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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
Cited by
Sorted by citations
Items 101–200 of 298
Lysosomes, Autophagy, and Hormesis in Cell Physiology, Pathology, and Age-Related Disease
Moore, M. N. (2020) · Dose-Response · doi:10.1177/1559325820934227 · Cited by 33
Ilie, O., Ciobica, A. S., Riga, S., Dhunna, N., McKenna, J., Mavroudis, I. A., Doroftei, B., Ciobanu, A. M., & Riga, D. (2020) · Medicina · doi:10.3390/medicina56110626 · Cited by 34
Degradation of mitochondria to lipofuscin upon heating and illumination
Frolova, M. S., Surin, A. M., Braslavski, A. V., & Vekshin, N. L. (2015) · BIOPHYSICS · doi:10.1134/s0006350915060081 · Cited by 31
Effects of apoptosis on liver aging
Hu, S., Jiang, S., Zhang, J., Luo, D., Yu, B., Yang, L.-Y., Zhong, H., Yang, M.-W., Liu, L.-Y. D., Hong, F., et al. (2019) · World Journal of Clinical Cases · doi:10.12998/wjcc.v7.i6.691 · Cited by 32
Multiparameter flow cytometric detection and quantification of senescent cells in vitro
Adewoye, A. B., Tampakis, D., Follenzi, A., & Stolzing, A. (2020) · Biogerontology · doi:10.1007/s10522-020-09893-9 · Cited by 31
Lopes, J., Coppola, F., Soares, A. M. V. M., Meucci, V., Pretti, C., Polese, G., & Freitas, R. (2021) · Environmental Research · doi:10.1016/j.envres.2021.112279 · Cited by 34
de Oliveira, S. E., Costa, P. D. M., do Nascimento, S. B., de Castro, W. V., Ribeiro, R. I. M. D. A., dos Santos, H. B., & Thomé, R. G. (2018) · Aquatic Toxicology · doi:10.1016/j.aquatox.2018.06.018 · Cited by 30
Zhao, Q., & Lai, K. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109770 · Cited by 31
Lominchar, P. L., Orue-Echebarria, M. I., Martín, L., Lisbona, C. J., Salcedo, M. M., Olmedilla, L., Sharma, H., Asencio, J. M., & López-Baena, J. Á. (2019) · World Journal of Hepatology · doi:10.4254/wjh.v11.i9.663 · Cited by 29
Takenaka, Y., Inoue, I., Nakano, T., Ikeda, M., & Kakinuma, Y. (2021) · FEBS Journal · doi:10.1111/febs.16249 · Cited by 29
Guix, F. X. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24526 · Cited by 30
Membrane damage by betulinic acid provides insights into cellular aging
Martins, W. K., Gomide, A. B., Costa, É. T., Junqueira, H. C., Stolf, B. S., Itri, R., & Baptista, M. S. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.10.018 · Cited by 29
Campbell, J. M., Gosnell, M. E., Agha, A., Handley, S., Knab, A., Anwer, A. G., Bhargava, A., & Goldys, E. M. (2024) · Advanced Materials · doi:10.1002/adma.202403761 · Cited by 29
Oxidized DJ-1 Levels in Urine Samples as a Putative Biomarker for Parkinson’s Disease
Jang, J., Jeong, S., Lee, S. I., Seol, W., Seo, H., Son, I., & Ho, D. H. (2018) · Parkinson s Disease · doi:10.1155/2018/1241757 · Cited by 27
Cao, X., & Thyfault, J. P. (2023) · Experimental Gerontology · doi:10.1016/j.exger.2023.112178 · Cited by 25
Neuroprotective expression of turmeric and curcumin
Abbas, S., Latif, M. S., Shafie, N. S., Ghazali, M. I., & Kormin, F. B. (2020) · Food Research · doi:10.26656/fr.2017.4(6).363 · Cited by 25
Renziehausen, J., Hiebel, C., Nagel, H., Kundu, A., Kins, S., Kögel, D., Behl, C., & Hajieva, P. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-140600 · Cited by 25
Effect of Temperature on the Rate of Ageing: An Experimental Study of the Blowfly Calliphora stygia
Kelly, M. A., Zieba, A. P., Buttemer, W. A., & Hulbert, A. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073781 · Cited by 25
Rizou, S. V., Evangelou, K., Myrianthopoulos, V., Mourouzis, I., Havaki, S., Athanasiou, A., Vasileiou, P. V. S., Margetis, A., Kotsinas, A., Kastrinakis, N. G., et al. (2019) · Methods in Molecular Biology · doi:10.1007/978-1-4939-8931-7_12 · Cited by 25
Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer’s Disease
Dhakal, S., & Macreadie, I. G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218014 · Cited by 26
Aging Induces Hepatic Oxidative Stress and Nuclear Proteomic Remodeling in Liver from Wistar Rats
Bárcena, B., Salamanca, A., Pintado, C., Mazuecos, L., Villar, M., Moltó, E., Bonzón‐Kulichenko, E., Vázquez, J., Andrés, A., & Gallardo, N. (2021) · Antioxidants · doi:10.3390/antiox10101535 · Cited by 24
The Role of Iron and Cobalt in Gynecological Diseases
Ćwiertnia, A., Kozłowski, M., & Cymbaluk‐Płoska, A. (2022) · Cells · doi:10.3390/cells12010117 · Cited by 25
Lemelle, L., Simionovici, A., Colin, P., Knott, G. W., Bohic, S., Cloetens, P., & Schneider, B. L. (2020) · Communications Biology · doi:10.1038/s42003-020-1084-0 · Cited by 23
Álvarez-Córdoba, M., Reche-López, D., Cilleros-Holgado, P., Talaverón-Rey, M., Villalón-García, I., Povea-Cabello, S., Suarez-Rivero, J. M., Suárez-Carrillo, A., Munuera-Cabeza, M., Piñero-Pérez, R., et al. (2022) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-022-02465-9 · Cited by 22
Modulation of Autophagy: A Novel “Rejuvenation” Strategy for the Aging Liver
Xu, F., Tautenhahn, H., Dirsch, O., & Dahmen, U. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6611126 · Cited by 21
Fu, K., Zhang, J., Wang, L., Zhao, X., & Luo, Y. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109217 · Cited by 21
Aging on a different scale – chronological versus pathology-related aging
Melis, J. P. M., Jonker, M. J., Vijg, J., Hoeijmakers, J. H. J., Breit, T. M., & STEEG, H. V. (2013) · Aging · doi:10.18632/aging.100606 · Cited by 21
Precision medicine in pantothenate kinase-associated neurodegeneration
Álvarez-Córdoba, M., Paz, M. V., Villalón-García, I., Povea-Cabello, S., Suarez-Rivero, J. M., Talaverón-Rey, M., Abril-Jaramillo, J., Vintimilla-Tosi, A. B., & Sánchez-Alcázar, J. A. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.251203 · Cited by 21
Autophagy as an emerging therapeutic target for age-related vascular pathologies
Munck, D. G. D., Meyer, G. R. Y. D., & Martinet, W. (2020) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2020.1723079 · Cited by 20
Cardiomyocyte Contractility and Autophagy in a Premature Senescence Model of Cardiac Aging
Häseli, S. P., Deubel, S., Jung, T., Grune, T., & Ott, C. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8141307 · Cited by 23
Self-citationKim, M. J., Kim, D. H., Kwak, H. S., Yu, I.-S., & Um, M. Y. (2022) · Antioxidants · doi:10.3390/antiox11040669 · Cited by 20
Wang, N., Bai, X., Jin, B., Han, W., Sun, X., & Chen, X. (2016) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2016.03.015 · Cited by 21
Signal regulatory protein α protects podocytes through promotion of autophagic activity
Li, L., Liu, Y., Li, S., Yang, R., Zeng, C., Rong, W., Liang, H., Zhang, M., Zhu, X., Kidder, K., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.124747 · Cited by 19
Davan-Wetton, C. S. A., & Montero‐Melendez, T. (2024) · PLoS ONE · doi:10.1371/journal.pone.0306275 · Cited by 20
Cell Signaling Pathway Reporters in Adult Hematopoietic Stem Cells
de Roo, J. J. D., & Staal, F. J. T. (2020) · Cells · doi:10.3390/cells9102264 · Cited by 19
Cardiac iron metabolism during aging – Role of inflammation and proteolysis
Walter, S., Mertens, C., Muckenthaler, M. U., & Ott, C. (2023) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2023.111869 · Cited by 19
Ng’oma, E., Reichwald, K., Dorn, A., Wittig, M., Balschun, T. C., Franke, A., Platzer, M., & Cellerino, A. (2014) · Aging · doi:10.18632/aging.100660 · Cited by 20
Biase, D. D., Costagliola, A., Pagano, T. B., Piegari, G., Wojcik, S. P., Dziewíatkowski, J., Grieco, E., Raso, G. M., Russo, V., Papparella, S., et al. (2017) · BMC Veterinary Research · doi:10.1186/s12917-017-1028-1 · Cited by 19
Toxic effects of prolonged exposure to [C14mim]Br on Caenorhabditis elegans
