Lysosomes and oxidative stress in aging and apoptosis
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
Cites
Statistics
Claims the paper makes
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?
ROS play a prominent causal role in LMP, as H2O2-driven luminal production of hydroxyl radicals by Fenton reactions destabilizes the lysosomal membrane upon lipid peroxidation.
“ROS play a prominent causal role in LMP, not only as the H2O2-driven luminal production of hydroxyl radicals by Fenton reactions destabilizes the lysosomal membrane upon lipid peroxidation [766, 767]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [766]
Damaged mitochondria are insensitive to mitophagy, and consequently mitochondrial number and size are not properly regulated in senescent cells.
“Moreover, damaged mitochondria are insensitive to mitophagy (i.e., selective autophagy of mitochondria), and consequently, mitochondrial number and size are not properly regulated in senescent cells [214].”
From Mechanisms and Regulation of Cellular Senescence (2021) · cites this paper as [214]
Cites
1 retracted
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 · see citing works
RetractedThe 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 · see citing works
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 · see citing works
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 3,560 · see citing works
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033 · see citing works
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,531 · see citing works
Ohkuma, S., & Poole, B. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.7.3327 · Cited by 2,185 · see citing works
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 1,938 · see citing works
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 1,737 · see citing works
Autophagy: molecular machinery for self-eating
Yorimitsu, T., & Klionsky, D. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401765 · Cited by 1,540 · see citing works
Lysosomes and autophagy in cell death control
Kroemer, G., & Jäättelä, M. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1738 · Cited by 1,291 · see citing works
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967 · see citing works
Brunk, U. T., & Terman, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00959-0 · Cited by 919 · see citing works
Self-citationHayashi, T., & Sherman, F. G. (1959) · Science · doi:10.1126/science.129.3341.100 · Cited by 867 · see citing works
Autophagy and aging: The importance of maintaining "clean" cells
Cuervo, A. M., Bergamini, E., Brunk, U. T., Dröge, W., Ffrench, M., & Terman, A. (2005) · Autophagy · doi:10.4161/auto.1.3.2017 · Cited by 792 · see citing works
Self-citationStudies on the mechanisms of autophagy: formation of the autophagic vacuole.
Dunn, W. A. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.6.1923 · Cited by 787 · see citing works
Ultrastructural Pathology of the Cell and Matrix
(1988) · Elsevier eBooks · doi:10.1016/c2013-0-06247-0 · Cited by 785 · see citing works
Michalovitz, D., Halevy, O., & Oren, M. (1990) · Cell · doi:10.1016/0092-8674(90)90113-s · Cited by 769 · see citing works
Guicciardi, M. E., Leist, M., & Gores, G. J. (2004) · Oncogene · doi:10.1038/sj.onc.1207512 · Cited by 716 · see citing works
The P53 pathway: what questions remain to be explored?
Levine, A. J., Hu, W., & Feng, Z. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401910 · Cited by 654 · see citing works
Barja, G. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.07.005 · Cited by 653 · see citing works
The autophagosomal–lysosomal compartment in programmed cell death
Bursch, W. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400852 · Cited by 616 · see citing works
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545 · see citing works
Arosio, P., & Levi, S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00842-0 · Cited by 543 · see citing works
Labile iron pool: the main determinant of cellular response to oxidative stress
Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 529 · see citing works
A block of autophagy in lysosomal storage disorders
Settembre, C., Fraldi, A., Jahreiss, L., Spampanato, C., Venturi, C. B., Medina, D. L., de Pablo, R., Tacchetti, C., Rubinsztein, D. C., & Ballabio, A. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm289 · Cited by 500 · see citing works
Ku, H., Brunk, U. T., & Sohal, R. S. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90165-q · Cited by 488 · see citing works
Self-citationLysosomal Membrane Permeabilization Induces Cell Death in a Mitochondrion-dependent Fashion
Boya, P., Andreau, K., Poncet, D., Zamzami, N., Perfettini, J.-L., Metivier, D., Ojcius, D. M., Jäättelä, M., & Kroemer, G. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021952 · Cited by 483 · see citing works
Cirman, T., Bender, K. O., Droga-Mazovec, G., Türk, V., Reed, J. C., Myers, R., Salvesen, G. S., & Turk, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308347200 · Cited by 479 · see citing works
Bidère, N., Lorenzo, H. K., Carmona, S., Laforge, M., Harper, F., Dumont, C., & Senik, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301911200 · Cited by 435 · see citing works
Duve, C. D. (2005) · Nature Cell Biology · doi:10.1038/ncb0905-847 · Cited by 422 · see citing works
Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae
Suzuki, K., & Ohsumi, Y. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.096 · Cited by 394 · see citing works
Eaton, J. W., & Qian, M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00772-4 · Cited by 389 · see citing works
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 · see citing works
Self-citationSphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590335 · Cited by 379 · see citing works
Self-citationOxidant-induced DNA damage of target cells.
Schraufstätter, I. U., Hyslop, P. A., Jackson, J. H., & Cochrane, C. G. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113660 · Cited by 373 · see citing works
Oxidative Stress, Accumulation of Biological 'Garbage', and Aging
Terman, A., & Brunk, U. T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.197 · Cited by 363 · see citing works
Self-citationStudies on the mechanisms of autophagy: maturation of the autophagic vacuole.
Dunn, W. A. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.6.1935 · Cited by 362 · see citing works
Antioxidant role of metallothioneins: a comparative overview.
Viarengo, A., Burlando, B., Ceratto, N., & Panfoli, I. (2000) · PubMed · Cited by 341 · see citing works
Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338 · see citing works
Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
Heinrich, M., Neumeyer, J., Jakob, M., Hallas, C., Tchikov, V., Winoto‐Morbach, S., Wickel, M., Schneider‐Brachert, W., Trauzold, A., Hethke, A., et al. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401382 · Cited by 333 · see citing works
Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells
Martı́nez–Zaguilán, R., Lynch, R. M., Martinez, G. M., & Gillies, R. J. (1993) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1993.265.4.c1015 · Cited by 291 · see citing works
Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
Zhao, M., Antunes, F., Eaton, J. W., & Brunk, U. T. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03765.x · Cited by 288 · see citing works
Self-citationAutophagy, organelles and ageing
Terman, A., Gustafsson, B., & Brunk, U. T. (2007) · The Journal of Pathology · doi:10.1002/path.2094 · Cited by 287 · see citing works
Self-citationAntunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560549 · Cited by 286 · see citing works
Self-citationPhoto-Oxidative Disruption of Lysosomal Membranes Causes Apoptosis of Cultured Human Fibroblasts
Brunk, U. T., Dalen, H., Roberg, K. B., & Hellquist, H. B. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00007-5 · Cited by 283 · see citing works
Self-citationAutophagy in cardiac myocyte homeostasis, aging, and pathology
Terman, A., & Brunk, U. T. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.08.014 · Cited by 266 · see citing works
Self-citationTumor Acidity, Chemoresistance and Proton Pump Inhibitors
Milito, A. D., & Fais, S. (2005) · Future Oncology · doi:10.2217/14796694.1.6.779 · Cited by 264 · see citing works
Release of iron from ferritin requires lysosomal activity
Kidane, T. Z., Sauble, E., & Linder, M. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00505.2005 · Cited by 263 · see citing works
Hypoxia, glucose metabolism and the Warburg’s effect
Bartrons, R., & Caro, J. (2007) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-007-9080-3 · Cited by 260 · see citing works
Autophagy Is Disrupted in a Knock-in Mouse Model of Juvenile Neuronal Ceroid Lipofuscinosis
Cao, Y., Espinola, J. A., Fossale, E., Massey, A. C., Cuervo, A. M., MacDonald, M. E., & Cotman, S. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602180200 · Cited by 254 · see citing works
Ultrastructural Pathology of the Cell and Matrix
de Harven, É. (1988) · Elsevier eBooks · doi:10.1016/c2013-0-06246-9 · Cited by 253 · see citing works
Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235 · see citing works
Lysosomal involvement in apoptosis
Brunk, U. T., Neužil, J., & Eaton, J. W. (1998) · Pathophysiology · doi:10.1016/s0928-4680(98)80586-5 · Cited by 232 · see citing works
Self-citationRole of Iron in Neurodegenerative Disorders
Berg, D., & Youdim, M. B. H. (2006) · Topics in Magnetic Resonance Imaging · doi:10.1097/01.rmr.0000245461.90406.ad · Cited by 227 · see citing works
Lysosomal destabilization in p53-induced apoptosis
Yuan, X., Li, W., Dalen, H., Lotem, J., Kama, R., Sachs, L., & Brunk, U. T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092135599 · Cited by 226 · see citing works
Self-citationThe lysosomal–mitochondrial axis theory of postmitotic aging and cell death
Terman, A., Gustafsson, B., & Brunk, U. T. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.04.013 · Cited by 217 · see citing works
Self-citationCuervo, A. M., & Dice, J. F. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00075-9 · Cited by 215 · see citing works
Synthesis, modifications, and turnover of proteins during aging
Rattan, S. I. S. (1996) · Experimental Gerontology · doi:10.1016/0531-5565(95)02022-5 · Cited by 208 · see citing works
Degradation of Proteasomes by Lysosomes in Rat Liver
Cuervo, A. M., Palmer, A., Rivett, A. J., & Knecht, E. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0792p.x · Cited by 207 · see citing works
Apoptotic Pathways: Involvement of Lysosomal Proteases
Turk, B., Stoka, V., Pungerčar, J. R., Cirman, T., Droga-Mazovec, G., Oreic, K., & Türk, V. (2002) · Biological Chemistry · doi:10.1515/bc.2002.112 · Cited by 206 · see citing works
‘The Metabolism of Tumours’: 70 Years Later
Semenza, G. L., Artemov, D., Bedi, A., Bhujwalla, Z. M., Chiles, K. A., Feldser, D. M., Laughner, E., Ravi, R. K., Simons, J. W., Taghavi, P., et al. (2001) · Novartis Foundation symposium · doi:10.1002/0470868716.ch17 · Cited by 203 · see citing works
Liu, X., Jin, W., & Theil, E. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0636928100 · Cited by 203 · see citing works
Autophagy, ageing and apoptosis: The role of oxidative stress and lysosomal iron
Kurz, T., Terman, A., & Brunk, U. T. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.01.013 · Cited by 199 · see citing works
Self-citationGlaumann, H., Ericsson, J. L. E., & Marzella, L. (1981) · International review of cytology · doi:10.1016/s0074-7696(08)61288-7 · Cited by 198 · see citing works
