The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
Abstract
The cell sap from pig liver contains a protein which protects phosphatidylcholine liposomes and biomembranes from peroxidative degradation in the presence of glutathione. The activity of this protein has been assayed by measuring the inhibition of aged phosphatidylcholine liposome peroxidation induced by the Fe3+-triethylenetetramine complex. The peroxidation-inhibiting protein from pig liver has been purified 585-fold to homogeneity with overall recovery of activity of 12%. (NH4)2SO4 precipitation, ion-exchange chromatography on DEAE-Sepharose CL-6B and CM23-cellulose, affinity chromatography on glutathione-bromosulfophthalein-Sepharose and gel filtration on Sephadex G-50 were used. Gel filtration and SDS- polyacrylamide gel electrophoresis indicated a molecular weight of approximately 20 000. The protein inhibited peroxidation by Fe3+-triethylenetetramine following a 15 min preincubation of phosphatidylcholine liposomes in the presence of 5mM glutathione or 2-mercapthoethanol. The pure protein exhibited glutathione peroxidase activity on hydroperoxide groups of phosphatidylcholine and on cumene and t-butyl hydroperoxides, with specific activities of 2.2, 3.8 and 0.9 mumol/min per mg protein, respectively. The protein appears to be distinct from the selenoenzyme glutathione peroxidase and from any known glutathione S-transferase. The peroxidation was studied also with fresh phosphatidylcholine liposomes and was induced in this case by Fe-ascorbate. To obtain protection by the peroxidation-inhibiting protein and glutathione, preincubation was not necessary, but alpha-tocopherol, incorporated in the liposomes in the molar ratio 1:250 to phosphatidylcholine, was required. Lipid peroxidation of rat liver mitoplasts and microsomes was blocked when these preparations were incubated in the peroxidizing mixture in the presence of peroxidation-inhibiting protein and glutathione. The protection from Fe3+-triethylenetetramine-induced peroxidation is related apparently to reduction of hydroperoxide groups in polyunsaturated fatty acid residues of phospholipids and to inhibition of free radicals formation by chain branching. Protection from the Fe-ascorbate-induced peroxidation is apparently attributable to the same mechanism. However, the requirement of alpha-tocopherol for protection in the Fe-ascorbate-induced peroxidation suggests that the cooperation of a free-radical scavenger is necessary. It is probable that the glutathione peroxidase activity is involved also in the glutathione-dependent protection exhibited by the protein on lipid peroxidation of biomembranes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The term ferroptosis was introduced to describe cell death induced by the compound erastin, which causes glutathione depletion through the glutamate-cystine antiporter system Xc- inhibition and consequently glutathione peroxidase 4 (GPX4) inactivation leading to accumulation of lipid peroxides (Ursini et al., 1982; Dixon et al., 2012).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Ursini et al., 1982
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
Habig, W. H., Pabst, M. J., & Jakoby, W. B. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42083-8 · Cited by 18,509
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688
[30] Microsomal lipid peroxidation
Buege, J. A., & Aust, S. D. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)52032-6 · Cited by 13,564
Assay of proteins in the presence of interfering materials
Bensadoun, A., & Weinstein, D. (1976) · Analytical Biochemistry · doi:10.1016/s0003-2697(76)80064-4 · Cited by 3,191
Quantitative analysis of phospholipids by thin-layer chromatography
Skipski, V. P., Peterson, R., & Barclay, M. (1964) · Biochemical Journal · doi:10.1042/bj0900374 · Cited by 1,402
Kellogg, E. W., & Fridovich, I. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40745-x · Cited by 966
ADP-activated lipid peroxidation coupled to the TPNH oxidase system of microsomes
Hochstein, P. E., & Ernster, L. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90111-6 · Cited by 536
Species, Tissue and Subcellular Distribution of Non Se-Dependent Glutathione Peroxidase Activity
Lawrence, R. A., & Burk, R. F. (1978) · Journal of Nutrition · doi:10.1093/jn/108.2.211 · Cited by 399
Lipid Peroxidation in Mitochondrial Membrane
VLADIMIROV, Y. A., Vi, O., Suslova, T. B., & Cheremisina, Z. P. (1980) · Advances in lipid research · doi:10.1016/b978-0-12-024917-6.50011-2 · Cited by 351
Research works printed but not linked: 5
- Flohe, 1979, Vol. 65, 95
- Wang, 1955, J. Org. Chem., 77, 4715
- Nicholls, 1963, Vol. 8, 147
- Pryor, 1973, 32, 1862
- McCay, 1981, 40, 199
Cited by
Sorted by citations
Items 301–400 of 885
Erkekoğlu, P., Giray, B., Rachidi, W., Hininger‐Favier, I., Roussel, A., Favier, A. E., & Hıncal, F. (2011) · Environmental Toxicology · doi:10.1002/tox.20776 · Cited by 63
Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics
Bhowmick, D., & Mugesh, G. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c5ob01665g · Cited by 63
Pacitti, D., Wang, T., Page, M. M., Martín, S., Sweetman, J. W., Feldmann, J., & Secombes, C. J. (2013) · Aquatic Toxicology · doi:10.1016/j.aquatox.2012.12.020 · Cited by 62
Tannins of Conifer Bark as Nordic Piquancy—Sustainable Preservative and Aroma?
