-senescence integrative network in osteoarthritis

Vinatier, C., Domínguez, E., Guicheux, J., & Caramés, B. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00706 · Cited by 135

Aging of Cardiac Myocytes in Culture: Oxidative Stress, Lipofuscin Accumulation, and Mitochondrial Turnover

Terman, A., Dalen, H., Eaton, J. W., Neužil, J., & BRUNK, U. T. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.015 · Cited by 135

Clinical oxidation parameters of aging

Voß, P., & Siems, W. (2006) · Free Radical Research · doi:10.1080/10715760600953859 · Cited by 134

Crosstalk between Hsp70 molecular chaperone, lysosomes and proteasomes in autophagy‐mediated proteolysis in human retinal pigment epithelial cells

Ryhänen, T., Hyttinen, J. M. T., Kopitz, J., Rilla, K., Kuusisto, E., Mannermaa, E., Viiri, J., Holmberg, C. I., Immonen, I., Meri, S., et al. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00577.x · Cited by 131

Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging

Cuanalo-Contreras, K., Mukherjee, A., & Soto, C. A. (2013) · International Journal of Cell Biology · doi:10.1155/2013/638083 · Cited by 137

Aluminium-induced electrophysiological, biochemical and cognitive modifications in the hippocampus of aging rats.

Sethi, P., Jyoti, A., Singh, R., Hussain, E., & Sharma, D. (2008) · Neurotoxicology · doi:10.1016/j.neuro.2008.08.005 · Cited by 140

Pathophysiological importance of aggregated damaged proteins

Höhn, A., Jung, T., & Grune, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.028 · Cited by 130

Sudan Black B, The Specific Histochemical Stain for Lipofuscin: A Novel Method to Detect Senescent Cells

Evangelou, K., & Gorgoulis, V. G. (2017) · Methods in Molecular Biology · doi:10.1007/978-1-4939-6670-7_10 · Cited by 124

Rescue of the Stargardt phenotype in Abca4 knockout mice through inhibition of vitamin A dimerization

Charbel Issa, P., Barnard, A. R., Herrmann, P., Washington, I., & MacLaren, R. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506960112 · Cited by 124

Adjustment of the lysosomal-mitochondrial axis for control of cellular senescence

Park, J. T., Lee, Y.-S., Cho, K. A., & Park, S. C. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.08.003 · Cited by 123

Aging, lipofuscin formation, and free radical-mediated inhibition of cellular proteolytic systems

Szweda, P. A., Camouse, M. M., Lundberg, K. C., Oberley, T. D., & Szweda, L. I. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00028-x · Cited by 123

Phospholipid transfer protein (PLTP) deficiency reduces brain vitamin E content and increases anxiety in mice.

Desrumaux, C., Risold, P.-Y., Schroeder, H., Deckert, V., Masson, D., Athias, A., Laplanche, H., Le Guern, N., Blache, D., Jiang, X.-C., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2400fje · Cited by 122

Bacopa monniera prevents from aluminium neurotoxicity in the cerebral cortex of rat brain

Jyoti, A., Sethi, P., & Sharma, D. (2007) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2006.10.037 · Cited by 119

Cushing's Syndrome and Fetal Features Resurgence in Adrenal Cortex–Specific Prkar1a Knockout Mice

Sahut‐Barnola, I., de Joussineau, C., Val, P., Lambert-Langlais, S., Damon‐Soubeyrand, C., Lefrançois‐Martinez, A., Pointud, J., Marceau, G., Sapin, V., Tissier, F., et al. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000980 · Cited by 118

Comparative pathology in bivalves: Aetiological agents and disease processes

Carella, F., Feist, S. W., Bignell, J. P., & Vico, G. D. (2015) · Journal of Invertebrate Pathology · doi:10.1016/j.jip.2015.07.012 · Cited by 117

Redox Activity Within the Lysosomal Compartment: Implications for Aging and Apoptosis

Kurz, T., Eaton, J. W., & Brunk, U. T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3005 · Cited by 121

Autofluorescence is a Reliable in vitro Marker of Cellular Senescence in Human Mesenchymal Stromal Cells

Bertolo, A., Baur, M., Guerrero, J., Pötzel, T., & Stoyanov, J. V. (2019) · Scientific Reports · doi:10.1038/s41598-019-38546-2 · Cited by 116

Aging as a catabolic malfunction

Terman, A., & Brunk, U. T. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.03.009 · Cited by 117

Proteasome Function in Aging and Oxidative Stress: Implications in Protein Maintenance Failure

Farout, L., & Friguet, B. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.205 · Cited by 118

Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins

Powell, S. R., Wang, P., Divald, A., Teichberg, S., Haridas, V., McCloskey, T. W., Davies, K. J. A., & Katzeff, H. L. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.01.003 · Cited by 113