Peng, Y., Tong, Z., Chong, H.-J., & Shao, X.-Y. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.05.176 · Cited by 19
Kim, D., Choi, Y. R., Shim, J., Choi, Y., Kim, Y. T., Kim, M. K., & Kim, M. J. (2020) · Molecules · doi:10.3390/molecules25071737 · Cited by 20
Nutrient Sensor mTOR and OGT: Orchestrators of Organelle Homeostasis in Pancreatic β-Cells
Esch, N., Jo, S., Moore, M., & Alejandro, E. U. (2020) · Journal of Diabetes Research · doi:10.1155/2020/8872639 · Cited by 18
Optimization of Immunofluorescent Detection of Bone Marrow Disseminated Tumor Cells
Axelrod, H. D., Pienta, K. J., & Valkenburg, K. C. (2018) · Biological Procedures Online · doi:10.1186/s12575-018-0078-5 · Cited by 18
Li, A.-P., Li, D., Tan, X., Xu, R., Mao, L., Kang, J.-J., Li, S., & Liu, Y. (2025) · Food & Function · doi:10.1039/d5fo01157d · Cited by 17
El‐Sherbiny, M., Atef, H., Helal, G. M., Al‐Serwi, R. H., Elkattawy, H. A., Shaker, G. A., Said, E., Abulfaraj, M. W., Albalawi, M. A., & Elsherbiny, N. M. (2022) · Antioxidants · doi:10.3390/antiox11112150 · Cited by 17
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Bravo, M., Simón, J., González‐Recio, I., Martínez‐Cruz, L. A., Goikoetxea‐Usandizaga, N., & Martínez‐Chantar, M. L. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.05.009 · Cited by 20
Leite, C., Russo, T., Cuccaro, A., Pinto, J., Polese, G., Soares, A. M. V. M., Pretti, C., Pereira, E., & Freitas, R. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.166085 · Cited by 17
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Krumm, L., Pozner, T., Zagha, N., Coras, R., Arnold, P., Tsaktanis, T., Scherpelz, K. P., Davis, M. Y., Kaindl, J., Stolzer, I., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-023-02675-w · Cited by 17
Suárez-Carrillo, A., Álvarez-Córdoba, M., Romero-González, A., Talaverón-Rey, M., Povea-Cabello, S., Cilleros-Holgado, P., Piñero-Pérez, R., Reche-López, D., Gómez-Fernández, D., Romero-Domínguez, J. M., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914576 · Cited by 15
Ross, J. M., Olson, L., & Coppotelli, G. (2024) · Biomolecules · doi:10.3390/biom14020162 · Cited by 17
Moore, M. N., Shaw, J. P., Pascoe, C. K., Beesley, A., Viarengo, A., & Lowe, D. M. (2020) · Marine Environmental Research · doi:10.1016/j.marenvres.2020.104903 · Cited by 16
Limberger, G. M., Nery, L. E. M., & da Fonseca, D. B. (2021) · Neotropical Entomology · doi:10.1007/s13744-020-00839-x · Cited by 16
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Călin, E., Popescu, S. I., Cernat, C., Patoni, C., Popescu, M.-N., & Mușat, O. (2021) · Romanian Journal of Ophthalmology · doi:10.22336/rjo.2021.23 · Cited by 18
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Wahid, R. M., Hassan, N. H., Samy, W. M., Abdelhadi, A. A., Saadawy, S. F., El-sayed, S. F., Seada, S. G., & Mohamed, S. R. A. (2024) · Scientific Reports · doi:10.1038/s41598-024-63644-1 · Cited by 16
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Miyoshi, Y., Yoshioka, Y., Suzuki, K., Miyazaki, T., Koura, M., Saigoh, K., Kajimura, N., Monobe, Y., Kusunoki, S., Matsuda, J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107867 · Cited by 15
Wada, Y., Nagai, A., Sheikh, A. M., Onoda, K., Terashima, M., Shiota, Y., Araki, A., & Yamaguchi, S. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.11.023 · Cited by 15
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Ruiz‐Soto, M., Riancho, J., Tapia, O., Lafarga, M., & Berciano, M. T. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.595751 · Cited by 15
Dontsov, A. E., Yakovleva, M. A., Трофимова, Н. Н., Sakina, N. L., Gulin, A. A., Aybush, A. V., Gostev, F. E., Vasin, A., Feldman, T. B., & Оstrovsky, М. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031534 · Cited by 15
Reprint of “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.2014.10.001 · Cited by 15
Self-citationBłasiak, J., & Kaarniranta, K. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2157260 · Cited by 16
Nasiri, L., Mahdavi, M. R. V., Hassanpour, H., Ghazanfari, T., Ardestani, S. K., Askari, N., Majd, M.-A. M., & Rahimlou, B. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109549 · Cited by 14
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Tang, B. L. (2015) · Ecological Indicators · doi:10.1016/j.ecolind.2015.07.022 · Cited by 13
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Seidman, J. D., & Woodburn, R. (2015) · International Journal of Gynecological Pathology · doi:10.1097/pgp.0000000000000154 · Cited by 13
Jin, M., Alam, M. M., Liu, A. Y. ‐., & Jiang, P. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.09.012 · Cited by 11
Bouamama, S., & Bouamama, A. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23354 · Cited by 12
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Divithotawela, C., Apte, S. H., Tan, M. E., de Silva, T. A., & Chambers, D. C. (2020) · Respirology Case Reports · doi:10.1002/rcr2.566 · Cited by 12
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Sanchez, W. Y., Pastore, M. N., Haridass, I. N., König, K., Becker, W. H., & Roberts, M. S. (2015) · Springer series in chemical physics · doi:10.1007/978-3-319-14929-5_15 · Cited by 12
Chang, K.-T., Lin, Y.-Y., Lin, Y.-Y., Lin, Y.-L., Cheng, H., Chang, Y., & Huang, M. (2018) · World Neurosurgery · doi:10.1016/j.wneu.2018.10.144 · Cited by 11
Sakamoto, K., Fujimoto, R., Nakagawa, S., Kamiyama, E., Kanai, K., Kawai, Y., Kojima, H., Hirasawa, A., Wakamatsu, K., & Masutani, T. (2023) · International Journal of Cosmetic Science · doi:10.1111/ics.12876 · Cited by 12
Notch1 participates in the activation of autophagy in the hippocampus of type I diabetic mice
Wáng, Y., Wang, S., Zhang, W., Liu, J., Yang, Z. R., & Liu, C. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105156 · Cited by 10
Cheng, Z., Ferris, C. P., Crowe, M. A., Ingvartsen, K. L., Grelet, C., Vanlierde, A., Foldager, L., Becker, F. O., & Wathes, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129906 · Cited by 13
Klotho: molecular mechanisms and emerging therapeutics in central nervous system diseases
Hosseini, L., Babaie, S., Shahabi, P., Fekri, K., Shafiee‐Kandjani, A. R., Mafikandi, V., Maghsoumi‐Norouzabad, L., & Abolhasanpour, N. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09862-2 · Cited by 11
Walter, S., Häseli, S. P., Owesny, P., Deubel, S., Jung, T., Höhn, A., Ott, C., & Grune, T. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103559 · Cited by 11
Self-citationBíscaro, R. C., Mussi, L., Sufi, B. D. S., Padovani, G., Camargo, F. B., Magalhães, W. V., & Stasi, L. C. D. (2022) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.14888 · Cited by 10
Díaz-Hernández, V., Montaño, L. M., Caldelas, I., & Marmolejo-Valencia, A. (2022) · Biomedicines · doi:10.3390/biomedicines10123068 · Cited by 10
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Pattison, C. J., & Korolchuk, V. I. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-2835-0_2 · Cited by 10
Schwann Cell Autophagy and Necrosis as Mechanisms of Cell Death by Acanthamoeba
Castelan-Ramírez, I., Salazar-Villatoro, L. I., Chávez‐Munguía, B., Salinas‐Lara, C., Sánchez-Garibay, C., Flores-Maldonado, C., Hernández-Martínez, D., Anaya-Martı́nez, V., Ávila-Costa, M. R., Méndez‐Cruz, A. R., et al. (2020) · Pathogens · doi:10.3390/pathogens9060458 · Cited by 10
Voisin, A., Monville, C., Plancheron, A., Béré, E., Gaillard, A., & Leveziel, N. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/5637075 · Cited by 10
Mohanty, S. K., & Suchiang, K. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121946 · Cited by 9
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Kallergi, E., & Nikoletopoulou, V. (2021) · Cell Stress · doi:10.15698/cst2021.10.257 · Cited by 10
Lipofuscin in saliva and plasma and its association with age in healthy adults
Feng, F.-K., Lingling, E., Kong, X., Wang, D., & Liu, H. (2015) · Aging Clinical and Experimental Research · doi:10.1007/s40520-015-0326-3 · Cited by 9
Badea, P., Petrescu, A., Moldovan, L., & Zărnescu, O. (2015) · Microscopy and Microanalysis · doi:10.1017/s1431927615000197 · Cited by 9
Occurrence and characterization of lipofuscin and ceroid in human atherosclerotic plaque
Perrotta, I. D. (2018) · Ultrastructural Pathology · doi:10.1080/01913123.2018.1544953 · Cited by 9
Popovic, M. E. (2022) · Preprints.org · doi:10.20944/preprints202210.0326.v1 · Cited by 9
Cardiometabolic Changes in Sirtuin1-Heterozygous Mice on High-Fat Diet and Melatonin Supplementation
Favero, G., Golić, I., Arnaboldi, F., Cappella, A., Korać, A., Monsalve, M., Stacchiotti, A., & Rezzani, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020860 · Cited by 8
Toward Systemic Lipofuscin Removal
Renteln, M. (2024) · Rejuvenation Research · doi:10.1089/rej.2024.0034 · Cited by 8
Luo, M.-M., Chen, L., Wang, S., Zeng, C., Li, D., Bi, Y., Liu, L., & Cai, S. (2021) · Journal of Ophthalmology · doi:10.1155/2021/5586659 · Cited by 8
Keenan, J., O’Sullivan, F., Henry, M. A., Breen, L., Doolan, P., Sinkunaite, I., Meleady, P., CLYNES, M. M., Horgan, K. A., & Murphy, R. A. (2018) · Food Science & Nutrition · doi:10.1002/fsn3.857 · Cited by 9
Manola, M. S., Tsakiri, E. N., & Trougakos, I. P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7823285 · Cited by 7
Lysosomes and lysosomal dysfunction in ageing biology
Steinhauser, M. L., Liu, Y., Rizzo, S. J. S., Chen, B. B., Finkel, T., & Tan, J. X. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-02007-6 · Cited by 9
Machihara, K., Kageyama, S., Oki, S., Makino, H., Sasaki, M., Iwahashi, H., & Namba, T. (2022) · Aging · doi:10.18632/aging.204303 · Cited by 7
Álvarez-Córdoba, M., Talaverón-Rey, M., Povea-Cabello, S., Cilleros-Holgado, P., Gómez-Fernández, D., Piñero-Pérez, R., Reche-López, D., Munuera-Cabeza, M., Suárez-Carrillo, A., Romero-González, A., et al. (2023) · Pharmaceuticals · doi:10.3390/ph16101359 · Cited by 6
Tao, T., Xu, N., Li, J., Zhao, M., Li, X., & Huang, L. (2023) · The Journal of Pathology · doi:10.1002/path.6201 · Cited by 7
Devi, A., Dwibedi, V., Rath, S. K., & Khan, Z. A. (2022) · Revista Brasileira de Farmacognosia · doi:10.1007/s43450-022-00254-w · Cited by 5
Wozniak, P. S., & Rampon, G. L. (2023) · Cureus · doi:10.7759/cureus.41318 · Cited by 5
Establishment of a Spontaneous Liver Fibrosis Model in NOD/SCID Mice Induced by Natural Aging
Qiu, L., Ma, Z., Sun, J., Wu, Z., Wang, M., Wang, S., Zhao, Y., Shu, L., Hu, M., & Li, Y. (2023) · Biology · doi:10.3390/biology12121493 · Cited by 5
Nooh, H. Z., El-Saify, G. H., & Nooreldien, N. M. (2017) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2017.05.001 · Cited by 5
Khatami, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-66475-0_3 · Cited by 6
Lipofuscin and Mitolipofuscin in the Organs of Young and Adult Rats
Chaplygina, A. V., & Vekshin, N. L. (2018) · Advances in Gerontology · doi:10.1134/s2079057018040057 · Cited by 5
Stem Cell Senescence as the Memory of Past Injuries
Gianfranceschi, G., Gri, G., Cesselli, D., & Beltrami, A. P. (2015) · Current Pathobiology Reports · doi:10.1007/s40139-015-0071-5 · Cited by 4
Yang, Y. F., Shao, Y., Wang, J., Cheng, Q., Yang, H., Li, Y., Liu, J., Zhou, Y., Zhou, Z., Wang, M., et al. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1185240 · Cited by 4
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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