Raitanen, J., Järvenpää, E., Korpinen, R. I., Mäkinen, S., Hellström, J., Kilpeläinen, P. O., Liimatainen, J., Ora, A., Tupasela, T., & Jyske, T. M. (2020) · Molecules · doi:10.3390/molecules25030567 · Cited by 63
Identification and characterization of antioxidant enzyme mRNAs in the rat epididymis
Zini, A. S., & Schlegel, P. N. (1997) · International Journal of Andrology · doi:10.1046/j.1365-2605.1997.00039.x · Cited by 63
Funk, C. D., & Powell, W. S. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39632-1 · Cited by 63
Bast, A., & Haenen, G. R. M. M. (1984) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(84)90273-1 · Cited by 63
PDTAC: Targeted Photodegradation of GPX4 Triggers Ferroptosis and Potent Antitumor Immunity
Liu, S., Zhao, X., Shui, S., Wang, B., Cui, Y., Dong, S., Yuwen, T., & Liu, G. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00855 · Cited by 63
Glutathionyl systems and metabolic dysfunction in obesity
Picklo, M. J., Long, E. K., & Vomhof‐DeKrey, E. E. (2015) · Nutrition Reviews · doi:10.1093/nutrit/nuv042 · Cited by 64
A Selenium‐Containing Phospholipid‐Hydroperoxide Glutathione Peroxidase in Schistosoma mansoni
Maiorino, M., Roche‐Lestienne, C., Kieß, M., Koenig, K., Gawlik, D., Matthes, M., Naldini, E., Pierce, R. J., & Flohé, L. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0838w.x · Cited by 62
Karlupia, N., Manley, N. C., Prasad, K., Schäfer, R., & Steinberg, G. K. (2014) · Stem Cell Research & Therapy · doi:10.1186/scrt434 · Cited by 61
Initiation of Apoptotic Signal by the Peroxidation of Cardiolipin of Mitochondria
Nakagawa, Y. (2004) · Springer eBooks · doi:10.1007/978-3-662-41088-2_18 · Cited by 61
Knopp, E. A., Arndt, T. L., Eng, K., Caldwell, M., LeBoeuf, R. C., Deeb, S. S., & O’Brien, K. D. (1999) · Mammalian Genome · doi:10.1007/s003359901053 · Cited by 61
Initiation of Apoptotic Signal by the Peroxidation of Cardiolipin of Mitochondria
NAKAGAWA, Y. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1293.018 · Cited by 60
Schwarz, M., Löser, A., Cheng, Q., Wichmann-Costaganna, M., Schädel, P., Werz, O., Arnér, E. S. J., & Kipp, A. P. (2023) · Redox Biology · doi:10.1016/j.redox.2022.102593 · Cited by 60
Kinsey, G. R., Blum, J. L., Covington, M. D., Cummings, B. S., McHowat, J., & Schnellmann, R. G. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800030-jlr200 · Cited by 60
Yang, Y., Sharma, R., Cheng, J., Saini, M. K., Ansari, N. H., Andley, U. P., Awasthi, S., & Awasthi, S. (2002) · PubMed · Cited by 60
Kelner, M. J., & Montoya, M. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9086 · Cited by 60
Molybdenum Cofactor Deficiency in Humans
Johannes, L., Fu, C.-Y., & Schwarz, G. (2022) · Molecules · doi:10.3390/molecules27206896 · Cited by 59
Brault, C., Levy, P. L., Duponchel, S., Michelet, M., Sallé, A., Pécheur, E., Plissonnier, M., Parent, R., Véricel, E., Ivanov, A. V., et al. (2014) · Gut · doi:10.1136/gutjnl-2014-307904 · Cited by 59
Marinho, H. S., Antunes, F., & Pinto, R. E. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00468-6 · Cited by 59
Haenen, G. R. M. M., Tsoi, J. N. L. T. T., Vermeulen, N. P. E., Timmerman, H., & Bast, A. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90511-x · Cited by 59
Farmer, L. A., Wu, Z., Poon, J., Zilka, O., Lorenz, S., Huehn, S., Proneth, B., Conrad, M., & Pratt, D. A. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c05252 · Cited by 62
Lipid Quality Control and Ferroptosis: From Concept to Mechanism
Li, Z., Lange, M., Dixon, S. J., & Olzmann, J. A. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052521-033527 · Cited by 68
The role of oxygen metabolism for the pathological phenotype of Fanconi anemia
Ruppitsch, W., Meißlitzer, C., Weirich‐Schwaiger, H., Klocker, H., Scheidereit, C., Schweiger, M., & Hirsch‐Kauffmann, M. (1997) · Human Genetics · doi:10.1007/s004390050437 · Cited by 58
Terao, J., Asano, I., & Matsushita, S. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90205-4 · Cited by 58
Biological and Catalytic Properties of Selenoproteins
Chaudière, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210109 · Cited by 64
Ferroptosis: A New Promising Target for Lung Cancer Therapy
Xiong, R., He, R., Liu, B., Jiang, W., Wang, B., Li, N., & Geng, Q. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8457521 · Cited by 57
BEHNE, D., & Kyriakopoulos, A. M. (1993) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/57.2.310s · Cited by 56
Ferroptosis and Cancer: Complex Relationship and Potential Application of Exosomes
Wu, S., Li, T., Liu, W., & Huang, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.733751 · Cited by 55
Heat Shock Proteins and Ferroptosis
Liu, Y., Zhou, L., Xu, Y., Li, K., Zhao, Y., Qiao, H., Xu, Q., & Zhao, J. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.864635 · Cited by 60
Phospholipid oxidation products in ferroptotic myocardial cell death
Stamenković, A., Pierce, G. N., & Ravandi, A. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00076.2019 · Cited by 57
Involvement of glutathione peroxidases in the occurrence and development of breast cancers
Zhang, M., Wu, H.-T., Chen, W.-J., Xu, Y., Ye, Q., Shen, J., & Liu, J. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02420-x · Cited by 55
Qu, X.-X., He, J.-H., Cui, Z., Yang, T., & Sun, X. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00516 · Cited by 54
Ferroptosis in cardiac hypertrophy and heart failure
Zhang, K., Tian, X.-M., Li, W., & Hao, L. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115765 · Cited by 55
Ćosić, A., Jukić, I., Stupin, A., Mihalj, M., Mihaljević, Z., Novak, S., Vuković, R., & Drenjančević, I. (2016) · The Journal of Physiology · doi:10.1113/jp272297 · Cited by 53
Liu, Y., Duan, C., Dai, R., & Zeng, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.739392 · Cited by 58
Julicher, R. H. M., Sterrenberg, L., Bast, A., Riksen, R. O. W. M., Koomen, J. M., & Noordhoek, J. (1986) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.1986.tb04566.x · Cited by 54
Lipid and protein corona of food-grade TiO2 nanoparticles in simulated gastrointestinal digestion
Coreas, R., Cao, X., DeLoid, G. M., Demokritou, P., & Zhong, W. (2020) · NanoImpact · doi:10.1016/j.impact.2020.100272 · Cited by 53
Zhang, Y., Zhang, J., Feng, D., Zhou, H., Gui, Z., Zheng, M., Hang, Z., Wang, Z., Wang, Z., Gu, M. J., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.11.002 · Cited by 53
Dynamic Regulation of Ferroptosis by Lipid Metabolism
Naowarojna, N., Wu, T. W., Pan, Z., Li, M., Han, J. R., & Zou, Y. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0278 · Cited by 56
Ferroptosis mechanism and Alzheimer's disease
Feng, L., Sun, J. J., Xia, L., Shi, Q., Hou, Y., Zhang, L., Li, M., Fan, C., & Sun, B. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.389362 · Cited by 56
Wang, H., Fleishman, J. S., Cheng, S., Wang, W., Wu, F., Wang, Y., & Wang, Y. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02088-7 · Cited by 56
RetractedWei, C. (2024) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2024.111065 · Cited by 58
Protection against free radical injury by selenoenzymes
