Cited by 287Autophagy in Disease and TherapyCalcium signaling and nucleotide metabolismGenetics, Aging, and Longevity in Model Organisms

The DOI matches its Crossref record; 128 of the 129 references it cites were found in a registry or an index.

Lysosomes and oxidative stress in aging and apoptosis

Kurz, Tino, Terman, Alexei, Gustafsson, Bertil, Brunk, Ulf T.·2008·Biochimica et Biophysica Acta (BBA) - General Subjects

DOI 10.1016/j.bbagen.2008.01.009

Open this paper in CoChat — free account

Abstract

The lysosomal compartment consists of numerous acidic vesicles (pH approximately 4-5) that constantly fuse and divide. It receives a large number of hydrolases from the trans-Golgi network, while their substrates arrive from both the cell's outside (heterophagy) and inside (autophagy). Many macromolecules under degradation inside lysosomes contain iron that, when released in labile form, makes lysosomes sensitive to oxidative stress. The magnitude of generated lysosomal destabilization determines if reparative autophagy, apoptosis, or necrosis will follow. Apart from being an essential turnover process, autophagy is also a mechanism for cells to repair inflicted damage, and to survive temporary starvation. The inevitable diffusion of hydrogen peroxide into iron-rich lysosomes causes the slow oxidative formation of lipofuscin in long-lived postmitotic cells, where it finally occupies a substantial part of the volume of the lysosomal compartment. This seems to result in a misdirection of lysosomal enzymes away from autophagosomes, resulting in depressed autophagy and the accumulation of malfunctioning mitochondria and proteins with consequent cellular dysfunction. This scenario might put aging into the category of autophagy disorders.

Integrity signals

Registry

Crossref · 10.1016/j.bbagen.2008.01.009

Cites

128 of 128 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

1 retracted

The Lysosome-associated Apoptosis-inducing Protein Containing the Pleckstrin Homology (PH) and FYVE Domains (LAPF), Representative of a Novel Family of PH and FYVE Domain-containing Proteins, Induces Caspase-independent Apoptosis via the Lysosomal-Mitochondrial Pathway
Chen, W., Li, N., Chen, T., Han, Y., Li, C., Wang, Y., He, W., Zhang, L., Wan, T. Y., & Cao, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502190200 · Cited by 82
Retracted
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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
Self-eating and self-killing: crosstalk between autophagy and apoptosis
Maiuri, M. C., Zalckvar, E., Kimchi, A., & Kroemer, G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2239 · Cited by 3,638
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
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,559
Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents.
Ohkuma, S., & Poole, B. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.7.3327 · Cited by 2,173
Autophagy: from phenomenology to molecular understanding in less than a decade
Klionsky, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2245 · Cited by 1,977
Lysosomes: fusion and function
Luzio, J. P., Pryor, P. R., & Bright, N. A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2217 · Cited by 1,807
Autophagy: molecular machinery for self-eating
Yorimitsu, T., & Klionsky, D. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401765 · Cited by 1,566