Rapamycin reverses age-related increases in mitochondrial ROS production at complex I, oxidative stress, accumulation of mtDNA fragments inside nuclear DNA, and lipofuscin level, and increases autophagy, in the liver of middle-aged mice

Martínez-Cisuelo, V., Gómez, J., García-Junceda, I., Naudí, A., Cabré, R., Mota‐Martorell, N., Lopez‐Torres, M., González-Sánchez, M., Pamplona, R., & Barja, G. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.08.002 · Cited by 111

Role of macrophages in age-related oxidative stress and lipofuscin accumulation in mice

Vida, C., de Toda, I. M., Cruces, J., Garrido, A., González-Sánchez, M., & la Fuente, M. D. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.005 · Cited by 110

Autophagy: Role in surviving environmental stress

Moore, M. N., Allen, J. I., & Somerfield, P. J. (2006) · Marine Environmental Research · doi:10.1016/j.marenvres.2006.04.055 · Cited by 110

Cell-based therapeutic strategies for replacement and preservation in retinal degenerative diseases

Jones, M. K., Lü, B., Girman, S., & Wang, S. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.01.004 · Cited by 114

Bestrophinopathy: An RPE-photoreceptor interface disease

Guziewicz, K. E., Sinha, D., Gómez, N. M., Zorych, K., Dutrow, E. V., Dhingra, A., Mullins, R. F., Stone, E. M., Gamm, D. M., Boesze‐Battaglia, K., et al. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.01.005 · Cited by 109

Age-dependent alterations in mouse exorbital lacrimal gland structure, innervation and secretory response

Ríos, J. D., Horikawa, Y., Chen, L., Kublin, C. L., Hodges, R. R., Dartt, D. A., & Zoukhri, D. (2004) · Experimental Eye Research · doi:10.1016/j.exer.2004.10.012 · Cited by 109

Senescence-associated phenotypes in Akita diabetic mice are enhanced by absence of bradykinin B2 receptors

Kakoki, M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci26958 · Cited by 107

Lipofuscin: Detection and Quantification by Microscopic Techniques

Jung, T., Höhn, A., & Grune, T. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-411-1_13 · Cited by 108

Depletion of type IA regulatory subunit (RIα) of protein kinase A (PKA) in mammalian cells and tissues activates mTOR and causes autophagic deficiency

Mavrakis, M., Lippincott‐Schwartz, J., Stratakis, C. A., & Bossis, I. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl239 · Cited by 107

The kallikrein-kinin system in health and in diseases of the kidney

Kakoki, M., & Smithies, O. (2009) · Kidney International · doi:10.1038/ki.2008.647 · Cited by 106

Spectroscopic and morphological studies of human retinal lipofuscin granules

Haralampus-Grynaviski, N. M., Lamb, L. E., Clancy, C. M. R., Skumatz, C., Burke, J. M., Sarna, T., & Simon, J. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630280100 · Cited by 104

Label-Free Optical Metabolic Imaging in Cells and Tissues

Georgakoudi, I., & Quinn, K. P. (2023) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071516-044730 · Cited by 109

Functional Aging and Gradual Senescence in Zebrafish

Kishi, S. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.097 · Cited by 103

Mitochondrial damage and intralysosomal degradation in cellular aging

Terman, A., Gustafsson, B., & Brunk, U. T. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.006 · Cited by 103

Low Density Lipoprotein Undergoes Oxidation Within Lysosomes in Cells

Wen, Y., & Leake, D. S. (2007) · Circulation Research · doi:10.1161/circresaha.107.151704 · Cited by 103

Autophagy Gene Atg16l1 Prevents Lethal T Cell Alloreactivity Mediated by Dendritic Cells

Hubbard-Lucey, V. M., Shono, Y., Maurer, K., West, M. L., Singer, N. V., Ziegler, C. G. K., Lezcano, C., Motta, A. C. F., Schmid, K., Levi, S. M., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.09.011 · Cited by 102

Fast, robust and effective decellularization of whole human livers using mild detergents and pressure controlled perfusion

Willemse, J., Verstegen, M. M. A., Vermeulen, A., Schurink, I. J., Roest, H. P., van der Laan, L. J. W., & de Jonge, J. (2020) · Materials Science and Engineering: C · doi:10.1016/j.msec.2019.110200 · Cited by 102

MicroRNA miR-29 controls a compensatory response to limit neuronal iron accumulation during adult life and aging

Ripa, R., Dolfi, L., Terrigno, M., Pandolfini, L., Savino, A., Arcucci, V., Groth, M., Tozzini, E. T., Baumgart, M., & Cellerino, A. (2017) · BMC Biology · doi:10.1186/s12915-017-0354-x · Cited by 109

Blue light effect on retinal pigment epithelial cells by display devices

Moon, J., Yun, J., Yoon, Y. D., Park, S.-I., Seo, Y.-J., Park, W., Chu, H. Y., Park, K. H., Lee, M. Y., Lee, C. W., et al. (2017) · Integrative Biology · doi:10.1039/c7ib00032d · Cited by 101

Retinal pigment epithelium in the pathogenesis of age‐related macular degeneration and photobiomodulation as a potential therapy?