Burk, R. F. (1990) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(90)90073-b · Cited by 53
Ferroptosis-mediated immune responses in cancer
Qi, D., & Peng, M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1188365 · Cited by 53
Rencuzogullari, N., & Erdoğan, S. (2007) · Biological Trace Element Research · doi:10.1007/s12011-007-0027-7 · Cited by 52
Chronic Cyclophosphamide Exposure Alters the Profile of Rat Sperm Nuclear Matrix Proteins1
Codrington, A. M., Hales, B. F., & Robaire, B. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.060244 · Cited by 52
Use of Exogenous Glutathione for Metabolism of Peroxidized Methyl Linoleate in Rat Small Intestine
Kowalski, D. P., Feeley, R. M., & Jones, D. P. (1990) · Journal of Nutrition · doi:10.1093/jn/120.9.1115 · Cited by 52
Spallholz, J. E. (1990) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0553-8_12 · Cited by 52
Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
Gu, C., Fan, X., & Yu, W. (2023) · Cells · doi:10.3390/cells12151947 · Cited by 58
Tiwari, R., Mondal, Y., Bharadwaj, K., Mahajan, M., Mondal, S., & Sarkar, A. (2025) · Drug Development Research · doi:10.1002/ddr.70107 · Cited by 55
Lü, D., Xia, Q., Yang, Z., Gao, S., Sun, S., Luo, X., Li, Z., Zhang, X., Han, S., Li, X., et al. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-471 · Cited by 49
Unveiling the Molecular Mechanisms Behind Selenium-Related Diseases Through Knockout Mouse Studies
Conrad, M., & Schweizer, U. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2912 · Cited by 51
Okamura, N., Iwaki, Y., Hiramoto, S., Tamba, M., Bannai, S., Sugita, Y., Syntin, P., Dacheux, F., & Dacheux, J. (1997) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(97)00016-0 · Cited by 51
Tirmenstein, M. A., & Reed, D. J. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90097-5 · Cited by 51
HOIP modulates the stability of GPx4 by linear ubiquitination
Dong, K., Wei, R., Jin, T., Zhang, M., Shen, J., Xiang, H., Shan, B., Yuan, J., & Li, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214227119 · Cited by 52
Im, S., Choi, H. N., Jeon, Y.-H., Song, M., Kim, W. K., & Woo, J. (2016) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph13070625 · Cited by 49
Carvedilol inhibition of lipid peroxidation. A new antioxidative mechanism
Tadolini, B., & Franconi, F. (1998) · Free Radical Research · doi:10.1080/10715769800300421 · Cited by 50
Nakagawa, Y. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.956 · Cited by 49
Molecular impact of glutathione peroxidases in antioxidant processes
Mlakar, S. J., Osredkar, J., & Marc, J. (2008) · Biochemia Medica · doi:10.11613/bm.2008.016 · Cited by 49
Banaś, A., Johansson, I., & Stymne, S. (1992) · Plant Science · doi:10.1016/0168-9452(92)90127-8 · Cited by 49
Glutathione-dependent protection against oxidative damage of the human red cell membrane
Fujii, S., Dale, G., & Beutler, E. (1984) · Blood · doi:10.1182/blood.v63.5.1096.1096 · Cited by 49
GPX4: old lessons, new features
da Silva, T. N. X., Angeli, J. P. F., & Ingold, I. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220682 · Cited by 52
Selenoproteins of the glutathione system
Flohé, L., & Brigelius‐Flohé, R. (2007) · Springer eBooks · doi:10.1007/0-387-33827-6_15 · Cited by 48
Antioxidants in the retinal pigment epithelium
Newsome, D., Miceli, M., Liles, M., Tate, D., & Oliver, P. D. (1994) · Progress in Retinal and Eye Research · doi:10.1016/1350-9462(94)90006-x · Cited by 58
Purification and characterization of a novel monomeric glutathione peroxidase from rat liver.
Duan, Y., KOMURA, S., Fiszer‐Szafarz, B., Szafarz, D., & Yagi, K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37381-2 · Cited by 48
Mitochondrial Reactive Oxygen Species and Lytic Programmed Cell Death in Acute Inflammation
Rius‐Pérez, S., Pérez, S., Tolédano, M. B., & Sastre, J. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0209 · Cited by 48
Role of ferroptosis and ferroptosis-related long non'coding RNA in breast cancer
Xiang, S., Yan, W., Ren, X., Feng, J., & Zu, X. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00560-2 · Cited by 51
Consequences of mutations and inborn errors of selenoprotein biosynthesis and functions
Fradejas‐Villar, N. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.04.572 · Cited by 47
Slater, T. F., Cheeseman, K. H., Benedetto, C., Collins, M., Emery, S., Maddix, S. P., Nodes, J. T., Proudfoot, K. A., Burton, G. W., & Ingold, K. U. (1990) · Biochemical Journal · doi:10.1042/bj2650051 · Cited by 47
Yamada, K., Terao, J., & Matsushita, S. (1987) · Lipids · doi:10.1007/bf02534865 · Cited by 47
Glutathione depletion increases chemiluminescence emission and lipid peroxidation in the heart
Barsacchi, R., Pelosi, G., Camici, P. G., Bonaldo, L., Maiorino, M., & Ursini, F. (1984) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(84)90139-3 · Cited by 47
Gpx 4 is involved in the proliferation, migration and apoptosis of glioma cells
Zhao, H., Ji, B., Chen, J., Huang, Q., & Lu, X. (2017) · Pathology - Research and Practice · doi:10.1016/j.prp.2017.04.025 · Cited by 46
Ross, B. M., Moszczyńska, A., Erlich, J. C., & Kish, S. J. (1998) · Neuroscience · doi:10.1016/s0306-4522(97)00454-5 · Cited by 46
Geiger, P. G., Thomas, J. P., & Girotti, A. W. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90250-m · Cited by 46
Geiger, P. G., Lin, F., & Girotti, A. W. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90022-m · Cited by 46
Iron in Alzheimer’s Disease: From Physiology to Disease Disabilities
Pal, A., Cerchiaro, G., Rani, I., Ventriglia, M., Rongioletti, M. C. A., Longobardi, A., & Squitti, R. (2022) · Biomolecules · doi:10.3390/biom12091248 · Cited by 49
Ferroptosis: mechanisms and advances in ocular diseases
Liu, K., Li, H., Wang, F., & Su, Y. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04644-5 · Cited by 47
Yang, K., Zeng, L., Zeng, J., Deng, Y., Wang, S., Xu, H., He, Q., Yuan, M., Luo, Y., Ge, A., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102063 · Cited by 46
Lethal dysregulation of energy metabolism during embryonic vitamin E deficiency
McDougall, M. Q., Choi, J., Kim, H., Bobe, G., Stevens, J. F., Cadenas, E., Tanguay, R. L., & Traber, M. G. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.020 · Cited by 45
Selenium-Dependent Glutathione Peroxidases During Tumor Development
Kipp, A. P. (2017) · Advances in cancer research · doi:10.1016/bs.acr.2017.07.004 · Cited by 47
Pantothenol Protects Rats Against Some Deleterious Effects of Gamma Radiation
Slyshenkov, V. S. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00378-x · Cited by 45
Tang, L., Gounaris, K., Griffiths, C. M., & Selkirk, M. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.31.18313 · Cited by 45
Ferroptosis and Its Emerging Role in Pre-Eclampsia
Chen, Z., Gan, J., Zhang, M., Du, Y., & Zhao, H. (2022) · Antioxidants · doi:10.3390/antiox11071282 · Cited by 46
Non-coding RNA: A key regulator in the Glutathione-GPX4 pathway of ferroptosis
Hussain, M. S., Gupta, G., Shahwan, M. J., Bansal, P., Kaur, H., Deorari, M., Pant, K., Ali, H., Singh, S. K., Allam, V. S. R. R., et al. (2024) · Non-coding RNA Research · doi:10.1016/j.ncrna.2024.05.007 · Cited by 44
Jin, E., Jo, Y., Wei, S., Rizzo, M., Ryu, D., & Gariani, K. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1447148 · Cited by 54
Friedrichs, B., Toborek, M. J., Hennig, B., Heinevetter, L., Müller, C., & Brigelius‐Flohé, R. (1999) · BioFactors · doi:10.1002/biof.5520090108 · Cited by 44
Singh, K., & Ahluwalia, P. (2003) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.49.145 · Cited by 44
Aerobic pyruvate metabolism sensitizes cells to ferroptosis primed by GSH depletion
Vučković, A., Venerando, R., Tibaldi, E. V., Bosello-Travain, V., Roveri, A., Bordin, L., Miotto, G., Cozza, G., Toppo, S., Maiorino, M., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.045 · Cited by 44
Shen, Y., Zhang, G., Wei, C., Zhao, P., Wang, Y., Li, M., & Sun, L. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01343 · Cited by 44
Intracellular metal ion-based chemistry for programmed cell death
You, Y., Guo, Z., Wolter, T., & Hu, Q. (2025) · Chemical Society Reviews · doi:10.1039/d4cs00930d · Cited by 46
Embryonic expression profile of phospholipid hydroperoxide glutathione peroxidase
Schneider, M., Weisenhorn, D. M. V., Seiler, A., Bornkamm, G. W., Brielmeier, M., & Conrad, M. (2006) · Gene Expression Patterns · doi:10.1016/j.modgep.2005.11.002 · Cited by 43
Imada, I., Fujita, T., Sugiyama, Y., OKAMOTO, K., & Kobayashi, Y. (1989) · Archives of Gerontology and Geriatrics · doi:10.1016/0167-4943(89)90014-9 · Cited by 43
Matrine disrupts Nrf2/GPX4 antioxidant system and promotes hepatocyte ferroptosis
Wang, X., Zhu, W., Xing, M., Zhu, H., Chen, E., & Zhou, J. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110713 · Cited by 42
Ferroptosis inducers: A new frontier in cancer therapy
Ma, W., Hu, N., Xu, W., Zhao, L., Tian, C., & Kamei, K. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107331 · Cited by 44
Li, Z., Zhang, Y. Z., Ji, M., Wu, C., Zhang, Y., & Ji, S.-L. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116777 · Cited by 42
Ensminger, D. C., Salvador‐Pascual, A., Arango, B. G., Allen, K. N., & Vázquez‐Medina, J. P. (2021) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2021.110929 · Cited by 45
Ufer, C. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg650 · Cited by 42
Ahluwalia, P., Tewari, K., & Choudhary, P. (1996) · Toxicology Letters · doi:10.1016/0378-4274(95)03612-1 · Cited by 41
Metadata
- Authors
- Ursini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C.
- Affiliations
- University of Padua (IT)
- Venue
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
- Publisher
- Elsevier BV
- Published
- 1982-02
- Volume
- 710
- Issue
- 2
- Pages
- 197-211
- ISSN
- 0005-2760 (ISSN-L)
- OpenAlex
- W1966920840
- Cited by
- 884
- References
- 25
- Citations by year
- 2026: 42 · 2025: 68 · 2024: 81 · 2023: 69 · 2022: 63 · 2021: 46 · 2020: 37 · 2019: 17 · 2018: 16 · 2017: 18 · 2016: 15 · 2015: 13 · 2014: 11 · 2013: 13 · 2012: 17
- FWCI
- 12.85
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- Regione del Veneto
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- glutathione peroxidase activity, phosphatidylcholine liposomes, lipid peroxidation, glutathione, porcine liver, protein purification, triethylenetetramine, alpha-tocopherol, liver microsomes, hydroperoxide reduction, antioxidant enzymes, glutathione S-transferase, cumene hydroperoxide
- MeSH terms
- Animals, Glutathione Peroxidase, Kinetics, Lipid Peroxides, Liposomes, Liver, Membranes, Peroxidases, Peroxides, Phosphatidylcholines, Proteins, Subcellular Fractions, Swine
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