The role of α-synuclein in neurodegenerative diseases
Bennett, M. C. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.10.010 · Cited by 195 · see citing works
Cathepsin B and its role(s) in cancer progression
Podgorski, I., & Sloane, B. F. (2003) · Biochemical Society Symposia · doi:10.1042/bss0700263 · Cited by 195 · see citing works
Brunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 182 · see citing works
Self-citationBreast cancer cells have a high capacity to acidify extracellular milieu by a dual mechanism
Montcourrier, P., Silver, I. A., Farnoud, R., Bird, I., & Rochefort, H. (1997) · Clinical & Experimental Metastasis · doi:10.1023/a:1018446104071 · Cited by 176 · see citing works
Koorts, A. M., & Viljoen, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701318583 · Cited by 164 · see citing works
Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
Radisky, D. C., & Kaplan, J. (1998) · Biochemical Journal · doi:10.1042/bj3360201 · Cited by 163 · see citing works
Pisoni, R. L., Acker, T. L., Lisowski, K. M., Lemons, R. M., & Thoene, J. G. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.2.327 · Cited by 162 · see citing works
The effect of age on formation and elimination of autophagic vacuoles in mouse hepatocytes
Terman, A. (2009) · Gerontology · doi:10.1159/000213753 · Cited by 162 · see citing works
Self-citationBrunk, U. T., & Ericsson, J. L. E. (1972) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(72)90080-9 · Cited by 147 · see citing works
Self-citationPower, sex, suicide: mitochondria and the meaning of life
(2006) · Choice Reviews Online · doi:10.5860/choice.43-4653 · Cited by 146 · see citing works
Metallothionein protects against oxidative stress-induced lysosomal destabilization
Baird, S. K., Kurz, T., & Brunk, U. T. (2006) · Biochemical Journal · doi:10.1042/bj20051143 · Cited by 145 · see citing works
Self-citationKaushik, S., & Cuervo, A. M. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.007 · Cited by 145 · see citing works
Cathepsin D: A protease involved in breast cancer metastasis
Rochefort, H., Capony, F., & Garcia, M. (1990) · Cancer and Metastasis Reviews · doi:10.1007/bf00049522 · Cited by 142 · see citing works
Elleder, M., Sokolová, J., & Hřebı́ček, M. (1997) · Acta Neuropathologica · doi:10.1007/s004010050629 · Cited by 139 · see citing works
Degradation of Proteasomes by Lysosomes in Rat Liver
Cuervo, A. M., Palmer, A., Rivett, A. J., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20203.x · Cited by 137 · see citing works
Autophagy, Mitochondria and Cell Death in Lysosomal Storage Diseases
Kiselyov, K., Jennings, J., Rbaibi, Y., & Chu, C. T. (2007) · Autophagy · doi:10.4161/auto.3906 · Cited by 134 · see citing works
Acidic pH amplifies iron-mediated lipid peroxidation in cells
Schafer, F. Q., & Buettner, G. R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00319-1 · Cited by 134 · see citing works
Aceruloplasminemia, an iron metabolic disorder
Miyajima, H. (2003) · Neuropathology · doi:10.1046/j.1440-1789.2003.00521.x · Cited by 134 · see citing works
Localized Unfolding at the Junction of Three Ferritin Subunits
Takagi, H., Shi, D., Ha, Y., Allewell, N. M., & Theil, E. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18685 · Cited by 130 · see citing works
Werneburg, N. W., Guicciardi, M. E., Bronk, S. F., Kaufmann, S. H., & Gores, G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705671200 · Cited by 126 · see citing works
HISTOCHEMICAL INDICATIONS FOR LYSOSOMAL LOCALIZATION OF HEAVY METALS IN NORMAL RAT BRAIN AND LIVER
Brun, A. E., & Brunk, U. T. (1970) · Journal of Histochemistry & Cytochemistry · doi:10.1177/18.11.820 · Cited by 123 · see citing works
Self-citationZhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 119 · see citing works
Stadtman, E. R., Starke-Reed, P. E., Oliver, C., Carney, J. M., & Floyd, R. A. (1992) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7460-1_7 · Cited by 117 · see citing works
Apoptotic Death of Inflammatory Cells in Human Atheroma
Li, W., Dalen, H., Eaton, J. W., & Yuan, X. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0701.092145 · Cited by 115 · see citing works
Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis
Τενοπούλου, Μ., Doulias, P., Barbouti, A., Brunk, U. T., & Galaris, D. (2005) · Biochemical Journal · doi:10.1042/bj20041650 · Cited by 109 · see citing works
Self-citationNILSSON, S. E. G., Sundelin, S. P., Wihlmark, U., & Brunk, U. T. (2003) · Documenta Ophthalmologica · doi:10.1023/a:1022419606629 · Cited by 107 · see citing works
Self-citationPower, Sex, Suicide: Mitochondria and the Meaning of Life
Alcolado, J. C. (2005) · BMJ · doi:10.1136/bmj.331.7520.851-a · Cited by 107 · see citing works
Insights Into the Diagnosis and Treatment of Lysosomal Storage Diseases
Wenger, D. A., Coppola, S., & Liu, S. (2003) · Archives of Neurology · doi:10.1001/archneur.60.3.322 · Cited by 107 · see citing works
Terman, A., Dalen, H., & Brunk, U. T. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(99)00070-4 · Cited by 106 · see citing works
Self-citationGiant mitochondria do not fuse and exchange their contents with normal mitochondria
Navratil, M., Terman, A., & Arriaga, E. A. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.09.013 · Cited by 94 · see citing works
Self-citationBrain Iron Metabolism and Neurodegenerative Disorders
Sipe, J. C., Lee, P. L., & Beutler, E. (2002) · Developmental Neuroscience · doi:10.1159/000065701 · Cited by 94 · see citing works
Mitochondria in hematopoiesis and hematological diseases
Fontenay, M., Cathelin, S., Amiot, M., Gyan, E., & Solary, É. (2006) · Oncogene · doi:10.1038/sj.onc.1209606 · Cited by 92 · see citing works
Colocalization of iron and ceroid in human atherosclerotic lesions
Lee, F.-Y., Lee, T., Pan, C., Huang, A.-L., & Chau, L. (1998) · Atherosclerosis · doi:10.1016/s0021-9150(98)00033-1 · Cited by 91 · see citing works
Bergamini, E. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.001 · Cited by 89 · see citing works
LIPOFUSCIN IN BOVINE MUSCLE AND BRAIN: A MODEL FOR STUDYING AGE PIGMENT
Jolly, R. D., Douglas, B. V., Davey, P. M., & Roiri, J. E. (2009) · Gerontology · doi:10.1159/000213750 · Cited by 88 · see citing works
Sakaida, I., Kyle, M. E., & Farber, J. L. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10830-4 · Cited by 86 · see citing works
Brunk, U. T., & Dricsson, J. L. E. (1972) · The Histochemical Journal · doi:10.1007/bf01011128 · Cited by 85 · see citing works
Self-citationBaumgartner, H. K., Gerasimenko, J. V., Thorne, C., Ashurst, L. H., Barrow, S. L., Chvanov, M., Gillies, S., Criddle, D. N., Tepikin, A. V., Petersen, O. H., et al. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00103.2007 · Cited by 84 · see citing works
Lysosomal heterogeneity between and within cells with respect to resistance against oxidative stress
Nilsson, E., Ghassemifar, R., & Brunk, U. T. (1997) · The Histochemical Journal · doi:10.1023/a:1026441907803 · Cited by 81 · see citing works
Self-citationYeung, B. H. Y., Huang, D.-C., & Sinicrope, F. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508533200 · Cited by 81 · see citing works
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 · see citing works
Self-citationBarbouti, A., Amorgianiotis, C., Kolettas, E., Kanavaros, P., & Galaris, D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.020 · Cited by 78 · see citing works
Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
Garner, B., Roberg, K. B., & Brunk, U. T. (1998) · Free Radical Research · doi:10.1080/10715769800300121 · Cited by 74 · see citing works
Self-citationVaisman, B. L., Fibach, E., & Konijn, A. M. (1997) · Blood · doi:10.1182/blood.v90.2.831 · Cited by 72 · see citing works
3-Aminopropanal, formed during cerebral ischaemia, is a potent lysosomotropic neurotoxin
Li, W., Yuan, X., Ivanova, S., Tracey, K. J., Eaton, J. W., & Brunk, U. T. (2003) · Biochemical Journal · doi:10.1042/bj20021520 · Cited by 71 · see citing works
Self-citationFerritin iron kinetics and protein turnover in K562 cells.
Roberts, S., & Bomford, A. B. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37407-6 · Cited by 68 · see citing works
ZDOLSEK, J. M., Roberg, K. B., & Brunk, U. T. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90120-j · Cited by 65 · see citing works
Self-citationPersson, H. L., Nilsson, K., & Brunk, U. T. (2001) · Redox Report · doi:10.1179/135100001101536049 · Cited by 56 · see citing works
Self-citationCytocidal effects of atheromatous plaque components: the death zone revisited
Li, W., Östblom, M., Xu, L., Hellsten, A., Leanderson, P., Liedberg, B., Brunk, U. T., Eaton, J. W., & Yuan, X. (2006) · The FASEB Journal · doi:10.1096/fj.06-6114com · Cited by 56 · see citing works
Self-citationMiyawaki, H. (1965) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/34.5.601 · Cited by 51 · see citing works
On the Cytoprotective Role of Ferritin in Macrophages and its Ability to Enhance Lysosomal Stability
Garner, B., Li, W., Roberg, K. B., & Brunk, U. T. (1997) · Free Radical Research · doi:10.3109/10715769709065788 · Cited by 50 · see citing works
Self-citationAutophagy of amyloid beta-protein in differentiated neuroblastoma cells exposed to oxidative stress
Zheng, L. P., Roberg, K. B., Jerhammar, F., Marcusson, J. O., & Terman, A. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.10.035 · Cited by 49 · see citing works
Self-citationLee, S., & Kim, M. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.01.022 · Cited by 46 · see citing works
Pandolfo, M. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_22 · Cited by 44 · see citing works
Lorenzo, K., Ton, P., Clark, J. L., Coulibaly, S., & Mach, L. (2000) · PubMed · Cited by 43 · see citing works
Yu, Z., Li, W., & Brunk, U. T. (2003) · Apmis · doi:10.1034/j.1600-0463.2003.1110607.x · Cited by 41 · see citing works
Self-citationTherapeutic Potential of Iron Chelators in Cancer Therapy
Richardson, D. R. (2002) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4615-0593-8_12 · Cited by 40 · see citing works
Distribution and shifts of ingested marker particles in residual bodies and other lysosomes
Brunk, U. T. (1973) · Experimental Cell Research · doi:10.1016/0014-4827(73)90485-0 · Cited by 38 · see citing works
Self-citationHeavy metal localization and age related accumulation in the rat nervous system
Brun, A. E., & Brunk, U. T. (1973) · Histochemie · doi:10.1007/bf00306305 · Cited by 29 · see citing works
Self-citationTHE PARTITION COEFFICIENTS OF HYDROGEN PEROXIDE BETWEEN WATER AND CERTAIN ORGANIC SOLVENTS.
Walton, J. H., & Lewis, H. A. (1916) · Journal of the American Chemical Society · doi:10.1021/ja02260a013 · Cited by 24 · see citing works
Victor, B. C., & Sloane, B. F. (2007) · Biological Chemistry · doi:10.1515/bc.2007.150 · Cited by 20 · see citing works
Fattoretti, P., Bertoni–Freddari, C., Casoli, T., Stefano, G. D., Solazzi, M., & Corvi, E. (2002) · Archives of Gerontology and Geriatrics · doi:10.1016/s0167-4943(02)00006-7 · Cited by 19 · see citing works
A protease involved in breast cancer metastasis.
Rochefort, H. (1990) · Medical Entomology and Zoology · Cited by 19 · see citing works
Flagged first, then by citations
1 of the 129 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952 · see citing works
Discerning the Chemistry in Individual Organelles with Small‐Molecule Fluorescent Probes
Xu, W., Zeng, Z., Jiang, J., Chang, Y., & Yuan, L. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510721 · Cited by 806 · see citing works
Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response
Olson, O. C., & Joyce, J. A. (2015) · Nature reviews. Cancer · doi:10.1038/nrc4027 · Cited by 703 · see citing works
Lysosomal cell death at a glance
Aits, S., & Jäättelä, M. (2013) · Journal of Cell Science · doi:10.1242/jcs.091181 · Cited by 667 · see citing works
MCOLN1 is a ROS sensor in lysosomes that regulates autophagy
Zhang, X., Cheng, X., Yu, L., Yang, J., Calvo, R., Patnaik, S., Hu, X., Gao, Q., Yang, M., Lawas, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms12109 · Cited by 558 · see citing works
Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548 · see citing works
Mechanisms and Regulation of Cellular Senescence
Roger, L., Tomas, F., & Gire, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313173 · Cited by 395 · see citing works
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 389 · see citing works
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
Emerging mechanisms of lipid peroxidation in regulated cell death and its physiological implications
Zheng, Y., Sun, J., Luo, Z., Li, Y., & Huang, Y. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07244-x · Cited by 349 · see citing works
Kaarniranta, K., Sinha, D., Blasiak, J., Kauppinen, A., Veréb, Z., Salminen, A., Boulton, M. E., & Petrovski, G. (2013) · Autophagy · doi:10.4161/auto.24546 · Cited by 326 · see citing works
Eguchi, T., Kuwahara, T., Sakurai, M., Komori, T., Fujimoto, T., Ito, G., Yoshimura, S., Harada, A., Fukuda, M., Koike, M., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1812196115 · Cited by 317 · see citing works
Wang, F., Gao, F., Lan, M., Yuan, H., Huang, Y., & Liu, J. (2009) · Toxicology in Vitro · doi:10.1016/j.tiv.2009.04.009 · Cited by 314 · see citing works
Nanopreparations for organelle-specific delivery in cancer
Biswas, S., & Torchilin, V. P. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.11.004 · Cited by 292 · see citing works
What does the commonly used DCF test for oxidative stress really show?
Karlsson, M., Kurz, T., Brunk, U. T., NILSSON, S. E. G., & Frennesson, C. I. (2010) · Biochemical Journal · doi:10.1042/bj20100208 · Cited by 278 · see citing works
Self-citationLysosomal degradation of membrane lipids
Kolter, T., & Sandhoff, K. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.021 · Cited by 276 · see citing works
An Activatable Prodrug for the Treatment of Metastatic Tumors
Kim, E. J., Bhuniya, S., Lee, H., Kim, H. M., Cheong, C., Maiti, S., Hong, K. S., & Kim, J. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5077684 · Cited by 269 · see citing works
Mucolipins: Intracellular TRPML1‐3 channels
Cheng, X., Shen, D., Samie, M., & Xu, H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.12.056 · Cited by 262 · see citing works
Distinct mechanisms of ferritin delivery to lysosomes in iron-depleted and iron-replete cells
Asano, T., Komatsu, M., Yamaguchi-Iwai, Y., Ishikawa, F., Mizushima, N., & Iwai, K. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01437-10 · Cited by 265 · see citing works
Aging‐dependent changes of microglial cells and their relevance for neurodegenerative disorders
Von Bernhardi, R., Tichauer, J. E., & Eugenín, J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06537.x · Cited by 258 · see citing works
Age-related macular degeneration (AMD): Alzheimer's disease in the eye?
Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248 · see citing works
The crucial impact of lysosomes in aging and longevity
Carmona‐Gutiérrez, D., Hughes, A. L., Madeo, F., & Ruckenstuhl, C. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.009 · Cited by 244 · see citing works
Microglial aging in the healthy CNS: phenotypes, drivers, and rejuvenation
Wong, W. T. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00022 · Cited by 227 · see citing works
Lysosomal pathways to cell death and their therapeutic applications
Česen, M. H., Pegan, K., Špes, A., & Turk, B. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.03.005 · Cited by 218 · see citing works
The role of lysosomes in iron metabolism and recycling
Kurz, T., Eaton, J. W., & Brunk, U. T. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.08.016 · Cited by 207 · see citing works
Self-citationTumor necrosis factor-mediated cell death: to break or to burst, that’s the question
Herreweghe, F. V., Festjens, N., Declercq, W., & Vandenabeele, P. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0283-0 · Cited by 206 · see citing works
Autophagy in Neuroprotection and Neurodegeneration: A Question of Balance
Cherra, S. J., & Chu, C. T. (2008) · Future Neurology · doi:10.2217/14796708.3.3.309 · Cited by 191 · see citing works
A comparative analysis of the cell biology of senescence and aging
Hwang, E. S., Yoon, G., & Kang, H. T. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0034-2 · Cited by 192 · see citing works
The role of lysosomal rupture in neuronal death
Yamashima, T., & Oikawa, S. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2009.09.003 · Cited by 183 · see citing works
Chemical screening identifies ATM as a target for alleviating senescence
Kang, H. T., Park, J. T., Choi, K., Kim, Y., Choi, H. J. C., Jung, C. W., Lee, Y.-S., & Park, S. C. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2342 · Cited by 184 · see citing works
A central role for dityrosine crosslinking of Amyloid-β in Alzheimer’s disease
Al‐Hilaly, Y. K., Williams, T. L., Stewart-Parker, M., Ford, L. K., Skaria, E., Cole, M., Bucher, W. G., Morris, K. L., Sada, A. A., Thorpe, J. R., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-83 · Cited by 184 · see citing works
Autophagy and Neuronal Cell Death in Neurological DisordersPreprint
Nixon, R. A., & Yang, D.-S. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008839 · Cited by 179 · see citing works
From oxygen to erythropoietin: Relevance of hypoxia for retinal development, health and disease
Caprara, C., & Grimm, C. (2012) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2011.11.003 · Cited by 176 · see citing works
Lipofuscin-bound iron is a major intracellular source of oxidants: Role in senescent cells
Höhn, A., Jung, T., Grimm, S., & Grune, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.030 · Cited by 162 · see citing works
A novel autophagy enhancer as a therapeutic agent against metabolic syndrome and diabetes
Lim, H. J., Lim, Y.-M., Kim, K. H., Jeon, Y. E., Park, K., Kim, J., Hwang, H., Lee, D., Pagire, H. S., Kwon, H. J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03939-w · Cited by 162 · see citing works
Han, R., Zhao, M., Wang, Z., Liu, H., Zhu, S., Huang, L., Wang, Y., Wang, L., Hong, Y., Sha, Y., et al. (2019) · ACS Nano · doi:10.1021/acsnano.9b05169 · Cited by 162 · see citing works
Mitochondria and lysosome-targetable fluorescent probes for HOCl: recent advances and perspectives
Ren, M., Zhou, K., He, L., & Lin, W. (2018) · Journal of Materials Chemistry B · doi:10.1039/c7tb03337k · Cited by 159 · see citing works
Morishige, T., Yoshioka, Y., Inakura, H., Tanabe, A., Yao, X., Narimatsu, S., Monobe, Y., Imazawa, T., Tsunoda, S., Tsutsumi, Y. M., et al. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.05.036 · Cited by 153 · see citing works
Jiang, Z., Hu, Z., Zeng, L., Lu, W., Zhang, H., Li, T., & Xiao, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.011 · Cited by 149 · see citing works
Kubota, C., Torii, S., Hou, N., Saito, N., Yoshimoto, Y., Imai, H., & Takeuchi, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053058 · Cited by 147 · see citing works
Calcium signaling alterations, oxidative stress, and autophagy in aging
Ureshino, R. P., Rocha, K. K., Lopes, G. S., Bincoletto, C., & Smaili, S. S. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5777 · Cited by 143 · see citing works
Ren, M., Li, Z., Deng, B., Wang, L., & Lin, W. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05116 · Cited by 139 · see citing works
Wilkens, V., Kohl, W., & Busch, K. B. (2012) · Journal of Cell Science · doi:10.1242/jcs.108852 · Cited by 134 · see citing works
Myocardial native T1 and extracellular volume with healthy ageing and gender
Rosmini, S., Bulluck, H., Captur, G., Treibel, T. A., Abdel‐Gadir, A., Bhuva, A., Culotta, V., Merghani, A., Fontana, M., Maestrini, V., et al. (2018) · European Heart Journal - Cardiovascular Imaging · doi:10.1093/ehjci/jey034 · Cited by 125 · see citing works
Shao, X., Ding, Z., Zhou, W., Li, Y., Li, Z., Cui, H., Lin, X., Cao, G., Cheng, B., Sun, H., et al. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00952-x · Cited by 120 · see citing works
Oxidative injury triggers autophagy in astrocytes: The role of endogenous zinc
Lee, S., Cho, K. S., & Koh, J. (2009) · Glia · doi:10.1002/glia.20854 · Cited by 115 · see citing works
Metabolic features and regulation in cell senescence
Kwon, S. M., Hong, S. M., Lee, Y.-K., Min, S., & Yoon, G. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.291 · Cited by 111 · see citing works
Viteri, G., Chung, Y. W., & Stadtman, E. R. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.11.006 · Cited by 112 · see citing works
Iron-sensitive fluorescent probes: monitoring intracellular iron pools
Ma, Y., Abbate, V., & Hider, R. C. (2014) · Metallomics · doi:10.1039/c4mt00214h · Cited by 106 · see citing works
Kim, Y., Shin, H.-T., Seo, Y., Byun, H., Yoon, S.-H., Lee, I., Hyun, D., Chung, H. Y., & Yoon, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.120386 · Cited by 98 · see citing works
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 97 · see citing works
Lin, Y., Epstein, D. L., & Liton, P. B. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5410 · Cited by 97 · see citing works
Role of Endolysosomes in HIV-1 Tat-Induced Neurotoxicity
Hui, L., Chen, X., Haughey, N. J., & Geiger, J. D. (2012) · ASN NEURO · doi:10.1042/an20120017 · Cited by 94 · see citing works
Guo, B., Zebda, R., Drake, S. J., & Sayes, C. M. (2009) · Particle and Fibre Toxicology · doi:10.1186/1743-8977-6-4 · Cited by 92 · see citing works
Fan, S., Meng, Q., Saha, T., Sarkar, F. H., & Rosen, E. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3309 · Cited by 92 · see citing works
Quarta, C., Clemmensen, C., Zhu, Z., Yang, B. S., Joseph, S. S., Lutter, D., Yi, C., Graf, E., García‐Cáceres, C., Legutko, B., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.023 · Cited by 88 · see citing works
Ferroptosis in viral infection: the unexplored possibility
Wang, M., Banda, J., Jin, N., Du, S., & Li, C. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00814-1 · Cited by 90 · see citing works
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 88 · see citing works
Wang, X., Zhang, M., Mao, C., Zhang, C., Ma, W., Tang, J., Xiang, D., & Qi, X. (2023) · Phytotherapy Research · doi:10.1002/ptr.7854 · Cited by 83 · see citing works
Spatially and temporally defined lysosomal leakage facilitates mitotic chromosome segregation
Hämälistö, S., Stahl, J. L., Favaro, E., Yang, Q., Liu, B., Christoffersen, L., Loos, B., Boldú, C. G., Joyce, J. A., Reinheckel, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14009-0 · Cited by 80 · see citing works
Autophagy, Redox Signaling, and Ventricular Remodeling
Gurusamy, N., & Das, D. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2524 · Cited by 81 · see citing works
Cystatin C protects neuronal cells against mutant copper-zinc superoxide dismutase-mediated toxicity
Watanabe, S., Hayakawa, T., Wakasugi, K., & Yamanaka, K. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.459 · Cited by 79 · see citing works
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 79 · see citing works
Mechanisms of protein aggregation in the retinal pigment epithelial cells
Kaarniranta, K. (2010) · Frontiers in Bioscience-Elite · doi:10.2741/e198 · Cited by 78 · see citing works
Autophagy in Lysosomal Myopathies
Malicdan, M., & Nishino, I. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00543.x · Cited by 74 · see citing works
A fluorescence turn-on H2O2 probe exhibits lysosome-localized fluorescence signals
Song, D., Lim, J. M., Cho, S., Park, S.-J., Cho, J., Kang, D., Rhee, S. G., You, Y., & Nam, W. (2012) · Chemical Communications · doi:10.1039/c2cc31632c · Cited by 75 · see citing works
Kaarniranta, K., & Salminen, A. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0418-z · Cited by 75 · see citing works
Xu, X., Wells, A. C., Padilla, M. T., Kato, K., Kim, K. C., & Lin, Y. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu159 · Cited by 75 · see citing works
Iron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74 · see citing works
Alverca, E., Andrade, M. A., Dias, E. M., Sam-Bento, F., Batoréu, M. C. C., Jordan, P., Silva, M. J., & Pereira, P. (2009) · Toxicon · doi:10.1016/j.toxicon.2009.04.014 · Cited by 74 · see citing works
Zorzi, E., & Bonvini, P. (2011) · Cancers · doi:10.3390/cancers3043921 · Cited by 73 · see citing works
Cell sensitivity to oxidative stress is influenced by ferritin autophagy
Kurz, T., Gustafsson, B., & Brunk, U. T. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.014 · Cited by 73 · see citing works
Self-citationSendtner, N., Seitz, R., Brandl, N., Müller, M., & Gülow, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010240 · Cited by 75 · see citing works
Oxidative stress induces overgrowth of the Drosophila neuromuscular junction
Milton, V. J., Jarrett, H. E., Gowers, K. H. C., Chalak, S., Briggs, L., Robinson, I. M., & Sweeney, S. T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014511108 · Cited by 66 · see citing works
Autophagy and ageing: Insights from invertebrate model organisms
Lionaki, E., Markaki, M., & Tavernarakis, N. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.05.001 · Cited by 69 · see citing works
Zhu, H., Tamura, T., Fujisawa, A., Nishikawa, Y., Cheng, R., Takato, M., & Hamachi, I. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c02547 · Cited by 67 · see citing works
Oxidative stress in synapse development and function
Milton, V. J., & Sweeney, S. T. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20957 · Cited by 67 · see citing works
Cell Senescence, Multiple Organelle Dysfunction and Atherosclerosis
Machado-Oliveira, G., Ramos, C., Marques, A. R. A., & Vieira, O. V. (2020) · Cells · doi:10.3390/cells9102146 · Cited by 66 · see citing works
Wahrnehmung der chemischen Prozesse in einzelnen Organellen mit niedermolekularen Fluoreszenzsonden
Xu, W., Zeng, Z., Jiang, J., Chang, Y., & Yuan, L. (2016) · Angewandte Chemie · doi:10.1002/ange.201510721 · Cited by 64 · see citing works
Role of Sirt1 During the Ageing Process: Relevance to Protection of Synapses in the Brain
Godoy, J. A., Zolezzi, J. M., Braidy, N., & Inestrosa, N. C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8645-5 · Cited by 60 · see citing works
Lysosomes as a Target of Anticancer Therapy
Trybus, W., Trybus, E., & Król, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032176 · Cited by 61 · see citing works
Jin, Y., Liu, X., Liu, H., Chen, S., Gao, C., Ge, K., Zhang, C., & Zhang, J. (2017) · RSC Advances · doi:10.1039/c7ra01008g · Cited by 61 · see citing works
Liu, J., Zhou, S., Ren, J., Wu, C.-L., & Zhao, Y.-B. (2017) · In Analysis · doi:10.1039/c7an01280b · Cited by 44 · see citing works
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 61 · see citing works
Rôżanowska, M. (2023) · Antioxidants · doi:10.3390/antiox12122111 · Cited by 59 · see citing works
Wang, F., Jiao, C., Liu, J., Yuan, H., Lan, M., & Gao, F. (2011) · Toxicology in Vitro · doi:10.1016/j.tiv.2011.05.019 · Cited by 59 · see citing works
Is autophagy a double-edged sword for the heart?
Gurusamy, N., & Das, D. K. (2009) · Acta Physiologica Hungarica · doi:10.1556/aphysiol.96.2009.3.2 · Cited by 59 · see citing works
Jing, J., & Zhang, J. (2013) · Chemical Science · doi:10.1039/c3sc50807b · Cited by 57 · see citing works
Gao, Y., Zeng, Z., Li, T., Xu, S., Wang, X., Chen, Z., & Lin, C. (2015) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000000977 · Cited by 57 · see citing works
Hipkiss, A. R. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00010 · Cited by 56 · see citing works
A novel EP-involved pathway for iron release from soya bean seed ferritin
Fu, X., Deng, J., Yang, H., Masuda, T., Goto, F., Yoshihara, T., & Zhao, G. (2010) · Biochemical Journal · doi:10.1042/bj20100015 · Cited by 56 · see citing works
Genetics and iron in the systems biology of Parkinson’s disease and some related disorders
Funke, C., Schneider, S. A., Berg, D., & Kell, D. B. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.11.015 · Cited by 54 · see citing works
Structure, Function, and Nutrition of Phytoferritin: A Newly Functional Factor for Iron Supplement
Liao, X., Yun, S., & Zhao, G. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.635914 · Cited by 54 · see citing works
Antioxidant biomedicine: from free radical chemistry to systems biology mechanisms
Koltover, V. K. (2010) · Russian Chemical Bulletin · doi:10.1007/s11172-010-0042-2 · Cited by 54 · see citing works
Magda, D. J., Lecane, P. S., Prescott, J. E., Thiemann, P. A., Ma, X., Dranchak, P. K., TOLENO, D. M., Ramaswamy, K. A., Siegmund, K. D., & Hacia, J. G. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-521 · Cited by 54 · see citing works
The role of redox-mediated lysosomal dysfunction and therapeutic strategies
He, X., Li, X., Tian, W., Li, C., Li, P., Zhao, J., Yang, S., & Li, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115121 · Cited by 53 · see citing works
Aluminum-Induced Entropy in Biological Systems: Implications for Neurological Disease
Shaw, C. A., Seneff, S., Kette, S. D., Tomljenovic, L., Oller, J. W., & Davidson, R. M. (2014) · Journal of Toxicology · doi:10.1155/2014/491316 · Cited by 55 · see citing works
Menezes, C., Alverca, E., Dias, E. M., Sam-Bento, F., & Pereira, P. (2012) · Toxicology in Vitro · doi:10.1016/j.tiv.2012.09.009 · Cited by 51 · see citing works
Chang, W., Bai, J., Tian, S., Ma, M., Li, W., Yin, Y., Deng, R., Cui, J., Li, J., Wang, G., et al. (2017) · Experimental Biology and Medicine · doi:10.1177/1535370216686221 · Cited by 51 · see citing works
- 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)
- 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
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Epidemiology › 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