Show all 129 references

Sorted by citations

Items 101–200 of 287

HIV-1 Vpr protein impairs lysosome clearance causing SNCA/alpha-synuclein accumulation in neurons
Santerre, M., Arjona, S. P., Allen, C. N. S., Callen, S. E., Buch, S. J., & Sawaya, B. E. (2021) · Autophagy · doi:10.1080/15548627.2021.1915641 · Cited by 51
Fluorescence-Based Detection and Quantification of Features of Cellular Senescence
Cho, S., & Hwang, E. S. (2011) · Methods in cell biology · doi:10.1016/b978-0-12-385493-3.00007-3 · Cited by 53
Photooxidative damage in retinal pigment epithelial cells via GRP78 and the protective role of grape skin polyphenols
Zhao, Z., Sun, T., Jiang, Y., Wu, L., Cai, X., Sun, X., & Sun, X. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.10.001 · Cited by 49
Tyrosine nitration as mediator of cell death
Franco, M. C., & Estévez, Á. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1662-8 · Cited by 50
Xylene Induces Oxidative Stress and Mitochondria Damage in Isolated Human Lymphocytes
Salimi, A., Talatappe, B. S., & Pourahmad, J. (2017) · Toxicological Research · doi:10.5487/tr.2017.33.3.233 · Cited by 49
Iron‐Mediated Lysosomal Membrane Permeabilization in Ethanol‐Induced Hepatic Oxidative Damage and Apoptosis: Protective Effects of Quercetin
Li, Y., Chen, M., Xu, Y., Xiao, Y., Xiong, T., Du, M., Sun, J., Liu, L., Tang, Y., & Yao, P. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4147610 · Cited by 49
Cold Atmospheric Plasma induces accumulation of lysosomes and caspase-independent cell death in U373MG glioblastoma multiforme cells
Conway, G. E., He, Z., Hutanu, A. L., Cribaro, G. P., Manaloto, E., Casey, A., Traynor, D., Milosavljevic, V., Howe, O. L., Barcia, C., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-49013-3 · Cited by 48
Structure of the Proteasome
Jung, T., & Grune, T. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00001-8 · Cited by 47
Nonfunctional mutant Wrn protein leads to neurological deficits, neuronal stress, microglial alteration, and immune imbalance in a mouse model of Werner syndrome
Hui, C. W., St‐Pierre, M., Detuncq, J., Aumailley, L., Dubois, M.-J., Couture, V., Skuk, D., Marette, A., Tremblay, J. P., Lebel, M., et al. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.06.007 · Cited by 47
High-dose chloroquine is metabolically cardiotoxic by inducing lysosomes and mitochondria dysfunction in a rat model of pressure overload hypertrophy
Chaanine, A. H., Gordon, R. E., Nonnenmacher, M. E., Kohlbrenner, E., Bénard, L., & Hajjar, R. J. (2015) · Physiological Reports · doi:10.14814/phy2.12413 · Cited by 45
Beyond basic research: the contribution of cathepsin B to cancer development, diagnosis and therapy
Zamyatnin, A. A., Gregory, L. C., Townsend, P. A., & Soond, S. M. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2161888 · Cited by 44
Chelation of lysosomal iron protects against ionizing radiation
Berndt, C., Kurz, T., Selenius, M., Fernandes, A. P., Edgren, M., & Brunk, U. T. (2010) · Biochemical Journal · doi:10.1042/bj20100996 · Cited by 44
Self-citation
Proteomic Analysis of Rat Cerebral Cortex in the Subacute to Long-Term Phases of Focal Cerebral Ischemia-Reperfusion Injury
Wen, M., Jin, Y., Zhang, H., Sun, X., Kuai, Y., & Tan, W. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00220 · Cited by 42
5′-Adenosine Monophosphate-Activated Protein Kinase–Mammalian Target of Rapamycin Axis As Therapeutic Target for Age-Related Macular Degeneration
Hyttinen, J. M. T., Petrovski, G., Salminen, A., & Kaarniranta, K. (2011) · Rejuvenation Research · doi:10.1089/rej.2011.1220 · Cited by 44
Nanoscopic X-ray fluorescence imaging and quantification of intracellular key-elements in cryofrozen Friedreich’s ataxia fibroblasts
Samber, B. D., Meul, E., Laforce, B., Paepe, B. D., Smet, J., Bruyne, M. D., Rycke, R. M. D., Bohic, S., Cloetens, P., Coster, R. V., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190495 · Cited by 42
Atrazine and chlorpyrifos exposure induces liver autophagic response in common carp
Xing, H., Wang, Z., Gao, X., Chen, D., Wang, L., Li, S., & Xu, S. (2014) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2014.11.027 · Cited by 43
