Lysosomes in iron metabolism, ageing and apoptosis

Kurz, Tino; Terman, Alexei; Gustafsson, Bertil; Brunk, Ulf T.

doi:10.1007/s00418-008-0394-y

Cited by 303Autophagy in Disease and TherapyCalcium signaling and nucleotide metabolismCellular transport and secretion

Lysosomes in iron metabolism, ageing and apoptosis

Open access

Kurz, Tino, Terman, Alexei, Gustafsson, Bertil, Brunk, Ulf T.·2008·Histochemistry and Cell Biology

DOI 10.1007/s00418-008-0394-yPMC PMC2668650

Open this paper in CoChat — free account Open PDF

Abstract

The lysosomal compartment is essential for a variety of cellular functions, including the normal turnover of most long-lived proteins and all organelles. The compartment consists of numerous acidic vesicles (pH approximately 4 to 5) that constantly fuse and divide. It receives a large number of hydrolases ( approximately 50) from the trans-Golgi network, and substrates from both the cells' outside (heterophagy) and inside (autophagy). Many macromolecules contain iron that gives rise to an iron-rich environment in lysosomes that recently have degraded such macromolecules. Iron-rich lysosomes are sensitive to oxidative stress, while 'resting' lysosomes, which have not recently participated in autophagic events, are not. The magnitude of oxidative stress determines the degree of lysosomal destabilization and, consequently, whether arrested growth, reparative autophagy, apoptosis, or necrosis will follow. Heterophagy is the first step in the process by which immunocompetent cells modify antigens and produce antibodies, while exocytosis of lysosomal enzymes may promote tumor invasion, angiogenesis, and metastasis. Apart from being an essential turnover process, autophagy is also a mechanism by which cells will be able to sustain temporary starvation and rid themselves of intracellular organisms that have invaded, although some pathogens have evolved mechanisms to prevent their destruction. Mutated lysosomal enzymes are the underlying cause of a number of lysosomal storage diseases involving the accumulation of materials that would be the substrate for the corresponding hydrolases, were they not defective. The normal, low-level diffusion of hydrogen peroxide into iron-rich lysosomes causes the slow formation of lipofuscin in long-lived postmitotic cells, where it occupies a substantial part of the lysosomal compartment at the end of the life span. This seems to result in the diversion of newly produced lysosomal enzymes away from autophagosomes, leading to the accumulation of malfunctioning mitochondria and proteins with consequent cellular dysfunction. If autophagy were a perfect turnover process, postmitotic ageing and several age-related neurodegenerative diseases would, perhaps, not take place.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1007/s00418-008-0394-y

Cites

145 of 145 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Lipofuscin is an age-related iron-rich pigment that is non-degradable and accumulates in lysosomes; lysosomes cannot remove intralysosomal iron bound to lipofuscin, leading to excessive iron accumulation.
“Lipofuscin, an age-related iron rich pigment is non-degradable and not hydrolyzed by lysosomal enzymes.As a result, lipofuscin accumulates in the lysosomes.Lysosomes do not have the capacity to remove intralysosomal iron bound to lipofuscin, leading to excessive iron accumulation.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
Lysosomes are a source of rapidly mobilized, chelatable iron, with accumulation of iron being higher with ageing.
“It has been shown that lysosomes are a source of rapidly mobilized, chelatable iron, with accumulation of iron being higher with ageing.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
Low internal pH (4 to 5) and reducing equivalents such as cysteine, ascorbic acid and glutathione favor intralysosomal Fenton reaction.
“Low internal pH i.e. 4 to 5 , presence of reducing equivalents, such as cysteine, ascorbic acid and glutathione favour intralysosomal Fenton reaction (Kurz et al., 2008).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
Iron depletion has been found to damage lysosomes, although the mechanism may be a consequence of other apoptotic factors.
“Iron depletion has been found to damage lysosomes although it has been suggested that the mechanism may be a consequence of other apopotogenic factors (Kurz et al., 2008).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al., 2008
Under normal conditions, iron-catalyzed peroxidation occurs intralysosomally, resulting in oxidative modification of autophagocytosed material and yielding lipofuscin, which accumulates in ageing postmitotic cells at a rate inversely correlated with longevity across species.
“Even under normal conditions, some iron-catalyzed peroxidation occurs intralysosomally (lysosomes are rich in redox-active iron), resulting in oxidative modification of autophagocytosed material and yielding lipofuscin, a polymeric compound slowly accumulating within ageing postmitotic cells at a rate that is inversely correlated to the longevity across species (Kurz et al, 2008).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Kurz et al, 2008

