Intralysosomal iron chelation protects against oxidative stress‐induced cellular damage
Open accessAbstract
Oxidant‐induced cell damage may be initiated by peroxidative injury to lysosomal membranes, catalyzed by intralysosomal low mass iron that appears to comprise a major part of cellular redox‐active iron. Resulting relocation of lytic enzymes and low mass iron would result in secondary harm to various cellular constituents. In an effort to further clarify this still controversial issue, we tested the protective effects of two potent iron chelators – the hydrophilic desferrioxamine (dfo) and the lipophilic salicylaldehyde isonicotinoyl hydrazone (sih), using cultured lysosome‐rich macrophage‐like J774 cells as targets. dfo slowly enters cells via endocytosis, while the lipophilic sih rapidly distributes throughout the cell. Following dfo treatment, long‐term survival of cells cannot be investigated because dfo by itself, by remaining inside the lysosomal compartment, induces apoptosis that probably is due to iron starvation, while sih has no lasting toxic effects if the exposure time is limited. Following preincubation with 1 m m dfo for 3 h or 10 µ m sih for a few minutes, both agents provided strong protection against an ensuing ∼LD50 oxidant challenge by preventing lysosomal rupture, ensuing loss of mitochondrial membrane potential, and apoptotic/necrotic cell death. It appears that once significant lysosomal rupture has occurred, the cell is irreversibly committed to death. The results lend strength to the concept that lysosomal membranes, normally exposed to redox‐active iron in high concentrations, are initial targets of oxidant damage and support the idea that chelators selectively targeted to the lysosomal compartment may have therapeutic utility in diminishing oxidant‐mediated cell injury.
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
Cites
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?
The critical dependency of ferroptosis on iron can be ascribed to the ability of iron to promote non-enzymatic lipid oxidation via lysosomal Fenton reactions.
“Alternatively, the critical dependency of ferroptosis on iron can also be ascribed to the ability of this heavy metal to promote non-enzymatic lipid oxidation via lysosomal Fenton reactions [538, 572, 576, 577].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [576]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,672 · 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
Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,166 · 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-citationLysosomal Protease Pathways to Apoptosis
Stoka, V., Turk, B., Schendel, S. L., Kim, T., Cirman, T., Snipas, S. J., Ellerby, L., Bredesen, D. E., Freeze, H. H., Abrahamson, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008944200 · Cited by 673 · see citing works
Estimation of H 2 O 2 gradients across biomembranes
Antunes, F., & Cadenas, E. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01638-0 · Cited by 498 · see citing works
Cirman, T., Bender, K. O., Droga-Mazovec, G., Türk, V., Reed, J. C., Myers, R., Salvesen, G. S., & Turk, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308347200 · Cited by 479 · see citing works
Lysosomes in biology and pathology
(1975) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(75)90338-7 · Cited by 469 · see citing works
Davies, K. J. A. (1999) · IUBMB Life · doi:10.1080/713803463 · Cited by 438 · see citing works
Zur Histochemie der Schwermetalle Das Sulfid-Silberverfahren
Timm, F. (1958) · International Journal of Legal Medicine · doi:10.1007/bf00665092 · Cited by 407 · see citing works
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-citationSuperoxide as an intracellular radical sink
Winterbourn, C. C. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90512-s · Cited by 365 · see citing works
Dypbukt, J. M., Ankarcrona, M., Burkitt, M. J., Sjöholm, Å., Ström, K., Orrenius, S., & Nicotera, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43849-5 · Cited by 361 · see citing works
Ferritin as a source of iron for oxidative damage
Reif, D. W. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90091-t · Cited by 357 · see citing works
Atractyloside‐induced release of cathepsin B, a protease with caspase‐processing activity
Vancompernolle, K., Herreweghe, F. V., PYNAERT, G. N., de Craen, M. V., Vos, K. J. D., Totty, N., Sterling, A., Fiers, W., Vandenabeele, P., & Grooten, J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01275-7 · Cited by 304 · see citing works
Uptake of dyes and drugs by living cells in culture
ALLISON, A. C., & Young, M. R. (1964) · Life Sciences · doi:10.1016/0024-3205(64)90082-7 · Cited by 299 · 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-citationPhoto-Oxidative Disruption of Lysosomal Membranes Causes Apoptosis of Cultured Human Fibroblasts
Brunk, U. T., Dalen, H., Roberg, K. B., & Hellquist, H. B. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00007-5 · Cited by 283 · see citing works
Self-citationSphingosine-induced apoptosis is dependent on lysosomal proteases
Kågedal, K., Ming, Z. H. A. O., Svensson, I., et al. (2001) · Biochemical Journal · doi:10.1042/bj3590335 · Cited by 273 · see citing works
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-citationCytochrome c release and caspase activation in hydrogen peroxide‐ and tributyltin‐induced apoptosis
Stridh, H., Kimland, M., Jones, D. P., Orrenius, S., & Hampton, M. B. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00630-9 · Cited by 251 · see citing works
Glickstein, H., El, R. B., Shvartsman, M., & Cabantchik, Z. I. (2005) · Blood · doi:10.1182/blood-2005-02-0460 · Cited by 249 · see citing works
Induction of cell death by the lysosomotropic detergent MSDH
Li, W., Yuan, X., Nordgren, G., Dalen, H., Dubowchik, G. M., Firestone, R. A., & Brunk, U. T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01286-2 · Cited by 245 · see citing works
Self-citationAutophagic proteolysis: control and specificity
Blommaart, E. F. C., Luiken, J. J. F. P., & Meijer, A. J. (1997) · The Histochemical Journal · doi:10.1023/a:1026486801018 · Cited by 236 · 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-citationEstimation of V?O2max from the ratio between HRmax and HRrest ? the Heart Rate Ratio Method
Uth, N., S�rensen, H., Overgaard, K., & Pedersen, P. K. (2003) · European Journal of Applied Physiology · doi:10.1007/s00421-003-0988-y · Cited by 231 · 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-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 226 · see citing works
Self-citationPetrat, F., de GROOT, H., & Rauen, U. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560061 · Cited by 215 · 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-citationBrunk, U. T., & Svensson, I. (1999) · Redox Report · doi:10.1179/135100099101534675 · Cited by 182 · see citing works
Self-citationDYNAMICS OF ACRIDINE ORANGE-CELL INTERACTION
Robbins, E., & Marcus, P. I. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.18.2.237 · Cited by 181 · see citing works
Evidence that desferrioxamine cannot enter cells by passive diffusion
Lloyd, J. B., Cable, H. C., & Rice-Evans, C. A. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90109-i · Cited by 163 · see citing works
Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
Radisky, D. C., & Kaplan, J. (1998) · Biochemical Journal · doi:10.1042/bj3360201 · Cited by 163 · see citing works
Pisoni, R. L., Acker, T. L., Lisowski, K. M., Lemons, R. M., & Thoene, J. G. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.2.327 · Cited by 162 · see citing works
Lysosomal destabilization during macrophage damage induced by cholesterol oxidation products
Yuan, X., Li, W., Brunk, U. T., Dalen, H., Chang, Y. H., & Sevanian, A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00220-8 · Cited by 147 · see citing works
Self-citationMetallothionein 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-citationPetrat, F., de GROOT, H., & Rauen, U. (2001) · Biochemical Journal · doi:10.1042/bj3560061 · Cited by 141 · 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
Participation of a Cathepsin L-Type Protease in the Activation of Caspase-3.
Ishisaka, R., Utsumi, T., Kanno, T., Arita, K., Katsumura, N., Akiyama, J., & Utsumi, K. (1999) · Cell Structure and Function · doi:10.1247/csf.24.465 · Cited by 129 · 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-citationThe transport systems of mammalian lysosomes
Pisoni, R. L., & Thoene, J. G. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(91)90002-e · Cited by 112 · see citing works
H2O2-Mediated Damage to Lysosomal Membranes of J-774 Cells
ZDOLSEK, J. M., Zhang, H., Roberg, K. B., Brunk, U. T., & Sies, H. (1993) · Free Radical Research Communications · doi:10.3109/10715769309147344 · Cited by 112 · see citing works
Self-citationActivation of caspase‐3‐like protease by digitonin‐treated lysosomes
Ishisaka, R., Utsumi, T., Yabuki, M., Kanno, T., Furuno, T., Inoue, M., & Utsumi, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01080-1 · Cited by 110 · 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-citationCellular Uptake and Release of Two Contrasting Iron Chelators
Cable, H. C., & Lloyd, J. B. (1999) · Journal of Pharmacy and Pharmacology · doi:10.1211/0022357991772231 · Cited by 102 · see citing works
Delayed oxidant‐induced cell death involves activation of phospholipase A2
Zhao, M., Brunk, U. T., & Eaton, J. W. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03184-2 · Cited by 102 · see citing works
Self-citationKURZ, T., LEAKE, A., von ZGLINICKI, T., & BRUNK, U. T. (2004) · Biochemical Journal · doi:10.1042/bj20031029 · Cited by 101 · see citing works
Self-citationFluorescence Microscopy of Lysosomes and Related Structures in Living Cells
Zelenin, A. V. (1966) · Nature · doi:10.1038/212425a0 · Cited by 100 · see citing works
Detection of H2O2 release from vascular endothelial cells
Panus, P. C., Radí, R., Chumley, P. H., Lillard, R. H., & Freeman, B. A. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90013-k · Cited by 98 · see citing works
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-citationRadiation-induced cell death: importance of lysosomal destabilization
Persson, H. L., Kurz, T., Eaton, J. W., & Brunk, U. T. (2005) · Biochemical Journal · doi:10.1042/bj20050271 · Cited by 94 · see citing works
Self-citationŠimůnek, T., Boer, C., Bouwman, R. A., VLASBLOM, R., Versteilen, A. M. G., Štěrba, M., Geršl, V., Hrdina, R., Poňka, P., & DELANGE, J. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.05.008 · Cited by 91 · see citing works
Vitolo, L. M. W., Hefter, G. T., Clare, B. W., & Webb, J. M. (1990) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)80472-7 · Cited by 86 · 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-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 · see citing works
Self-citationHorackova, M. (2000) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00088-2 · Cited by 77 · see citing works
Iron chelation by pyridoxal isonicotinoyl hydrazone and analogues in hepatocytes in culture
Baker, E., Vitolo, M. L., & Webb, J. (1985) · Biochemical Pharmacology · doi:10.1016/0006-2952(85)90142-x · Cited by 67 · see citing works
ZDOLSEK, J. M., Roberg, K. B., & Brunk, U. T. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90120-j · Cited by 65 · see citing works
Self-citationA thermodynamic appraisal of the radical sink hypothesis
Koppenol, W. H. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90513-t · Cited by 62 · see citing works
Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide
Starke-Reed, P. E., Gilbertson, J. D., & Farber, J. L. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90916-7 · Cited by 62 · see citing works
Acylhydrazones of o-Oxy- and o-Aminoaldehydes and Ketones as Tridentate Complexing Agents
Sacconi, L. (1953) · Journal of the American Chemical Society · doi:10.1021/ja01117a519 · Cited by 39 · 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-citationOxidant-induced apoptosis: a consequence of lethal lysosomal leak?
Hellquist, H. B., Svensson, I., & Brunk, U. T. (1997) · Redox Report · doi:10.1080/13510002.1997.11747092 · Cited by 36 · see citing works
Self-citationβ -Cells, Oxidative Stress, Lysosomal Stability, and Apoptotic/Necrotic Cell Death
Olejnicka, B. T., Andersson, A., Tyrberg, B., Dalen, H., & Brunk, U. T. (1999) · Antioxidants and Redox Signaling · doi:10.1089/ars.1999.1.3-305 · Cited by 23 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
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
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
Cao, J. Y., & Dixon, S. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2194-1 · Cited by 1,515 · see citing works
Koskenkorva-Frank, T. S., Weiss, G., Koppenol, W. H., & Burckhardt, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.001 · Cited by 406 · see citing works
The siderophore yersiniabactin binds copper to protect pathogens during infection
Chaturvedi, K. S., Hung, C. S., Crowley, J. R., Stapleton, A. E., & Henderson, J. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1020 · Cited by 301 · see citing works
Lysosomes in iron metabolism, ageing and apoptosis
Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0394-y · Cited by 302 · see citing works
Self-citationOxidative Stress and the Homeodynamics of Iron Metabolism
Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works
Organelle-specific initiation of cell death
Galluzzi, L., Bravo-San Pedro, J. M., & Kroemer, G. (2014) · Nature Cell Biology · doi:10.1038/ncb3005 · Cited by 239 · 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-citationIron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74 · see citing works
Bendova, P., Mackova, E., Haskova, P., Vavrova, A., Jirkovsky, E., Sterba, M., Popelova, O., Kalinowski, D. S., Kovarikova, P., Vavrova, K., et al. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100125t · Cited by 73 · see citing works
Limited Role for Iron Regulation in <i>Coxiella burnetii</i> Pathogenesis
Briggs, H. L., Pul, N., Seshadri, R., Wilson, M. J., Tersteeg, C., Russell-Lodrigue, K. E., Andoh, M., Bäumler, A. J., & Samuel, J. E. (2008) · Infection and Immunity · doi:10.1128/iai.01609-07 · Cited by 52 · see citing works
Charkoudian, L. K., Dentchev, T., Lukinova, N., Wolkow, N., Dunaief, J. L., & Franz, K. J. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.08.001 · Cited by 49 · see citing works
- Authors
- Kurz, T., Gustafsson, B., & Brunk, U. T.
- Affiliations
- Linköping University (SE)
- Linköping University Hospital (SE)
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2006-06-07
- Volume
- 273
- Issue
- 13
- Pages
- 3106-3117
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2003317994
- Cited by
- 175
- References
- 65
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 9 · 2023: 6 · 2022: 6 · 2021: 6 · 2020: 4 · 2019: 10 · 2018: 10 · 2017: 6 · 2016: 8 · 2015: 5 · 2014: 14 · 2013: 14 · 2012: 13
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of Cambridge
- University of New South Wales
- University of Sydney
- Topics
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- iron chelation, oxidative stress, deferoxamine, salicylaldehyde isonicotinoyl hydrazone, lysosomal rupture, mitochondrial membrane potential, apoptosis, necrosis, redox-active iron, cell death protection
- MeSH terms
- Aldehydes, Chelating Agents, Deferoxamine, Endocytosis, Hydrazones, Hydrogen Peroxide, Iron, Iron Chelating Agents, Lysosomes, Membrane Potentials, Models, Biological, Necrosis, Oxidants, Apoptosis, Oxidative Stress, Cell Proliferation
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
