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
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“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]
In the citing paper
“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]
Citations
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
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
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
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
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
Lysosomes and autophagy in cell death control
Kroemer, G., & Jäättelä, M. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1738 · Cited by 1,322
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
Brunk, U. T., & Terman, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00959-0 · Cited by 919
Self-citationHayashi, T., & Sherman, F. G. (1959) · Science · doi:10.1126/science.129.3341.100 · Cited by 867
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
Self-citationUltrastructural Pathology of the Cell and Matrix
(1988) · Elsevier eBooks · doi:10.1016/c2013-0-06247-0 · Cited by 787
Studies 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
Michalovitz, D., Halevy, O., & Oren, M. (1990) · Cell · doi:10.1016/0092-8674(90)90113-s · Cited by 769
Guicciardi, M. E., Leist, M., & Gores, G. J. (2004) · Oncogene · doi:10.1038/sj.onc.1207512 · Cited by 731
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 661
Barja, G. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.07.005 · Cited by 653
The autophagosomal–lysosomal compartment in programmed cell death
Bursch, W. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400852 · Cited by 620
Arosio, P., & Levi, S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00842-0 · Cited by 553
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
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 538
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 509
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
Self-citationCirman, 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 484
Lysosomal 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
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
Duve, C. D. (2005) · Nature Cell Biology · doi:10.1038/ncb0905-847 · Cited by 422
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
Eaton, J. W., & Qian, M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00772-4 · Cited by 389
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
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
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
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
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
Antioxidant role of metallothioneins: a comparative overview.
Viarengo, A., Burlando, B., Ceratto, N., & Panfoli, I. (2000) · PubMed · Cited by 340
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
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
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 291
Self-citationVacuolar-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
Autophagy, organelles and ageing
Terman, A., Gustafsson, B., & Brunk, U. T. (2007) · The Journal of Pathology · doi:10.1002/path.2094 · Cited by 287
Self-citationAntunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560549 · Cited by 286
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
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 270
Self-citationHypoxia, 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 267
Tumor Acidity, Chemoresistance and Proton Pump Inhibitors
Milito, A. D., & Fais, S. (2005) · Future Oncology · doi:10.2217/14796694.1.6.779 · Cited by 264
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
Ultrastructural Pathology of the Cell and Matrix
de Harven, É. (1988) · Elsevier eBooks · doi:10.1016/c2013-0-06246-9 · Cited by 256
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
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
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
Self-citationLysosomal 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 230
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 228
The 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 220
Self-citationCuervo, A. M., & Dice, J. F. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00075-9 · Cited by 215
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
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
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
‘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
Liu, X., Jin, W., & Theil, E. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0636928100 · Cited by 203
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
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
The role of α-synuclein in neurodegenerative diseases
Bennett, M. C. (2004) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.10.010 · Cited by 198
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
Brunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 184
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 181
Koorts, A. M., & Viljoen, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701318583 · Cited by 164
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
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
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
Self-citationBrunk, U. T., & Ericsson, J. L. E. (1972) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(72)90080-9 · Cited by 147
Self-citationPower, sex, suicide: mitochondria and the meaning of life
(2006) · Choice Reviews Online · doi:10.5860/choice.43-4653 · Cited by 146
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
Self-citationKaushik, S., & Cuervo, A. M. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.007 · Cited by 145
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
Elleder, M., Sokolová, J., & Hřebı́ček, M. (1997) · Acta Neuropathologica · doi:10.1007/s004010050629 · Cited by 139
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
Aceruloplasminemia, an iron metabolic disorder
Miyajima, H. (2003) · Neuropathology · doi:10.1046/j.1440-1789.2003.00521.x · Cited by 135
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
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
Autophagy, Mitochondria and Cell Death in Lysosomal Storage Diseases
Kiselyov, K. I., Jennings, J. J., Jr., Rbaibi, Y., & Chu, C. T. (2007) · Autophagy · doi:10.4161/auto.3906 · Cited by 128
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
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
Self-citationZhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 123
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
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
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
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 108
NILSSON, S. E. G., Sundelin, S. P., Wihlmark, U., & Brunk, U. T. (2003) · Documenta Ophthalmologica · doi:10.1023/a:1022419606629 · Cited by 107
Self-citationInsights 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
Terman, A., Dalen, H., & Brunk, U. T. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(99)00070-4 · Cited by 106
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
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
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
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 92
Bergamini, E. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.001 · Cited by 90
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
Sakaida, I., Kyle, M. E., & Farber, J. L. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10830-4 · Cited by 86
Brunk, U. T., & Dricsson, J. L. E. (1972) · The Histochemical Journal · doi:10.1007/bf01011128 · Cited by 85
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 85
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
Self-citationThe 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
Self-citationYeung, B. H. Y., Huang, D.-C., & Sinicrope, F. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508533200 · Cited by 80
Barbouti, 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
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
Self-citationVaisman, B. L., Fibach, E., & Konijn, A. M. (1997) · Blood · doi:10.1182/blood.v90.2.831 · Cited by 72
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
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
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
Self-citationPersson, H. L., Nilsson, K., & Brunk, U. T. (2001) · Redox Report · doi:10.1179/135100001101536049 · Cited by 56
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
Self-citationMiyawaki, H. (1965) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/34.5.601 · Cited by 51
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
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 50
Self-citationLee, S., & Kim, M. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.01.022 · Cited by 47
Pandolfo, M. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_22 · Cited by 44
Lorenzo, K., Ton, P., Clark, J. L., Coulibaly, S., & Mach, L. (2000) · PubMed · Cited by 43
Yu, Z., Li, W., & Brunk, U. T. (2003) · Apmis · doi:10.1034/j.1600-0463.2003.1110607.x · Cited by 41
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
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
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
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
Victor, B. C., & Sloane, B. F. (2007) · Biological Chemistry · doi:10.1515/bc.2007.150 · Cited by 20
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
A protease involved in breast cancer metastasis.
Rochefort, H. (1990) · Medical Entomology and Zoology · Cited by 19
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
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952
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 808
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
Lysosomal cell death at a glance
Aits, S., & Jäättelä, M. (2013) · Journal of Cell Science · doi:10.1242/jcs.091181 · Cited by 667
Metadata
- 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
- 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