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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 · see citing works
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 · 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
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 · cited 1× · see citing works
“An active role for lysosomes in the induction of cell death was an early suggestion (reviewed in de Duve and Wattiaux 1966).”
Background
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,532 · see citing works
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 2,185 · 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
Lipofuscin: mechanisms of age-related accumulation and influence on cell function12 1Guest Editor: Rajindar S. Sohal 2This article is part of a series of reviews on “Oxidative Stress and Aging.” The full list of papers may be found on the homepage of the journal.
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-citation
Subcellular Particles
Hayashi, 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-citation
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 · see citing works
Conditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53
Michalovitz, D., Halevy, O., & Oren, M. (1990) · Cell · doi:10.1016/0092-8674(90)90113-s · Cited by 769 · see citing works
Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila
Simonsen, A., Cumming, R. C., Brech, A., Isakson, P., Schubert, D. R., & Finley, K. D. (2008) · Autophagy · doi:10.4161/auto.5269 · Cited by 716 · see citing works
Lysosomes in cell death
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
Free radicals and aging
Barja, G. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.07.005 · Cited by 653 · 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
Ferritin, iron homeostasis, and oxidative damage1,2 1Guest Editor: Mario Comporti 2This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.
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
Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species
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-citation
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 · see citing works
Selective Disruption of Lysosomes in HeLa Cells Triggers Apoptosis Mediated by Cleavage of Bid by Multiple Papain-like Lysosomal Cathepsins
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
Lipofuscin
Terman, A., & Brunk, U. T. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.08.009 · Cited by 451 · see citing works
Self-citation
Cathepsin D Triggers Bax Activation, Resulting in Selective Apoptosis-inducing Factor (AIF) Relocation in T Lymphocytes Entering the Early Commitment Phase to Apoptosis
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
The lysosome turns fifty
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
Molecular bases of cellular iron toxicity12 1Guest Editor: Mario Comporti 2This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.
Eaton, J. W., & Qian, M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00772-4 · Cited by 389 · cited 1× · see citing works
“…and diffuses into lysosomes (Walton and Lewis 1916), which do not contain these enzymes (those that are autophagocytosed are rapidly degraded), to react with labile iron and form hydroxyl radicals, or similarly reactive ferryl or perferryl compounds (reviewed in Eaton and Qian 2002) (see Fig.”
Background
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-citation
Sphingosine-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-citation
Oxidant-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-citation
Studies 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-citation
Autophagy, 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-citation
In vivospectrofluorimetry reveals endogenous biomarkers that report healthspan and dietary restriction inCaenorhabditis elegans
Gerstbrein, B., Stamatas, G., Kollias, N., & Driscoll, M. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00153.x · Cited by 286 · see citing works
Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture
Antunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560549 · Cited by 286 · see citing works
Self-citation
Photo-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-citation
Autophagy 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-citation
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 · 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
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-citation
Role 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
Intralysosomal iron: a major determinant of oxidant-induced cell death
Yu, Z., Persson, H. L., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00109-6 · Cited by 226 · see citing works
Self-citation
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-citation
PKCζ Regulates TNF-α–Induced Activation of NADPH Oxidase in Endothelial Cells
Frey, R. S., Rahman, A., Kefer, J., Minshall, R. D., & Malik, A. B. (2002) · Circulation Research · doi:10.1161/01.res.0000017631.28815.8e · Cited by 225 · see citing works
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 217 · see citing works
Self-citation
When lysosomes get old☆
Cuervo, 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
Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral
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-citation
Mechanisms of Intralysosomal Degradation with Special Reference to Autophagocytosis and Heterophagocytosis of Cell Organelles
Glaumann, 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
Lysosomal involvement in apoptosis
Brunk, U. T., Neuzil, J., & Eaton, J. W. (2001) · Redox Report · doi:10.1179/135100001101536094 · Cited by 198
Self-citation
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
Prevention of oxidant-induced cell death by lysosomotropic iron chelators
Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00106-0 · Cited by 185 · see citing works
Self-citation
Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
Brunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 182 · see citing works
Self-citation
Breast 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
Intralysosomal iron chelation protects against oxidative stress‐induced cellular damage
Kurz, T., Gustafsson, B., & Brunk, U. T. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05321.x · Cited by 175 · see citing works
Self-citation
Lysosomal storage diseases as disorders of autophagy
Settembre, C., Fraldi, A., Rubinsztein, D. C., & Ballabio, A. (2008) · Autophagy · doi:10.4161/auto.5227 · Cited by 172 · see citing works
The AGE of the matrix: chemistry, consequence and cure
DeGroot, J. (2004) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2004.01.007 · Cited by 165 · see citing works
Ferritin and ferritin isoforms I: Structure–function relationships, synthesis, degradation and secretion
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
A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: possible role in supporting lysosomal proteolysis.
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-citation
Electron microscopical studies on rat brain neurons. Localization of acid phosphatase and mode of formation of lipofuscin bodies
Brunk, 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-citation
Power, 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-citation
Autophagy as a cell-repair mechanism: Activation of chaperone-mediated autophagy during oxidative stress
Kaushik, 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