Monitoring intracellular labile iron pools: A novel fluorescent iron(iii) sensor as a potential non-invasive diagnosis tool
Fakih, S., Podinovskaia, M., Kong, X., Schaible, U. E., Collins, H., & Hider, R. C. (2008) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21583 · Cited by 40
The Aging Liver: Redox Biology and Liver Regeneration
Bellanti, F., & Vendemiale, G. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0048 · Cited by 40
Flow cytometry detection of lysosomal presence and lysosomal membrane integrity in the three-spined stickleback (Gasterosteus aculeatus L.) immune cells: applications in environmental aquatic immunotoxicology.
Bado‐Nilles, A., Betoulle, S., Geffard, A., Porcher, J., Gagnaire, B., & Sánchez, W. (2013) · Environmental Science and Pollution Research · doi:10.1007/s11356-012-1410-2 · Cited by 39
Hyperferritinemia and iron metabolism in Gaucher disease: Potential pathophysiological implications
Regenboog, M., Kuilenburg, A. B. P., Verheij, J., Swinkels, D. W., & Hollak, C. E. M. (2016) · Blood Reviews · doi:10.1016/j.blre.2016.05.003 · Cited by 41
A coumarin-based fluorescent probe for specific detection of cysteine in the lysosome of living cells
Lü, G., Dong, J., Fan, C., Tu, Y., & Pu, S. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105558 · Cited by 38
The Link Between Endoplasmic Reticulum Stress and Lysosomal Dysfunction Under Oxidative Stress in Cancer Cells
Vietri, M., Miranda, M. R., Amodio, G., Ciaglia, T., Bertamino, A., Campiglia, P., Remondelli, P., Vestuto, V., & Moltedo, O. (2025) · Biomolecules · doi:10.3390/biom15070930 · Cited by 39
Role of intracellular labile iron, ferritin, and antioxidant defence in resistance of chronically adapted Jurkat T cells to hydrogen peroxide
Al-Qenaei, A., Yiakouvaki, A., Reelfs, O., Santambrogio, P., Levi, S., Hall, N. D., Tyrrell, R. M., & Pourzand, C. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.006 · Cited by 37
Mitochondrial Dysfunction, Proteotoxicity, and Aging
Hipkiss, A. R. (2010) · Advances in clinical chemistry · doi:10.1016/s0065-2423(10)50007-6 · Cited by 35
Mitochondrial dysfunction, proteotoxicity, and aging: causes or effects, and the possible impact of NAD+-controlled protein glycation.
Hipkiss, A. R. (2010) · PubMed · Cited by 34
Inhibition of Transient Receptor Potential Channel Mucolipin-1 (TRPML1) by Lysosomal Adenosine Involved in Severe Combined Immunodeficiency Diseases
Zhong, X. Z., Zou, Y., Sun, X. J., Dong, G., Cao, Q., Pandey, A. N., Rainey, J. K., Zhu, X., & Dong, X. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.743963 · Cited by 33
Genetic Regulation of Caenorhabditis elegans Lysosome Related Organelle Function
Soukas, A. A., Carr, C. E., & Ruvkun, G. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003908 · Cited by 34
Novel turn-on fluorescent biosensors for selective detection of cellular Fe3+ in lysosomes: Thiophene as a selectivity-tuning handle for Fe3+ sensors
Lim, B., Baek, B., Jang, K., Lee, N. K., Lee, J. H., Lee, Y., Kim, J., Kang, S. W., Park, J., Kim, S., et al. (2019) · Dyes and Pigments · doi:10.1016/j.dyepig.2019.05.008 · Cited by 34
Oxidative Damage to Proteins
Davies, M. J. (2012) · Wiley eBooks · doi:10.1002/9781119953678.rad045 · Cited by 38
Biphasic ROS production, p53 and BIK dictate the mode of cell death in response to DNA damage in colon cancer cells
Kütük, Ö., Aytan, N., Karakaş, B., Kurt, A. G., Acikbas, U., Temel, Ş. G., & Başağa, H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182809 · Cited by 33
Repair activity and crystal adhesion inhibition of polysaccharides with different molecular weights from red algae Porphyra yezoensis against oxalate-induced oxidative damage in renal epithelial cells
Sun, X., Zhang, H., Liu, J., & Ouyang, J. (2019) · Food & Function · doi:10.1039/c8fo02556h · Cited by 33
Mini-Review on Lipofuscin and Aging: Focusing on The Molecular Interface, The Biological Recycling Mechanism, Oxidative Stress, and The Gut-Brain Axis Functionality
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
Sequential detection of H2S and HOBr with a novel lysosome-targetable fluorescent probe and its application in biological imaging
Mu, S., Zhang, J., Gao, H. J., Wang, Y., Rizvi, S. F. A., Ding, N., Liu, X., Wu, L., & Zhang, H. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2021.126898 · Cited by 32
Neurobiological mechanisms of mood disorders: Stress vulnerability and resilience
Pereira, C. M., Castro, F. C. D. A. Q., Barcelos, R. M., Chiepe, K. C. M. B., Rossoni, J. V., Ambrósio, R. P., Chiarelli-Neto, O., & Pesarico, A. P. (2022) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2022.1006836 · Cited by 36
Lysosome-targetable red-emitting ratiometric fluorescent probe for hypobromous acid imaging in living cells
Qu, W., Li, K.-B., Han, D., Zhong, X.-X., Chen, C., Liang, X.-X., & Liu, H. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.126826 · Cited by 31
Low doses of urban air particles from Buenos Aires promote oxidative stress and apoptosis in mice lungs
Martin, S., Fernandez-Alanis, E., Delfosse, V. C., Evelson, P., Yakisich, J. S., Saldiva, P. H. N., & Tasat, D. R. (2010) · Inhalation Toxicology · doi:10.3109/08958378.2010.523030 · Cited by 31
Heme Oxygenase 1 in Schwann Cells Regulates Peripheral Nerve Degeneration Against Oxidative Stress
Kim, M., Kim, H., Kim, D., Kim, D., Huh, Y., Park, C., Chung, H.-J., Jung, J., & Jeong, N. Y. (2019) · ASN NEURO · doi:10.1177/1759091419838949 · Cited by 31
Tacrine induces apoptosis through lysosome- and mitochondria-dependent pathway in HepG2 cells
Gao, C., Ding, Y., Zhong, L., Jiang, L., Geng, C., Yao, X., & Cao, J. (2014) · Toxicology in Vitro · doi:10.1016/j.tiv.2014.02.001 · Cited by 30
In Situ Observation of Lysosomal Hypobromous Acid Fluctuations in the Brain of Mice with Depression Phenotypes by Two-Photon Fluorescence Imaging
Zhu, H., Jia, P., Wang, X., Tian, Y., Liu, C., Li, X., Wang, K., Li, P., Zhu, B., & Tang, B. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01884 · Cited by 29
Camalexin-Induced Apoptosis in Prostate Cancer Cells Involves Alterations of Expression and Activity of Lysosomal Protease Cathepsin D
Smith, B. A., Randle, D. D., Mezencev, R., Thomas, L. D., Hinton, C. V., & Odero-Marah, V. (2014) · Molecules · doi:10.3390/molecules19043988 · Cited by 30
Increased In Vitro Lysosomal Function in Oxidative Stress-Induced Cell Lines
Yoon, J., Bang, S. H., Park, J., Chang, S.-T., Kim, Y., & Min, J. (2010) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-010-9104-z · Cited by 28
Subcellular Drug Distribution: Exploring Organelle-Specific Characteristics for Enhanced Therapeutic Efficacy
Liu, X., Li, M., & Woo, S. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16091167 · Cited by 28
Recent progress in organelle-targeting fluorescent probes for the detection of peroxynitrite
Li, L., Wang, C., Hu, J., & Chen, W. (2024) · Chemical Communications · doi:10.1039/d4cc03452j · Cited by 27
Imaging of cellular aging in human retinal blood vessels
Catita, J., López‐Luppo, M., Ramos, D., Nacher, V., Navarro, M., Carretero, A., Sánchez‐Chardi, A., Mendes-Jorge, L., Rodríguez‐Baeza, A., & Ruberte, J. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.03.019 · Cited by 25
Castanea sativa Mill. Bark Extract Protects U‐373 MG Cells and Rat Brain Slices Against Ischemia and Reperfusion Injury
Santulli, C., Brizi, C., Micucci, M., Ambra, D. G., Cristofaro, A. D., Bracco, F., Lucia, P. G., Ilaria, D. P., Budriesi, R., Chiarini, A., et al. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25760 · Cited by 27
Physical and chemical modulation of lipid rafts by a dietary n-3 polyunsaturated fatty acid increases ethanol-induced oxidative stress
Aliche-Djoudi, F., Podechard, N., Chevanne, M., Nourissat, P., Catheline, D., Legrand, P., Dimanche‐Boitrel, M., Lagadic‐Gossmann, D., & Sergent, O. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.031 · Cited by 26
Pre-clinical Mouse Models of Neurodegenerative Lysosomal Storage Diseases
Favret, J., Weinstock, N. I., Feltri, M. L., & Shin, D. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00057 · Cited by 28
Engaging the Lysosome and Lysosome-Dependent Cell Death in Cancer
Berg, A. L., Rowson-Hodel, A. R., Wheeler, M. R., Hu, M., Free, S. R., & Carraway, K. L. (2022) · Exon Publications eBooks · doi:10.36255/exon-publications-breast-cancer-lysosome · Cited by 26
Annexins: Ca2+ Effectors Determining Membrane Trafficking in the Late Endocytic Compartment
Enrich, C., Rentero, C., Meneses‐Salas, E., Tebar, F., & Grewal, T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55858-5_14 · Cited by 26
‘Patchiness’ and basic cancer research: unravelling the proteases
Soond, S. M., Kozhevnikova, M. V., & Zamyatnin, A. A. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1632639 · Cited by 26
Aspirin Eugenol Ester Reduces H2O2-Induced Oxidative Stress of HUVECs via Mitochondria-Lysosome Axis
Huang, M., Yang, Y., Liu, X.-W., Qin, Z., & Li, J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8098135 · Cited by 26
A neuronal aging pattern unique to humans and common chimpanzees
Gilissen, E., Leroy, K., Yilmaz, Z., Kövari, E., Bouras, C., Boom, A., Poncelet, L., ERWIN, J. M., Sherwood, C. C., Hof, P. R., et al. (2014) · Brain Structure and Function · doi:10.1007/s00429-014-0931-5 · Cited by 26
Loss of lysosomal protein NCU-G1 results in spontaneous liver fibrosis with accumulation of lipofuscin and iron in Kupffer cells
Kong, X. Y., Nesset, C. K., Daμμe, M., Løberg, E. M., Lübke, T., Mæhlen, J., Andersson, K. B., Lorenzo, P. I., Roos, N., Thoresen, G. H., et al. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014050 · Cited by 25
A network pharmacology-based strategy for predicting the protective mechanism of Ginkgo biloba on damaged retinal ganglion cells
Hua, Y. U., Li-Hong, D. O. N. G., ZHANG, Y., & Qiang, L. I. U. (2022) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(21)60109-7 · Cited by 24
Reactive oxygen species and autophagy play a role in survival and differentiation of the phytopathogen Moniliophthora perniciosa
Pungartnik, C., Melo, S. C. O., Basso, T. S., Macena, W. G., Cascardo, J. C. M., & Brendel, M. (2009) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2009.03.007 · Cited by 24
Exploding vesicles
Zhu, T. F., & Szostak, J. W. (2011) · Journal of Systems Chemistry · doi:10.1186/1759-2208-2-4 · Cited by 25
Autophagy and Heart Failure: A Possible Role for Homocysteine
Vacek, T. P., Vacek, J. C., Tyagi, N., & Tyagi, S. C. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9281-6 · Cited by 24
Analysis of the coding sequences of clownfish reveals molecular convergence in the evolution of lifespan
Sahm, A., Pagán, P., Bens, M., Mutalipassi, M., Lucas-Sánchez, A., Ruiz, J. D. C., Görlach, M., & Cellerino, A. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1409-0 · Cited by 25
Morphological Stages of Mitochondrial Vacuolar Degeneration in Phenylephrine-Stressed Cardiac Myocytes and in Animal Models and Human Heart Failure
Chaanine, A. H. (2019) · Medicina · doi:10.3390/medicina55060239 · Cited by 23
PKG and NHR-49 signalling co-ordinately regulate short-term fasting-induced lysosomal lipid accumulation in C. elegans
Huang, W.-M., Li, Z., Xu, Y.-J., Wang, W., Zhou, M.-G., Zhang, P., Liu, P.-S., Xu, T., & Wu, Z.-X. (2014) · Biochemical Journal · doi:10.1042/bj20140191 · Cited by 23
Autophagy upregulation and loss of NF-κB in oxidative stress-related immunodeficient SAMP8 mice
Caballero, B., Vega‐Naredo, I., Sierra, V., de Gonzalo‐Calvo, D., Medrano‐Campillo, P., Guerrero, J. M., Tolivia, D., Rodríguez‐Colunga, M. J., & Coto‐Montes, A. M. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.09.001 · Cited by 22
Depleted Uranium Disturbs Immune Parameters in Zebrafish, Danio rerio: An Ex Vivo/In Vivo Experiment
Gagnaire, B., Bado‐Nilles, A., & Sánchez, W. (2014) · Archives of Environmental Contamination and Toxicology · doi:10.1007/s00244-014-0022-x · Cited by 23
Deletion of lec-10, a Galectin-Encoding Gene, Increases Susceptibility to Oxidative Stress in Caenorhabditis elegans
Nemoto‐Sasaki, Y., & Kasai, K. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.1973 · Cited by 21
Mitochondrial Dysfunction in Cardiac Disease: The Fort Fell
PARASKEVAIDIS, I. A., Kourek, C., Farmakis, D. T., & Tsougos, E. (2024) · Biomolecules · doi:10.3390/biom14121534 · Cited by 22
Ultrastructural Analysis in Preclinical Safety Evaluation
Fagerland, J. A., Wall, H. G., Pandher, K., LeRoy, B. E., & Gagné, G. D. (2012) · Toxicologic Pathology · doi:10.1177/0192623311430239 · Cited by 21
Comparison of three different cell viability assays for evaluation of vanadyl sulphate cytotoxicity in a Chinese hamster ovary K1 cell line
Zwolak, I. (2014) · Toxicology and Industrial Health · doi:10.1177/0748233714544190 · 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
Atlantic salmon (Salmo salar) muscle structure integrity and lysosomal cathepsins B and L influenced by dietary n-6 and n-3 fatty acids
Bahuaud, D., Østbye, T.-K. K., Torstensen, B. E., Rørå, M. B., Ofstad, R., Veiseth-Kent, E., Thomassen, M. S., & Ruyter, B. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.11.039 · Cited by 21
Mitochondrial Pathobiology and Metabolic Remodeling in Progression to Overt Systolic Heart Failure
Chaanine, A. H., LeJemtel, T. H., & Delafontaine, P. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9113582 · Cited by 20
Role of Lysosomal Acidification Dysfunction in Mesenchymal Stem Cell Senescence
Zhang, W., Bai, J., Hang, K., Xu, J., Zhou, C., Li, L., Wang, Z., Wang, Y., Wang, K., & Xue, D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.817877 · Cited by 21
Aggregatibacter actinomycetemcomitans leukotoxin induces cytosol acidification in LFA‐1 expressing immune cells
Balashova, N. V., Dhingra, A., Boesze‐Battaglia, K., & Lally, E. T. (2015) · Molecular Oral Microbiology · doi:10.1111/omi.12136 · Cited by 20
In vitrocell-based assays for evaluation of antioxidant potential of plant-derived products
da Silva, L. C. N., Filho, C. M. B., de Paula, R. A., Figueiredo, C. S. S. E. S., de Souza, L. I. O., da Silva, M. V., Correia, M. T. D. S., & de Figueiredo, R. C. B. Q. (2016) · Free Radical Research · doi:10.1080/10715762.2016.1193668 · Cited by 20
Heat shock proteins: keys to healthy ageing?
Rodgers, K. J., Ford, J. L., & Brunk, U. T. (2009) · Redox Report · doi:10.1179/135100009x392593 · Cited by 19
Self-citation
A two-photon fluorescent probe based on link-anthocyanin for detecting cysteine in nucleoli and lysosomes
Li, H., Chen, R., Jiang, Y., Liu, W., Chen, C., Li, Z., & Liu, W. (2020) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2020.129159 · Cited by 18
A simple pyridine-based highly specific fluorescent probe for tracing hypochlorous acid in lysosomes of living cells
Wang, K., Liu, Y., Liu, C., Zhu, H., Li, X., Zhang, F., Gao, N., Pang, X., Sheng, W., & Zhu, B. (2021) · New Journal of Chemistry · doi:10.1039/d1nj02256c · Cited by 18
Effect of Dried Apple Pomace (DAP) as a Feed Additive on Antioxidant System in the Rumen Fluid
Bartel, I., Koszarska, M., Wysocki, K., Kozłowska, M., Szumacher‐Strabel, M., Cieślak, A., Wyrwał, B., Szejner, A., Strzałkowska, N., Horbańczuk, J. O., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810475 · Cited by 18
Hyperglycemia-induced cardiomyocyte death is mediated by lysosomal membrane injury and aberrant expression of cathepsin D
Kobayashi, S., Zhao, F., Kobayashi, T., Hagiwara, M., Kaminaris, A., Li, C., Cai, F., Huang, Y., & Liang, Q. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.12.051 · Cited by 18
Use of intracellular transport processes for targeted drug delivery into a specified cellular compartment
Rosenkranz, A. A., Ulasov, A. V., Slastnikova, T. A., Khramtsov, Y. V., & Sobolev, A. S. (2014) · Biochemistry (Moscow) · doi:10.1134/s0006297914090090 · Cited by 18
Oxidised protein metabolism: recent insights
Samardzic, K., & Rodgers, K. J. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0124 · Cited by 18
SIRT1 Activation Using CRISPR/dCas9 Promotes Regeneration of Human Corneal Endothelial Cells through Inhibiting Senescence
Joo, H. J., Ma, D. J., Hwang, J. S., & Shin, Y. J. (2020) · Antioxidants · doi:10.3390/antiox9111085 · Cited by 17
Making Connections: p53 and the Cathepsin Proteases as Co-Regulators of Cancer and Apoptosis
Soond, S. M., Savvateeva, L. V., Makarov, V. A., Gorokhovets, N. V., Townsend, P. A., & Zamyatnin, A. A. (2020) · Cancers · doi:10.3390/cancers12113476 · Cited by 18
Functional characterization of starvation-induced lysosomal activity in Saccharomyces cerevisiae
Yoon, J., Chang, S.-T., Park, J., Kim, Y., & Min, J. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2755-4 · Cited by 17
Reduced mitochondria membrane potential and lysosomal acidification are associated with decreased oligomeric Aβ degradation induced by hyperglycemia: A study of mixed glia cultures
Huang, Y., Hsu, S.-M., Shie, F., Shiao, Y., Chao, L.-J., Chen, H., Yao, H.-H., Chien, M. A., Lin, C., & Tsay, H.-J. (2022) · PLoS ONE · doi:10.1371/journal.pone.0260966 · Cited by 17
A novel near-infrared ratiometric fluorescent probe targeting lysosomes for imaging HOCl in vitro and in vivo
Chen, X., Jiang, D., Jiang, C., & Yao, C. (2022) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2022.121966 · Cited by 17
Human Bladder Smooth Muscle Cell Damage in Disturbed Oxygen Tension
Azadzoi, K. M., Yalla, S. V., & Siroky, M. B. (2011) · Urology · doi:10.1016/j.urology.2011.06.034 · Cited by 17
A subcellular study on reactive oxygen species generation by PFAS in HepG2 cells
Amstutz, V. H., Mircheva, A., Cengo, A., Dubois, L. J., Sijm, D. T. H. M., & Vrolijk, M. F. (2025) · Scientific Reports · doi:10.1038/s41598-025-07503-7 · Cited by 20
Attenuation of iron‐binding proteins in ARPE ‐19 cells reduces their resistance to oxidative stress
Karlsson, M., & Kurz, T. (2016) · Acta Ophthalmologica · doi:10.1111/aos.13076 · Cited by 16
Self-citation
Approaching a Unified Theory for Particle-Induced Inflammation
Bunderson‐Schelvan, M., Hamilton, R. F., Trout, K. L., Jessop, F., Gulumian, M., & Holian, A. (2015) · Current topics in environmental health and preventive medicine · doi:10.1007/978-4-431-55732-6_3 · Cited by 15
Antioxidant and Free Radical Scavenging Potential of Yakuchinone B Derivatives in Reduction of Lipofuscin Formation Using H2O2-Treated Neuroblastoma Cells
Bayati, S., & Yazdanparast, R. (1996) · Europe PMC (PubMed Central) · doi:10.6091/ibj.1010.2012 · Cited by 15
Protein Redox-Regulation Mechanisms in Aging
Çakatay, U. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-602-3_1 · Cited by 15
The dependence of enhanced lysosomal activity on the cellular aging of bovine aortic endothelial cells
Yoon, J., Kim, K., Choi, Y. W., Shin, H. S., Kim, Y., & Min, J. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0415-8 · Cited by 15
Autophagy and Myocardial Remodeling
Chaanine, A. H. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.02.067 · Cited by 15
Investigation of cerebrocortical and cerebellar pathology in canine fucosidosis and comparison to aged brain
Kondagari, G. S., Yang, J. L., & Taylor, R. M. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.026 · Cited by 14
ABT-737, a Bcl-2 Selective Inhibitor, and Chloroquine Synergistically Kill Renal Cancer Cells
Yin, P., Jia, J.-P., Li, J., Song, Y., Zhang, Y., & Chen, F. (2016) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504016x14587366983838 · Cited by 14
Analysis of cytotoxic effects of chlorhexidine gluconate as antiseptic agent on human blood lymphocytes
Salimi, A., Alami, B., & Pourahmad, J. (2017) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.21918 · Cited by 14
Oxidative-Stress-Associated Proteostasis Disturbances and Increased DNA Damage in the Hippocampal Granule Cells of the Ts65Dn Model of Down Syndrome
Puente-Bedia, A., Berciano, M. T., Martínez‐Cué, C., Lafarga, M., & Rueda, N. (2022) · Antioxidants · doi:10.3390/antiox11122438 · Cited by 13
Cathepsin-B dependent autophagy ameliorates steatoheaptitis in chronic exercise rats.
Guo, R., Yu, Q., Liong, E. C., Fung, M., & Tipoe, G. L. (2020) · PubMed · doi:10.14670/hh-18-204 · Cited by 12
The mRNA level of the galectin-10 of Angiostrongylus cantonensis induced by reactive oxygen stress
Liu, L.-H., He, H.-J., Lv, Z., Wei, J., Zeng, X., Liang, J., Zheng, H., Yu, X., Sun, X., & Wu, Z. (2012) · Parasitology Research · doi:10.1007/s00436-012-3210-5 · Cited by 12
The Different Biomarkers in the Assessment of the Marine Environmental Quality Using the Representative Species Mytilus trossulus
Istomina, A. A., Mazur, A. A., Chelomin, V. P., Kukla, S. P., Slobodskova, V. V., Zvyagintsev, A., Kolosova, L. F., Zhukovskaya, A. F., & Fedorets, Y. V. (2020) · Water Air & Soil Pollution · doi:10.1007/s11270-020-04782-w · Cited by 12
Impaired Lysosomal Cobalamin Transport in Alzheimer's Disease
Zhao, H., Li, H., Ruberu, K. R., & Garner, B. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140681 · Cited by 12

Authors: Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T.
Affiliations: Linköping University (SE)
Linköping University Hospital (SE)
Corresponding author: Brunk, Ulf T.
Venue: Biochimica et Biophysica Acta (BBA) - General Subjects
Publisher: Elsevier BV
Published: 2008-11
Volume: 1780
Issue: 11
Pages: 1291-1303
ISSN: 0304-4165 (ISSN-L)
DOI: 10.1016/j.bbagen.2008.01.009
OpenAlex: W2056367295
Cited by: 287
References: 129
Citations by year: 2026: 13 · 2025: 11 · 2024: 9 · 2023: 7 · 2022: 13 · 2021: 14 · 2020: 14 · 2019: 21 · 2018: 13 · 2017: 13 · 2016: 21 · 2015: 11 · 2014: 23 · 2013: 16 · 2012: 15
FWCI: 2.56
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords: lysosomes, oxidative stress, aging, apoptosis, autophagy, iron release, lipofuscin, lysosomal destabilization, hydrogen peroxide, mitochondrial dysfunction, lysosomal enzymes, necrosis, starvation survival
MeSH terms: Aging, Animals, Humans, Iron, Lysosomes, Mitosis, Apoptosis, Oxidative Stress

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Lysosomes and oxidative stress in aging and apoptosis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks