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Lipofuscin: formation, effects and role of macroautophagy
Open accessAbstract
Oxidative stress plays a crucial role in the development of the aging process and age dependent diseases. Both are closely connected to disturbances of proteostasis by protein oxidation and an impairment of the proteasomal system. The final consequence is the accumulation of highly cross-linked undegradable aggregates such as lipofuscin. These aggregates of damaged proteins are detrimental to normal cell functions. Here we provide an overview about effect of these aggregates on the proteasomal system, followed by transcription factor activation and loss of cell viability. Furthermore, findings on the mechanism of radical genesis, proteasomal inhibition and the required components of lipofuscin formation were resumed.
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“Cellular senescence is associated with changes in cellular metabolism. These include upregulation of lysosomal senescence-associated β-galactosidase, a shift from oxidative phosphorylation to glycolysis [54,55] and accumulation of lipofuscin in the cytoplasm [56,57].”
From Ageing, Cellular Senescence and Neurodegenerative Disease (2018) · cites this paper as [56]
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Cites
Function and Activation of NF-kappaB in the Immune System
Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745
Autophagy: process and functionPreprint
Mizushima, N. (2007) · Genes & Development · doi:10.1101/gad.1599207 · Cited by 4,104
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,105
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · cited 1×
“All rights reserved.”
The ubiquitin-proteasome proteolytic pathway
Ciechanover, A. J. (1994) · Cell · doi:10.1016/0092-8674(94)90396-4 · Cited by 1,804
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529
Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation
Brown, K., Gerstberger, S., Carlson, L., Franzoso, G., & Siebenlist, U. (1995) · Science · doi:10.1126/science.7878466 · Cited by 1,434
Unveiling the roles of autophagy in innate and adaptive immunity
Levine, B., & Deretic, V. P. (2007) · Nature reviews. Immunology · doi:10.1038/nri2161 · Cited by 934
Brunk, U. T., & Terman, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00959-0 · Cited by 919
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Oxidative Stress in Aging Human Skin
Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015) · Biomolecules · doi:10.3390/biom5020545 · Cited by 1,053
Curcumin, Inflammation, and Chronic Diseases: How Are They Linked?
He, Y., Yue, Y., Zheng, X., Zhang, K., Chen, S., & Du, Z. (2015) · Molecules · doi:10.3390/molecules20059183 · Cited by 632
Kim, I. H., Kisseleva, T., & Brenner, D. A. (2015) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000176 · Cited by 508
Ageing, Cellular Senescence and Neurodegenerative Disease
Kritsilis, M., V. Rizou, S., Koutsoudaki, P. N., Evangelou, K., Gorgoulis, V. G., & Papadopoulos, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102937 · Cited by 448
“These include upregulation of lysosomal senescence-associated β-galactosidase, a shift from oxidative phosphorylation to glycolysis [54,55] and accumulation of lipofuscin in the cytoplasm [56,57].”
BackgroundThe topograpy of demyelination and neurodegeneration in the multiple sclerosis brain
Haider, L., Zrzavy, T., Hametner, S., Höftberger, R., Bagnato, F., Grabner, G., Trattnig, S., Pfeifenbring, S., Brück, W., & Lassmann, H. (2016) · Brain · doi:10.1093/brain/awv398 · Cited by 400
Mitochondrial dysfunction in neurodegenerative disorders
Klemmensen, M. M., Borrowman, S. H., Pearce, C., Pyles, B., & Chandra, B. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.002 · Cited by 396
Endocannabinoid signalling and the deteriorating brain
Marzo, V. D., Stella, N., & Zimmer, A. (2014) · Nature reviews. Neuroscience · doi:10.1038/nrn3876 · Cited by 395
An Overview of the Role of Lipofuscin in Age-Related Neurodegeneration
Moreno-García, A., Kun, A., Calero, O., Medina, M., & Calero, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00464 · Cited by 372
Höhn, A., Weber, D., Jung, T., Ott, C., Hugo, M., Kochlik, B., Kehm, R., König, J., Grune, T., & Castro, J. P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.12.001 · Cited by 388
Self-citationAutophagy as an essential cellular antioxidant pathway in neurodegenerative disease
Giordano, S. S., Darley-Usmar, V. M., & Zhang, J. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.013 · Cited by 372
Cellular Senescence in Neurodegenerative Diseases
Martínez‐Cué, C., & Rueda, N. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00016 · Cited by 299
Proteostasis, oxidative stress and aging
Korovila, I., Hugo, M., Castro, J. P., Weber, D., Höhn, A., Grune, T., & Jung, T. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.008 · Cited by 285
Self-citationAutophagy and A lpha‐ S ynuclein: R elevance to P arkinson's D isease and R elated S ynucleopathies
Xilouri, M., Brekk, O. R., & Stefanis, L. (2016) · Movement Disorders · doi:10.1002/mds.26477 · Cited by 280
4-Hydroxynonenal (HNE) modified proteins in metabolic diseases
Castro, J. P., Jung, T., Grune, T., & Siems, W. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.497 · Cited by 223
Self-citationRegulation of neuronal development and function by ROS
Oswald, M. C. W., Garnham, N., Sweeney, S. T., & Landgraf, M. (2018) · FEBS Letters · doi:10.1002/1873-3468.12972 · Cited by 213
Gladyshev, V. N., Kritchevsky, S. B., Clarke, S. G., Cuervo, A. M., Fiehn, O., de Magalhães, J. P., Mau, T., Maes, M., Moritz, R. L., Niedernhofer, L. J., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00150-3 · Cited by 222
Loss of hepatic chaperone‐mediated autophagy accelerates proteostasis failure in aging
Schneider, J. L., Villarroya, J., Díaz-Carretero, A. M., Patel, B., Urbanska, A. M., Thi, M. M., Villarroya, F., Santambrogio, L., & Cuervo, A. M. (2015) · Aging Cell · doi:10.1111/acel.12310 · Cited by 201
Jung, T., Höhn, A., & Grune, T. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.008 · Cited by 193
Self-citationProtein Oxidation in Aging: Does It Play a Role in Aging Progression?
Reeg, S., & Grune, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6062 · Cited by 191
Self-citationMacrophages in the Aging Liver and Age-Related Liver Disease
Stahl, E. C., Haschak, M. J., Popovic, B., & Brown, B. N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02795 · Cited by 171
Redox control of protein degradation
Pajares, M., Jiménez-Moreno, N., Dias, I. H. K., BÜTÜNER, B. D., Vučetić, M., Fladmark, K. E., Başağa, H., Ribarič, S., Milisav, I., & Cuadrado, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.003 · Cited by 177
Senescence in Post-Mitotic Cells: A Driver of Aging?
von Zglinicki, T., Wan, T., & Miwa, S. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8048 · Cited by 170
Abokyi, S., To, C. H., Lam, T. T., & Tse, D. Y. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7901270 · Cited by 180
Senescence and senotherapeutics: a new field in cancer therapy
Myrianthopoulos, V., Evangelou, K., Vasileiou, P. V. S., Cooks, T., Vassilakopoulos, T. P., Pangalis, G. A., Kouloukoussa, M., Kittas, C., Georgakilas, A. G., & Gorgoulis, V. G. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.08.006 · Cited by 160
Lysosomes in senescence and aging
Tan, J. X., & Finkel, T. (2023) · EMBO Reports · doi:10.15252/embr.202357265 · Cited by 178
Lipoxidation in cardiovascular diseases
Gianazza, E., Brioschi, M., Fernandez, A. M., & Banfi, C. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101119 · Cited by 152
Calderón‐Garcidueñas, L., Kulesza, R. J., Doty, R. L., D’Angiulli, A., & Torres‐Jardón, R. (2014) · Environmental Research · doi:10.1016/j.envres.2014.12.012 · Cited by 145
CLINICAL ENDPOINTS FOR THE STUDY OF GEOGRAPHIC ATROPHY SECONDARY TO AGE-RELATED MACULAR DEGENERATION
Sadda, S. R., Chakravarthy, U., Birch, D. G., Staurenghi, G., Henry, E. C., & Brittain, C. J. (2016) · Retina · doi:10.1097/iae.0000000000001283 · Cited by 137
Jung, T., Höhn, A., & Grune, T. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.029 · Cited by 136
Self-citationOxidative theory of atherosclerosis and antioxidants
Salvayre, R., Nègre‐Salvayre, A., & Camaré, C. (2015) · Biochimie · doi:10.1016/j.biochi.2015.12.014 · Cited by 129
Reactive oxygen species regulate activity-dependent neuronal plasticity in Drosophila
Oswald, M. C. W., Brooks, P. S., Zwart, M., Mukherjee, A., West, R. J. H., Giachello, C. N., Morarach, K., Baines, R., Sweeney, S. T., & Landgraf, M. (2018) · eLife · doi:10.7554/elife.39393 · Cited by 113
Michalska, P., & Leon, R. M. (2020) · Antioxidants · doi:10.3390/antiox9080740 · Cited by 119
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Nousis, L., Kanavaros, P., & Barbouti, A. (2023) · Antioxidants · doi:10.3390/antiox12061250 · Cited by 103
Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts
Ott, C., König, J., Höhn, A., Jung, T., & Grune, T. (2016) · Redox Biology · doi:10.1016/j.redox.2016.10.015 · Cited by 96
Self-citationThe dialogue between the ubiquitin-proteasome system and autophagy: Implications in ageing
Sun‐Wang, J. L., Ivanova, S., & Antonio Zorzano, A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101203 · Cited by 98
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
Vicious cycle of lipid peroxidation and iron accumulation in neurodegeneration
Sánchez-Alcázar, J. A., Villalón-García, I., Povea-Cabello, S., Álvarez-Córdoba, M., Talaverón-Rey, M., Suarez-Rivero, J. M., Suárez-Carrillo, A., Munuera-Cabeza, M., Reche-López, D., Cilleros-Holgado, P., et al. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.358614 · Cited by 89
Healthy brain aging: Interplay between reactive species, inflammation and energy supply
Garaschuk, O., Semchyshyn, H. M., & Lushchak, V. I. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.02.003 · Cited by 91
Zeng, C., Yang, T.-T., Zhou, H., Zhao, Y., Kuang, X., Duan, W., & Du, J. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.02.003 · Cited by 87
Kim, I. H., Xu, J., Liu, X., Koyama, Y., Ma, H., Diggle, K., You, Y.-H., Schilling, J. M., Jeste, D. V., Sharma, K., et al. (2016) · AGE · doi:10.1007/s11357-016-9938-6 · Cited by 86
Hu, Q., Lei, T., Hu, Y., & Lei, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673827 · Cited by 83
Martínez‐Fábregas, J., Prescott, A. R., van Kasteren, S. I., Pedrioli, D. M. L., McLean, W. H. I., Moles, A., Reinheckel, T., Poli, V., & Watts, C. K. W. (2018) · Nature Communications · doi:10.1038/s41467-018-07741-6 · Cited by 82
Significance of Singlet Oxygen Molecule in Pathologies
Murotomi, K., Umeno, A., Shichiri, M., Tanito, M., & Yoshida, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032739 · Cited by 86
Implications of Oxidative Stress and Cellular Senescence in Age-Related Thymus Involution
Barbouti, A., Vasileiou, P. V. S., Evangelou, K., Vlasis, K. G., Papoudou‐Bai, A., Gorgoulis, V. G., & Kanavaros, P. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7986071 · Cited by 86
Accumulation of modified proteins and aggregate formation in aging
Nowotny, K., Jung, T., Grune, T., & Höhn, A. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.05.016 · Cited by 84
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Guardo, G. D. (2015) · European Journal of Histochemistry · doi:10.4081/ejh.2015.2485 · Cited by 79
Comparative histology in the liver and spleen of three species of freshwater teleost
Sales, C. F., Silva, R. F., Amaral, M. G. C., Domingos, F. F. T., Ribeiro, R. I. M. D. A., Thomé, R. G., & dos Santos, H. B. (2017) · Neotropical Ichthyology · doi:10.1590/1982-0224-20160041 · Cited by 79
Burns, J. C., Cotleur, B., Walther, D. M., Bajrami, B., Rubino, S. J., Wei, R., Franchimont, N., Cotman, S. L., Ransohoff, R. M., & Mingueneau, M. (2020) · eLife · doi:10.7554/elife.57495 · Cited by 82
Reversible Age-Related Phenotypes Induced during Larval Quiescence in C. elegans
Roux, A. E., Langhans, K. E., Huynh, W., & Kenyon, C. J. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.024 · Cited by 79
Klotho as Potential Autophagy Regulator and Therapeutic Target
Zhou, H., Pu, S., Zhou, H., & Guo, Y. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.755366 · Cited by 80
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The Role of Free Radicals in Autophagy Regulation: Implications for Ageing
Pajares, M. A., Cuadrado, A., Engedal, N., Jirsova, Z., & Cahová, M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2450748 · Cited by 69
Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond
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Self-citationEffects of sulforaphane on D-galactose-induced liver aging in rats: Role of keap-1/nrf-2 pathway.
Saleh, D. O., Mansour, D. F., Hashad, I. M., & Bakeer, R. M. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.04.043 · Cited by 65
Peroxisomal dysfunction in neurodegenerative diseases
Jo, D. S., & Cho, D. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01131-2 · Cited by 66
Lysosomes in programmed cell death pathways: from initiators to amplifiers
Kavčič, N., Pegan, K., & Turk, B. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0252 · Cited by 66
Bethke, K., Kwidzińska, K., Stepnowski, P., & Caban, M. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.162829 · Cited by 63
Álvarez-Córdoba, M., Khoury, A. F., Paz, M. V., Gómez-Navarro, C., Villalón-García, I., Suarez-Rivero, J. M., Povea-Cabello, S., de la Mata, M., Cotán, D., Talaverón-Rey, M., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1333-0 · Cited by 64
Liu, T., Qi, H., Ma, L., Liu, Z., Fu, H., Zhu, W., Song, T., Yang, B., & Li, G. (2015) · Rejuvenation Research · doi:10.1089/rej.2014.1618 · Cited by 62
Evidence in Support of Potential Applications of Lipid Peroxidation Products in Cancer Treatment
Erejuwa, O. O., Sulaiman, S. A., & Wahab, M. S. A. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/931251 · Cited by 58
Catic, A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.12.003 · Cited by 58
Zhu, Y., Fenik, P., Zhan, G., Somach, R. T., Xin, R., & Veasey, S. C. (2016) · SLEEP · doi:10.5665/sleep.6030 · Cited by 65
Role of autophagy in environmental neurotoxicity
Pellacani, C., & Costa, L. G. (2018) · Environmental Pollution · doi:10.1016/j.envpol.2017.12.102 · Cited by 53
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Vitamin E prevents lipid peroxidation and iron accumulation in PLA2G6-Associated Neurodegeneration
Villalón-García, I., Álvarez-Córdoba, M., Povea-Cabello, S., Talaverón-Rey, M., Paz, M. V., Luzón–Hidalgo, R., Suarez-Rivero, J. M., Suárez-Carrillo, A., Munuera-Cabeza, M., Salas, J. J., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105649 · Cited by 54
Tetrandrine is a potent cell autophagy agonist via activated intracellular reactive oxygen species
Wang, H., Liu, T., Li, L., Wang, Q., Yu, C., Liu, X., & Li, W. (2015) · Cell & Bioscience · doi:10.1186/2045-3701-5-4 · Cited by 52
Maccarinelli, F., Pagani, A., Cozzi, A., Codazzi, F., Giacomo, G. D., Capoccia, S., Rapino, S., Finazzi, D., Politi, L. S., Cirulli, F., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.10.023 · Cited by 52
Baroncelli, L., Molinaro, A., Cacciante, F., Alessandri, M., Napoli, D., Putignano, E., Tola, J., Leuzzi, V., Cioni, G., & Pizzorusso, T. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw252 · Cited by 51
García-Sevillano, M. Á., García‐Barrera, T., Navarro, F., Montero, Z., & Gómez‐Ariza, J. L. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.02.011 · Cited by 49
A novel role for 12/15-lipoxygenase in regulating autophagy
Morgan, A. H., Hammond, V. J., Sakoh‐Nakatogawa, M., Ohsumi, Y., Thomas, C. P., Blanchet, F. P., Piguet, V., Kiselyov, K. I., & O’Donnell, V. B. (2014) · Redox Biology · doi:10.1016/j.redox.2014.11.005 · Cited by 48
Courtland, J. L., Bradshaw, T. W., Waitt, G., Soderblom, E. J., Ho, T., Rajab, A., Vancini, R., Kim, I. H., & Soderling, S. H. (2021) · eLife · doi:10.7554/elife.61590 · Cited by 49
Aging, Senescence, and Dementia
Behfar, Q., Zuniga, A. R., & Adami, P. V. M. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.42 · Cited by 52
Kou, B., Liu, W., Xu, X., Yang, Y., Yi, Q.-Y., Guo, F., Li, J., Zhou, J., & Kou, Q. (2017) · Oncology Reports · doi:10.3892/or.2017.5988 · Cited by 47
Toxic impacts of rutile titanium dioxide in Mytilus galloprovincialis exposed to warming conditions
Leite, C., Coppola, F., Monteiro, R. J. R., Russo, T., Polese, G., Silva, M. R. F., Lourenço, M. A. O., Ferreira, P., Soares, A. M. V. M., Pereira, E., et al. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.126563 · Cited by 47
Wang, D., Wang, T., Li, Z., Guo, Y., & Granato, D. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.836112 · Cited by 48
Neumann, P., Lenz, D. E., Streit, W. J., & Bechmann, I. (2022) · Glia · doi:10.1002/glia.24282 · Cited by 47
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Disturbances in the control of capillary flow in an aged APPswe/PS1ΔE9 model of Alzheimer's disease
Gutiérrez‐Jiménez, E., Angleys, H., Rasmussen, P. M., West, M. J., Catalini, L., Iversen, N., Jensen, M. S., Frische, S., & Østergaard, L. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.006 · Cited by 44
How, C. M., Li, S.-W., & Liao, V. H. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.05.314 · Cited by 43
Age-Related Lysosomal Dysfunctions
Guerrero‐Navarro, L., Jansen‐Dürr, P., & Cavinato, M. S. (2022) · Cells · doi:10.3390/cells11121977 · Cited by 44
Cirrhotic patients and older people
Carrier, P., Debette-Gratien, M., Jacques, J., & Loustaud-Ratti, V. (2019) · World Journal of Hepatology · doi:10.4254/wjh.v11.i9.678 · Cited by 42
Coppola, F., Bessa, A., Henriques, B., Russo, T., Soares, A. M. V. M., Figueira, E. M. D. A. P., Marques, P. A. A. P., Polese, G., Cosmo, A. D., Pereira, E., et al. (2020) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2020.110674 · Cited by 41
Wiktor, A., Sarna, M., Wnuk, D., & Sarna, T. (2018) · Scientific Reports · doi:10.1038/s41598-018-36322-2 · Cited by 40
Modulation of therapy-induced senescence by reactive lipid aldehydes
Flor, A. C., Doshi, A. P., & Kron, S. J. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.45 · Cited by 40
Oxidized protein aggregates: Formation and biological effects
Grune, T. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.014 · Cited by 45
Self-citationLiu, M., Wang, J., Song, Z., & Pei, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1642248 · Cited by 39
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Metadata
- Authors
- Höhn, A., & Grune, T.
- Affiliations
- Friedrich Schiller University Jena (DE)
- Corresponding author
- Grune, Tilman
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2013
- Volume
- 1
- Issue
- 1
- Pages
- 140-144
- ISSN
- 2213-2317 (ISSN-L)
- PMC
- PMC3757681
- OpenAlex
- W2018027031
- Cited by
- 298
- References
- 51
- Citations by year
- 2026: 19 · 2025: 18 · 2024: 14 · 2023: 30 · 2022: 30 · 2021: 22 · 2020: 33 · 2019: 25 · 2018: 32 · 2017: 15 · 2016: 18 · 2015: 23 · 2014: 14 · 2013: 5
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Redox Biology (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- lipofuscin, macroautophagy, oxidative stress, aging, proteostasis, protein oxidation, proteasome, protein aggregates, transcription factor activation, cell viability, radical formation, proteasome inhibition
- MeSH terms
- Animals, Autophagy, Humans, Lipofuscin, Transcription Factors, Proteasome Endopeptidase Complex
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