Follow-up study of subunit c of mitochondrial ATP synthase (SCMAS) in Batten disease and in unrelated lysosomal disorders
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
Cycloheximide-induced T-cell Death Is Mediated by a Fas-associated Death Domain-dependent Mechanism
Tang, D., Lahti, J. M., Grenet, J. A., & Kidd, V. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7245 · Cited by 135 · 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
Tumor Necrosis Factor-related Apoptosis-inducing Ligand Activates a Lysosomal Pathway of Apoptosis That Is Regulated by Bcl-2 Proteins
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-citation
Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria
Zhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 119 · see citing works
Protein modification in aging
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-citation
Aging of cultured retinal pigment epithelial cells: oxidative reactions, lipofuscin formation and blue light damage
NILSSON, 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-citation
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
Ceroid/lipofuscin-loaded human fibroblasts show decreased survival time and diminished autophagocytosis during amino acid starvation☆
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-citation
Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage
KURZ, T., LEAKE, A., von ZGLINICKI, T., & BRUNK, U. T. (2004) · Biochemical Journal · doi:10.1042/bj20031029 · Cited by 101 · see citing works
Self-citation
Organelle Pathology in Primary and Secondary Haemochromatosis with Special Reference to Lysosomal Changes
Seymour, C. A., & Peters, T. J. (1978) · British Journal of Haematology · doi:10.1111/j.1365-2141.1978.tb03661.x · Cited by 100 · see citing works
Endosomal and lysosomal effects of desferrioxamine: protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest
Doulias, P., Christoforidis, S., Brunk, U. T., & Galaris, D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00396-4 · Cited by 96 · see citing works
Self-citation
Giant 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-citation
Brain 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
Ceroid/Lipofuscin-loaded human fibroblasts show increased susceptibility to oxidative stress
Terman, A., Abrahamsson, N., & Brunk, U. T. (1999) · Experimental Gerontology · doi:10.1016/s0531-5565(99)00045-5 · Cited by 93 · see citing works
Self-citation
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
Autophagy: A cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically
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
Cathepsin D–Bax death pathway in oxidative stressed neuroblastoma cells
Castino, R., Bellio, N., Nicotra, G., Follo, C., Trincheri, N. F., & Isidoro, C. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.12.030 · Cited by 86 · see citing works
Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress.
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
Cytochemical evidence for the leakage of acid phosphatase through ultrastructurally intact lysosomal membranes
Brunk, U. T., & Dricsson, J. L. E. (1972) · The Histochemical Journal · doi:10.1007/bf01011128 · Cited by 85 · see citing works
Self-citation
Caspase-8-mediated apoptosis induced by oxidative stress is independent of the intrinsic pathway and dependent on cathepsins
Baumgartner, 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-citation
PS-341 (Bortezomib) Induces Lysosomal Cathepsin B Release and a Caspase-2-dependent Mitochondrial Permeabilization and Apoptosis in Human Pancreatic Cancer Cells
Yeung, 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-citation
Hydrogen peroxide inhibits caspase-dependent apoptosis by inactivating procaspase-9 in an iron-dependent manner
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 · 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-citation
Utilization of Intracellular Ferritin Iron for Hemoglobin Synthesis in Developing Human Erythroid Precursors
Vaisman, 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-citation
The Involvement of Lysosomes in Myocardial Aging and Disease
Terman, A., Kurz, T., Gustafsson, B., & BRUNK, U. T. (2008) · Current Cardiology Reviews · doi:10.2174/157340308784245801 · Cited by 69 · see citing works
Self-citation
Ferritin 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
Visualization of iron in cultured macrophages: A cytochemical light and electron microscopic study using autometallography
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-citation
Power, sex, suicide Mitochondria and the meaning of life
Schon, E. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29253 · Cited by 59 · see citing works
Novel cellular defenses against iron and oxidation: ferritin and autophagocytosis preserve lysosomal stability in airway epithelium
Persson, H. L., Nilsson, K., & Brunk, U. T. (2001) · Redox Report · doi:10.1179/135100001101536049 · Cited by 56 · see citing works
Self-citation
Cytocidal 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-citation
Histochemistry and Electron Microscopy of Iron-Containing Granules, Lysosomes, and Lipofuscin in Mouse Mammary Glands 2
Miyawaki, 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-citation
Autophagy 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-citation
Aging and neurodegeneration
Lee, S., & Kim, M. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.01.022 · Cited by 46 · see citing works
Iron and Friedreich ataxia
Pandolfo, M. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_22 · Cited by 44 · see citing works
Invasive properties of murine squamous carcinoma cells: secretion of matrix-degrading cathepsins is attributable to a deficiency in the mannose 6-phosphate/insulin-like growth factor II receptor.
Lorenzo, K., Ton, P., Clark, J. L., Coulibaly, S., & Mach, L. (2000) · PubMed · Cited by 43 · see citing works
3‐Aminopropanal is a lysosomotropic aldehyde that causes oxidative stress and apoptosis by rupturing lysosomes
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-citation
Therapeutic 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-citation
Heavy 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-citation
THE 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
Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function
Victor, B. C., & Sloane, B. F. (2007) · Biological Chemistry · doi:10.1515/bc.2007.150 · Cited by 20 · see citing works
Rat liver lysosome membranes are enriched in α-tocopherol
Rupar, C. A., Albo, S., & Whitehall, J. D. (1992) · Biochemistry and Cell Biology · doi:10.1139/o92-075 · Cited by 19 · see citing works
Morphometry of age pigment (lipofuscin) and of ceroid pigment deposits associated with vitamin E deficiency
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
Intracellular free iron and acidic pathways mediate TNF-induced death of rat hepatoma cells
Autelli, R., Crepaldi, S., Stefanis, D. D., Parola, M., Bonelli, G., & Baccino, F. M. (2005) · APOPTOSIS · doi:10.1007/s10495-005-2944-2 · Cited by 12 · see citing works
Everybody's friend, or, Josh Billing's encyclopedia and proverbial philosophy of wit and humor
Billings, J. (1971) · Cited by 8 · see citing works
Peroxide hormesis? A commentary on “Hydrogen peroxide inhibits caspase-dependent apoptosis by inactivating procaspase-9 in an iron-dependent manner”
Brunk, U. T., & Jw, E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.008 · Cited by 3 · see citing works
Self-citation