Ao, J., Wood, J. P. M., Chidlow, G., Gillies, M. C., & Casson, R. J. (2017) · Clinical and Experimental Ophthalmology · doi:10.1111/ceo.13121 · Cited by 104

Interactive effects of temperature and salinity on shell formation and general condition in Baltic Sea Mytilus edulis and Arctica islandica

Hiebenthal, C., Philipp, E. E. R., Eisenhauer, A., & Wahl, M. (2011) · Aquatic Biology · doi:10.3354/ab00405 · Cited by 100

Myocardial lipofuscin accumulation in ageing and sudden cardiac death

Kakimoto, Y., Okada, C., Kawabe, N., Sasaki, A., Tsukamoto, H., Nagao, R., & Osawa, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-40250-0 · Cited by 103

A Hereditary Spastic Paraplegia Mouse Model Supports a Role of ZFYVE26/SPASTIZIN for the Endolysosomal System

Khundadze, M., Kollmann, K., Koch, N., Biskup, C. U., Nietzsche, S., Zimmer‐Bensch, G., Hennings, J. C., Huebner, A. K., Symmank, J., Jahić, A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003988 · Cited by 100

Myocyte aging and mitochondrial turnover

Terman, A., & Brunk, U. T. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.01.005 · Cited by 102

Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations

Kuzu, O. F., Granerud, L. J. T., & Saatcioglu, F. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02439-w · Cited by 128

Iron Accumulation during Cellular Senescence

KILLILEA, D. W., WONG, S. L., CAHAYA, H. S., ATAMNA, H., & AMES, B. N. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.063 · Cited by 97

Status of mTOR Activity May Phenotypically Differentiate Senescence and Quiescence

Cho, S., & Hwang, E. S. (2012) · Molecules and Cells · doi:10.1007/s10059-012-0042-1 · Cited by 106

Intralysosomal Iron Induces Lysosomal Membrane Permeabilization and Cathepsin D–Mediated Cell Death in Trabecular Meshwork Cells Exposed to Oxidative Stress

Lin, Y., Epstein, D. L., & Liton, P. B. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5410 · Cited by 97

Blue light induced A2E oxidation in rat eyes — experimental animal model of dry AMD

Wielgus, A. R., Collier, R. J., Martin, E. A., Lih, F. B., Tomer, K. B., Chignell, C. F., & Roberts, J. E. (2010) · Photochemical & Photobiological Sciences · doi:10.1039/c0pp00133c · Cited by 97

Coenzyme Q10 Depletion in Medical and Neuropsychiatric Disorders: Potential Repercussions and Therapeutic Implications

Morris, G., Anderson, G., Berk, M., & Maes, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8477-8 · Cited by 96

Oxidative Stress-Induced Cellular Senescence: Is Labile Iron the Connecting Link?

Nousis, L., Kanavaros, P., & Barbouti, A. (2023) · Antioxidants · doi:10.3390/antiox12061250 · Cited by 103

PGC-1α activity in nigral dopamine neurons determines vulnerability to α-synuclein

Ciron, C., Zheng, L., Bobela, W., Knott, G. W., Leone, T. C., Kelly, D. P., & Schneider, B. L. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0200-8 · Cited by 98

The Role of Autophagy in Chondrocyte Metabolism and Osteoarthritis: A Comprehensive Research Review

Luo, P., Gao, F., Niu, D., Sun, X., Song, Q., Guo, C., Liang, Y., & Sun, W. (2019) · BioMed Research International · doi:10.1155/2019/5171602 · Cited by 97

Aging increases mitochondrial DNA damage and oxidative stress in liver of rhesus monkeys

Castro, M. D. R., Suárez, E., Kraiselburd, E., Isidro, A., de la Paz, J. L. F., Ferder, L., & Ayala‐Torres, S. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.10.002 · Cited by 95

Complement inhibition as a therapeutic strategy in retinal disorders

Kassa, E., Ciulla, T. A., Hussain, R. M., & Dugel, P. U. (2019) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2019.1575358 · Cited by 94

Brain injury accelerates the onset of a reversible age-related microglial phenotype associated with inflammatory neurodegeneration

Ritzel, R. M., Li, Y., Jiao, Y., Lei, Z., Doran, S. J., He, J., Shahror, R. A., Henry, R. J., Khan, R., Tan, C., et al. (2023) · Science Advances · doi:10.1126/sciadv.add1101 · Cited by 90

Mitochondrial Dysfunction: The Road to Alpha-Synuclein Oligomerization in PD

Esteves, A. R., Arduíno, D. M., Silva, D. F., Oliveira, C. R., & Cardoso, S. M. (2011) · Parkinson s Disease · doi:10.4061/2011/693761 · Cited by 90

Retinal pigment epithelium response to oxidant injury in the pathogenesis of early age-related macular degeneration

Mettu, P. S., Wielgus, A. R., Ong, S. S. Y., & Cousins, S. W. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.04.006 · Cited by 92

Oxidative stress, intestinal damage, and cell apoptosis: Toxicity induced by fluopyram in Caenorhabditis elegans

Liu, Y., Zhang, W., Wang, Y., Liu, H., Zhang, S., Ji, X., & Qiao, K. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.131830 · Cited by 89

Selective autophagy in the maintenance of cellular homeostasis in aging organisms

Hubbard, V. M., Valdor, R., Macián, F., & Cuervo, A. M. (2011) · Biogerontology · doi:10.1007/s10522-011-9331-x · Cited by 90

Inhibition of autophagy with 3-methyladenine results in impaired turnover of lysosomes and accumulation of lipofuscin-like material

Stroikin, Y., Dalen, H., Lööf, S., & Terman, A. (2004) · European Journal of Cell Biology · doi:10.1078/0171-9335-00433 · Cited by 88

Beta-caryophyllene modulates expression of stress response genes and mediates longevity in Caenorhabditis elegans

Pant, A., Saikia, S. K., Shukla, V., Asthana, J., Akhoon, B. A., & Pandey, R. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.05.007 · Cited by 89

Non-cell autonomous effects of the senescence-associated secretory phenotype in cancer therapy.

Saleh, T., Tyutynuk-Massey, L., Cudjoe, E. K., Idowu, M. O., Landry, J. W., & Gewirtz, D. A. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00164 · Cited by 85

Melanin and lipofuscin as hallmarks of skin aging

Skoczyńska, A., Budzisz, E., Trznadel-Grodzka, E., & Rotsztejn, H. (2017) · Advances in Dermatology and Allergology · doi:10.5114/ada.2017.67070 · Cited by 86

Lysosomal and Autophagic Reactions as Predictive Indicators of Environmental Impact in Aquatic Animals

Moore, M. N., Allen, J. I., McVeigh, A., & Shaw, J. (2006) · Autophagy · doi:10.4161/auto.2663 · Cited by 83

Small-molecule G-quadruplex stabilizers reveal a novel pathway of autophagy regulation in neurons

Moruno-Manchon, J. F., Lejault, P., Wang, Y., McCauley, B. S., Honarpisheh, P., Morales‐Scheihing, D., Singh, S. S., Dang, W., Kim, N., Urayama, A., et al. (2020) · eLife · doi:10.7554/elife.52283 · Cited by 84

Neuroprotective actions of deferiprone in cultured cortical neurones and SHSY‐5Y cells

Molina‐Holgado, F., Gaeta, A., Francis, P. T., Williams, R. J., & Hider, R. C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05332.x · Cited by 84

Age‐related accumulation of Marinesco bodies and lipofuscin in rhesus monkey midbrain dopamine neurons: Relevance to selective neuronal vulnerability

Kanaan, N. M., Kordower, J. H., & Collier, T. J. (2007) · The Journal of Comparative Neurology · doi:10.1002/cne.21333 · Cited by 82

Age-related differences in oxidative protein-damage in young and senescent fibroblasts

Jung, T., Höhn, A., Catalgol, B., & Grune, T. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.12.007 · Cited by 86

The aging myocardium: roles of mitochondrial damage and lysosomal degradation

Terman, A., & Brunk, U. T. (2005) · Heart, Lung and Circulation · doi:10.1016/j.hlc.2004.12.023 · Cited by 80

Endogenous Photosensitizers in Human Skin

Bastos, E. L., Quina, F. H., & Baptista, M. S. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00787 · Cited by 86

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Gurusamy, N., & Das, D. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2524 · Cited by 83

Murine Cathepsin F Deficiency Causes Neuronal Lipofuscinosis and Late-Onset Neurological Disease

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Lipofuscin

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Lipofuscin: Mechanisms of formation and increase with age

TERMAN, A., & BRUNK, U. T. (1998) · APMIS · doi:10.1111/j.1699-0463.1998.tb01346.x · Cited by 387

Lipofuscinogenesis in a model system of cultured cardiac myocytes

Marzabadi, M. R., Yin, D., & Brunk, U. T. (1992) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7460-1_9 · Cited by 12

Free radicals in cellular pathology : Mechanisms behind lipofucin formation in cultured myocardial cells

Marzabadi, M. R. (1991)

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