Flagged first, then by citations

Sorted by citations

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.
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
Fluorescent Sensors for Measuring Metal Ions in Living Systems
Carter, K. P., Young, A. M., & Palmer, A. E. (2014) · Chemical Reviews · doi:10.1021/cr400546e · Cited by 2,443 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
Role of ROS and RNS Sources in Physiological and Pathological Conditions
Meo, S. D., Reed, T. T., Venditti, P., & Víctor, V. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1245049 · Cited by 1,638 · 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
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
Autophagy Failure in Alzheimer's Disease – Locating the Primary Defect
Nixon, R., & Yang, D.-S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.021 · Cited by 634 · see citing works
Mechanisms of Selective Autophagy
Zaffagnini, G., & Martens, S. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.004 · Cited by 591 · see citing works
The position of lysosomes within the cell determines their luminal pH
Johnson, D. E., Ostrowski, P., Jaumouillé, V., & Grinstein, S. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507112 · Cited by 590 · see citing works
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., & Xu, H. (2008) · Nature · doi:10.1038/nature07311 · Cited by 572 · see citing works
Self-citation
The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management
Yadati, T., Houben, T., Bitorina, A., & Shiri-Sverdlov, R. (2020) · Cells · doi:10.3390/cells9071679 · Cited by 466 · see citing works
Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol
Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536 · see citing works
Mechanisms of Ferroptosis and Relations With Regulated Cell Death: A Review
Lei, P., Bai, T., & Sun, Y. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00139 · Cited by 535 · see citing works
Identification of artesunate as a specific activator of ferroptosis in pancreatic cancer cells
Eling, N., Reuter, L., Hazin, J., Hamacher-Brady, A., & Brady, N. R. (2015) · Oncoscience · doi:10.18632/oncoscience.160 · Cited by 524 · see citing works
Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging
Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490 · see citing works
Self-citation
Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease
Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399 · see citing works
The proteasomal system
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
Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples
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
Antitumor Activity of Metal-Chelating Compound Dp44mT Is Mediated by Formation of a Redox-Active Copper Complex That Accumulates in Lysosomes
Lovejoy, D. B., Jansson, P. J., Brunk, U. T., Wong, J., Ponka, P., & Richardson, D. R. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1218 · Cited by 311 · see citing works
Self-citation
Mechanisms of Brain Iron Transport: Insight into Neurodegeneration and CNS Disorders
Mills, E., Dong, X.-P., Wang, F., & Xu, H. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.09.140 · Cited by 309 · see citing works
Targeting the lysosome in cancer
Piao, S., & Amaravadi, R. K. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12953 · Cited by 303 · see citing works
Lipofuscin: formation, effects and role of macroautophagy
Höhn, A., & Grune, T. (2013) · Redox Biology · doi:10.1016/j.redox.2013.01.006 · Cited by 298 · see citing works
Programmed Necrosis, Not Apoptosis, in the Heart
Kung, G., Konstantinidis, K., & Kitsis, R. N. (2011) · Circulation Research · doi:10.1161/circresaha.110.225730 · Cited by 290 · 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-citation
Lysosomal 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
Lysosomes as “Suicide Bags” in Cell Death: Myth or Reality?
Turk, B., & Türk, V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.023820 · Cited by 270 · 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
In vitro analysis of iron chelating activity of flavonoids
Mladěnka, P., Macáková, K., Filipský, T., Zatloukalová, L., Jahodář, L., Bovicelli, P., Silvestri, I. P., Hrdina, R., & Saso, L. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.02.003 · Cited by 257 · see citing works
Lysosomal membrane permeabilization in cell death: Concepts and challenges
Repnik, U., Česen, M. H., & Turk, B. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.06.006 · Cited by 235 · see citing works
Artesunate Activates Mitochondrial Apoptosis in Breast Cancer Cells via Iron-catalyzed Lysosomal Reactive Oxygen Species Production
Hamacher‐Brady, A., Stein, H., Turschner, S., Toegel, I., Mora-Rodríguez, R. A., Jennewein, N., Efferth, T., Eils, R., & Brady, N. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.210047 · Cited by 230 · see citing works
New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases
Zhang, N., Yu, X., Xie, J., & Xu, H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02277-7 · Cited by 218 · see citing works
Mechanisms of apoptosis
Savitskaya, M. A., & Онищенко, Г. Е. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915110012 · Cited by 214 · 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-citation
Critical Functions of the Lysosome in Cancer Biology
Davidson, S. M., & Heiden, M. G. V. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103101 · Cited by 209 · see citing works
Lysosomal Lipid Storage DiseasesPreprint
Schulze, H., & Sandhoff, K. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004804 · Cited by 198 · see citing works
Degradability of superparamagnetic nanoparticles in a model of intracellular environment: follow-up of magnetic, structural and chemical properties
Lévy, M., Lagarde, F., Maraloiu, V., Blanchin, M.-G., Gendron, F., Wilhelm, C., & Gazeau, F. (2010) · Nanotechnology · doi:10.1088/0957-4484/21/39/395103 · Cited by 191 · see citing works
Autophagy–physiology and pathophysiology
Uchiyama, Y., Shibata, M., Koike, M., Yoshimura, K., & Sasaki, M. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0406-y · Cited by 185 · see citing works
TRP channels of intracellular membranes
Dong, X., Wang, X., & Xu, H. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06626.x · Cited by 167 · 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
The Aging of Iron Man
Ashraf, A., Clark, M., & So, P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00065 · Cited by 158 · see citing works
Why should neuroscientists worry about iron? The emerging role of ferroptosis in the pathophysiology of neuroprogressive diseases
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 154 · see citing works
A novel method for autophagy detection in primary cells: Impaired levels of macroautophagy in immunosenescent T cells
Phadwal, K., Alegre-Abarrategui, J., Watson, A. S., Pike, L., Anbalagan, S., Hammond, E. M., Wade-Martins, R., McMichael, A., Klenerman, P., & Simon, A. K. (2012) · Autophagy · doi:10.4161/auto.18935 · Cited by 155 · see citing works
The renaissance of polypharmacology in the development of anti-cancer therapeutics: Inhibition of the “Triad of Death” in cancer by Di-2-pyridylketone thiosemicarbazones
Jansson, P. J., Kalinowski, D. S., Lane, D. J. R., Kovačević, Ž., Seebacher, N. A., Fouani, L., Sahni, S., Merlot, A. M., & Richardson, D. R. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.08.013 · Cited by 151 · see citing works
Programmed Necrosis
Galluzzi, L., Berghe, T. V., Vanlangenakker, N., Büttner, S., Eisenberg, T., Vandenabeele, P., Madeo, F., & Kroemer, G. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00001-8 · Cited by 150 · see citing works
Myoferlin targeting triggers mitophagy and primes ferroptosis in pancreatic cancer cells
Rademaker, G., Boumahd, Y., Peiffer, R., Anania, S., Wissocq, T., Liegeois, M. A., Luis, G., Sounni, N. E., Agirman, F., Maloujahmoum, N., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102324 · Cited by 143 · see citing works
miR-210 Targets Iron-Sulfur Cluster Scaffold Homologue in Human Trophoblast Cell Lines
Lee, D.-C., Romero, R., Kim, J.-S., Tarca, A. L., Montenegro, D., Pineles, B. L., Kim, E., Lee, J., Kim, S. Y., Draghici, S., et al. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.04.035 · Cited by 135 · see citing works
The endocytic pathway in microglia during health, aging and Alzheimer’s disease
Solé-Domènech, S., Cruz, D. L., Capetillo-Zarate, E., & Maxfield, F. R. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.07.002 · Cited by 133 · see citing works
Cell Death Pathways: a Novel Therapeutic Approach for Neuroscientists
Morris, G., Walker, A. J., Berk, M., Maes, M. H. J., & Puri, B. K. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0793-y · Cited by 129 · see citing works
Redox cycling metals: Pedaling their roles in metabolism and their use in the development of novel therapeutics
Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 129 · see citing works
Oxidized proteins: Mechanisms of removal and consequences of accumulation
Dunlop, R. A., Brunk, U. T., & Rodgers, K. J. (2009) · IUBMB Life · doi:10.1002/iub.189 · Cited by 124 · see citing works
Self-citation
ROS and intracellular ion channels
Kiselyov, K. I., & Muallem, S. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.03.004 · Cited by 123 · see citing works
Redox Activity Within the Lysosomal Compartment: Implications for Aging and Apoptosis
Kurz, T., Eaton, J. W., & Brunk, U. T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3005 · Cited by 117 · see citing works
Self-citation
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
Lipofuscin inhibits the proteasome by binding to surface motifs
Höhn, A., Jung, T., Grimm, S., Catalgol, B., Weber, D., & Grune, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.011 · Cited by 112 · see citing works
Mobilization of Stored Iron in Mammals: A Review
Linder, M. C. (2013) · Nutrients · doi:10.3390/nu5104022 · Cited by 111 · see citing works
Cathepsin B is a New Drug Target for Traumatic Brain Injury Therapeutics: Evidence for E64d as a Promising Lead Drug Candidate
Hook, G., Jacobsen, J. S., Grabstein, K. H., Kindy, M. S., & HOOK, V. Y. H. (2015) · Frontiers in Neurology · doi:10.3389/fneur.2015.00178 · Cited by 104 · see citing works
Ferritinophagy drives uropathogenicEscherichia colipersistence in bladder epithelial cells
Bauckman, K. A., & Mysorekar, I. U. (2016) · Autophagy · doi:10.1080/15548627.2016.1160176 · Cited by 100 · see citing works
Quercetin and iron metabolism: What we know and what we need to know
Xiao, L., Luo, G., Tang, Y., & Yao, P. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.02.022 · Cited by 101 · see citing works
Ferritin Protein Regulates the Degradation of Iron Oxide Nanoparticles
Volatron, J., Carn, F., Kolosnjaj‐Tabi, J., Javed, Y., Vuong, Q. L., Gossuin, Y., Ménager, C., Luciani, N., Charron, G., Hémadi, M., et al. (2016) · Small · doi:10.1002/smll.201602030 · Cited by 99 · see citing works
Diclofenac impairs autophagic flux via oxidative stress and lysosomal dysfunction: Implications for hepatotoxicity
Jung, S.-H., Lee, W., Park, S.-H., Lee, K.-Y., Choi, Y., Choi, S., Kang, D., Kim, S. R., Chang, T.-S., Hong, S., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101751 · Cited by 97 · 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
Intralysosomal Iron Induces Lysosomal Membrane Permeabilization and Cathepsin D–Mediated Cell Death in Trabecular Meshwork Cells Exposed to Oxidative Stress
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
Oxidative Stress-Induced Cellular Senescence: Is Labile Iron the Connecting Link?
Nousis, L., Kanavaros, P., & Barbouti, A. (2023) · Antioxidants · doi:10.3390/antiox12061250 · Cited by 96 · see citing works
Detection of cellular redox reactions and antioxidant activity assays
Meng, D., Zhang, P., Zhang, L., Wang, H., Ho, C., Li, S., Shahidi, F., & Zhao, H. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.08.008 · Cited by 95 · see citing works
Typical and Atypical Inducers of Lysosomal Cell Death: A Promising Anticancer Strategy
Domagała, A., Fidyt, K., Bobrowicz, M., Stachura, J., Szczygiel, K., & Firczuk, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082256 · Cited by 91 · see citing works
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 92 · see citing works
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 92 · see citing works
Telomerase deficiency delays renal recovery in mice after ischemia–reperfusion injury by impairing autophagy
Cheng, H., Fan, X., Lawson, W. E., Paueksakon, P., & Harris, R. C. (2015) · Kidney International · doi:10.1038/ki.2015.69 · Cited by 89 · see citing works
Targeting oxidative stress-mediated regulated cell death as a vulnerability in cancer
Chen, D., Guo, Z., Yao, L., Sun, Y., Dian, Y., Zhao, D., Ke, Y., Zeng, F., Zhang, C., Deng, G., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103686 · Cited by 88 · see citing works
Hepatic reticuloendothelial system cell iron deposition is associated with increased apoptosis in nonalcoholic fatty liver disease
Maliken, B. D., Nelson, J. E., Klintworth, H. M., Beauchamp, M. D., Yeh, M. M., & Kowdley, K. V. (2013) · Hepatology · doi:10.1002/hep.26238 · Cited by 86 · see citing works
Plant Cell Nucleolus as a Hot Spot for Iron
Roschzttardtz, H., Grillet, L., Isaure, M., Conéjéro, G., Ortega, R., Curie, C., & Mari, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.269720 · Cited by 85 · see citing works
Sphingosine mediates TNFα-induced lysosomal membrane permeabilization and ensuing programmed cell death in hepatoma cells
Ullio, C., Casas, J., Brunk, U. T., Sala, G. L., Fabriàs, G., Ghidoni, R., Bonelli, G., Baccino, F. M., & Autelli, R. (2012) · Journal of Lipid Research · doi:10.1194/jlr.m022384 · Cited by 84 · see citing works
Self-citation
Alzheimer’s disease: as it was in the beginning
Kozlov, S. O., Afonin, A. М., Evsyukov, I., & Бондаренко, А. Б. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0006 · Cited by 84 · see citing works
Free radicals: Relationship to Human Diseases and Potential Therapeutic applications
Zarić, B. L., Mačvanin, M., & Isenović, E. R. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106346 · Cited by 100 · see citing works
Iron overload is accompanied by mitochondrial and lysosomal dysfunction in WDR45 mutant cells
Seibler, P., Burbulla, L. F., Dulović, M., Zittel, S., Heine, J., Schmidt, T., Rudolph, F., Westenberger, A., Raković, A., Münchau, A. M., et al. (2018) · Brain · doi:10.1093/brain/awy230 · Cited by 80 · see citing works
Morphological Features of Organelles during Apoptosis: An Overview
Bottone, M. G., Santin, G., Aredia, F., Bernocchi, G., Pellicciari, C., & Scovassi, A. I. (2013) · Cells · doi:10.3390/cells2020294 · Cited by 79 · see citing works
Cytotoxicity of silver and copper nanoparticles on rainbow trout (Oncorhynchus mykiss) hepatocytes
Ostaszewska, T., Śliwiński, J., Kamaszewski, M., Sysa, P., & Chojnacki, M. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-017-0494-0 · Cited by 78 · see citing works
Tyrosine Modifications in Aging
Feeney, M. B., & Schöneich, C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4595 · Cited by 78 · see citing works
Lysosomal Destabilizing Drug Siramesine and the Dual Tyrosine Kinase Inhibitor Lapatinib Induce a Synergistic Ferroptosis through Reduced Heme Oxygenase-1 (HO-1) Levels
Villalpando-Rodriguez, G. E., Blankstein, A. R., Konzelman, C., & Gibson, S. B. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9561281 · Cited by 76 · see citing works
Autophagy in the brain of neonates following hypoxia-ischemia shows sex- and region-specific effects.
Weis, S. N., Toniazzo, A., Ander, B., Zhan, X.-H., Careaga, M., Ashwood, P., Wyse, A., Netto, C., & Sharp, F. R. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2013.10.046 · Cited by 78 · see citing works
Targeted radionuclide therapy with astatine-211: Oxidative dehalogenation of astatobenzoate conjugates
Tezé, D., Sergentu, D., Kalichuk, V., Barbet, J., Deniaud, D., Galland, N., Maurice, R., & Montavon, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-02614-2 · Cited by 76 · see citing works
The Anticancer Agent Di-2-pyridylketone 4,4-Dimethyl-3-thiosemicarbazone (Dp44mT) Overcomes Prosurvival Autophagy by Two Mechanisms
Gutierrez, E., Richardson, D. R., & Jansson, P. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599480 · Cited by 75 · see citing works
Effect of gadolinium-based nanoparticles on nuclear DNA damage and repair in glioblastoma tumor cells
Štefančíková, L., Lacombe, S., Leza, D. S., Porcel, E., Pagáčová, E., Tillement, O., Lux, F., Depeš, D., Kozubek, S., & Falk, M. (2016) · Journal of Nanobiotechnology · doi:10.1186/s12951-016-0215-8 · Cited by 74 · 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-citation
Enhanced Brain Delivery of Deferasirox–Lactoferrin Conjugates for Iron Chelation Therapy in Neurodegenerative Disorders: In Vitro and in Vivo Studies
Kamalinia, G., Khodagholi, F., Atyabi, F., Amini, M., Shaerzadeh, F., Sharifzadeh, M. S., & Dinarvand, R. (2013) · Molecular Pharmaceutics · doi:10.1021/mp4002014 · Cited by 73 · see citing works
Three-Dimensional Imaging of Biological Tissue by Cryo X-Ray Ptychography
Shahmoradian, S. H., Tsai, E. H. R., Díaz, A., Guizar‐Sicairos, M., Raabe, J., Spycher, L., Britschgi, M., Ruf, A., Stahlberg, H., & Holler, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-05587-4 · Cited by 72 · see citing works
Chelation of Lysosomal Iron Protects Dopaminergic SH-SY5Y Neuroblastoma Cells from Hydrogen Peroxide Toxicity by Precluding Autophagy and Akt Dephosphorylation
Castino, R., Fiorentino, I., Cagnin, M., Giovia, A., & Isidoro, C. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr179 · Cited by 68 · 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
Profound Morphological Changes in the Erythrocytes and Fibrin Networks of Patients with Hemochromatosis or with Hyperferritinemia, and Their Normalization by Iron Chelators and Other Agents
Pretorius, E., Bester, J., Vermeulen, N., Lipiński, B., Gericke, G. S., & Kell, D. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085271 · Cited by 67 · see citing works
Massive Intracellular Remodeling of CuS Nanomaterials Produces Nontoxic Bioengineered Structures with Preserved Photothermal Potential
Curcio, A., de Walle, A. V., Benassai, E., Serrano, A., Luciani, N., Menguy, N., Manshian, B. B., Sargsian, A., Soenen, S. J., Espinosa, A., et al. (2021) · ACS Nano · doi:10.1021/acsnano.1c00567 · Cited by 66 · see citing works
Iron reduction potentiates hydroxyl radical formation only in flavonols
Macáková, K., Mladěnka, P., Filipský, T., Říha, M., Jahodář, L., Trejtnar, F., Bovicelli, P., Silvestri, I. P., Hrdina, R., & Saso, L. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.06.107 · Cited by 64 · 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
Retention of Gadolinium in Brain Parenchyma: Pathways for Speciation, Access, and Distribution. A Critical Review
Rasschaert, M., Weller, R. O., Schroeder, J. A., Brochhausen, C., & Idée, J. (2020) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.27124 · Cited by 64 · see citing works
Regulation of ATP13A2 via PHD2-HIF1α Signaling Is Critical for Cellular Iron Homeostasis: Implications for Parkinson's Disease
Rajagopalan, S., Rane, A., Chinta, S. J., & Andersen, J. K. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3117-15.2016 · Cited by 63 · see citing works
Iron-mediated oxidative stress plays an essential role in ferritin-induced cell death
Bresgen, N., Jaksch, H., Lacher, H., Ohlenschläger, I., Uchida, K., & Eckl, P. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.019 · Cited by 62 · see citing works
Taxifolin ameliorates iron overload-induced hepatocellular injury: Modulating PI3K/AKT and p38 MAPK signaling, inflammatory response, and hepatocellular regeneration
Salama, S. A., & Kabel, A. M. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109230 · Cited by 62 · 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 63 · see citing works
Handling of Iron Oxide and Silver Nanoparticles by Astrocytes
Hohnholt, M. C., Geppert, M., Luther, E. M., Petters, C., Bulcke, F., & Dringen, R. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0930-y · Cited by 61 · see citing works
Autophagy, reactive oxygen species and the fate of mammalian cells
Szumiel, I. (2010) · Free Radical Research · doi:10.3109/10715762.2010.525233 · Cited by 61 · 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: Histochemistry and Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2008-02-08
Volume: 129
Issue: 4
Pages: 389-406
ISSN: 0948-6143 (ISSN-L)
1432-119X
DOI: 10.1007/s00418-008-0394-y
PMC: PMC2668650
OpenAlex: W2130287342
Cited by: 302
References: 143
Citations by year: 2026: 11 · 2025: 20 · 2024: 10 · 2023: 19 · 2022: 20 · 2021: 15 · 2020: 16 · 2019: 10 · 2018: 12 · 2017: 19 · 2016: 18 · 2015: 24 · 2014: 7 · 2013: 21 · 2012: 17
FWCI: 2.25
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc
creativecommons.org/licenses/by-nc/2.0 (tdm)
creativecommons.org/licenses/by-nc/2.0 (vor)
Locations: Histochemistry and Cell Biology (publishedVersion, cc-by-nc)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
KTH Publication Database DiVA (KTH Royal Institute of Technology) (submittedVersion, other-oa)
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 › Cell Biology › Cellular transport and secretion
Keywords: lysosomes, iron metabolism, aging, apoptosis, autophagy, heterophagy, oxidative stress, lysosomal destabilization, lysosomal enzymes, lysosomal storage disease, lipofuscin, hydrogen peroxide, mitochondrial dysfunction, age-related neurodegenerative diseases, necrosis
MeSH terms: Aging, Animals, Humans, Iron, Lipofuscin, Lysosomes, Mitochondria, Models, Biological, 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 in iron metabolism, ageing and apoptosis

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks