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 501–600 of 885
Nutritional antioxidants: A battle for better health
Rathore, G. S., Suthar, M., Pareek, A., & Gupta, R. (2011) · Journal of Natural Pharmaceuticals · doi:10.4103/2229-5119.78490 · Cited by 22
Wang, Y., Hu, J., Fleishman, J. S., Li, Y., Zhao, R., Wang, J., Feng, Y., Chen, J., & Wang, H. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1290183 · Cited by 21
Cheng, Q., Roveri, A., Cozza, G., Bordin, L., Rohn, I., Schwerdtle, T., Kipp, A. P., Ursini, F., Maiorino, M., Miotto, G., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102070 · Cited by 21
Ruan, D., Wen, J., Fang, F., Lei, Y., Zhao, Z., & Miao, Y. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01721-6 · Cited by 21
Lou, T., Wu, H., Feng, M., Liu, L., Yang, X., Pan, M., Wei, Z., Zhang, Y., Shi, L., Qu, B., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117868 · Cited by 24
Thompson, K. M., Haibach, H., Evenson, J. K., & Sunde, R. A. (1998) · Journal of Nutrition · doi:10.1093/jn/128.8.1289 · Cited by 21
BIOCHEMICAL FUNCTIONS OF SELENIUM
Combs, G. F., & Combs, S. B. (1986) · Elsevier eBooks · doi:10.1016/b978-0-12-183495-1.50011-7 · Cited by 21
Tang, N., Liu, X., Liu, Y., Wang, H., Zhao, Y., Wang, H., & Hu, Z. (2024) · Oncology Letters · doi:10.3892/ol.2024.14470 · Cited by 20
Selenium-containing Peptides and their Biological Applications
Ahmed, K., Ashraf, D., Chotana, G. A., Faisal, A., Khan, K. M., & Saleem, R. S. Z. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220214104010 · Cited by 20
Regulatory mechanism and research progress of ferroptosis in obstetrical and gynecological diseases
Wang, X., Wei, Y., Wei, F., & Kuang, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1146971 · Cited by 23
Dong, X., Xu, L., Wang, S., Jiao, X., Yan, S., Huang, Y., Yuan, M., & Wang, G. (2023) · Molecular Human Reproduction · doi:10.1093/molehr/gaad046 · Cited by 20
CRISPR activation screens identify the SWI/SNF ATPases as suppressors of ferroptosis
Bhat, K. P., Vijay, J., Vilas, C. K., Asundi, J., Zou, J., Lau, T., Cai, X. T., Ahmed, M., Kabza, M., Weng, J., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114345 · Cited by 23
Nair, P. M. G., Park, S. Y., & Choi, J. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.04.004 · Cited by 20
Development of therapies for rare genetic disorders of GPX4: roadmap and opportunities
Cheff, D. M., Muotri, A. R., Stockwell, B. R., Schmidt, E. E., Ran, Q., Kartha, R. V., Johnson, S. C., Mittal, P., Arnér, E. S. J., Wigby, K. M., et al. (2021) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-021-02048-0 · Cited by 24
DMPS and N-acetylcysteine induced renal toxicity in mice exposed to mercury
Brandão, R., Cibin, F. W. S., Zeni, G. R., da Rocha, J. B. T., & Nogueira, C. W. (2006) · BioMetals · doi:10.1007/s10534-005-4020-3 · Cited by 20
Kernstock, R. M., & Girotti, A. W. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.07.014 · Cited by 20
Chambers, S. J., Lambert, N., & Williamson, G. (1994) · International Journal of Biochemistry · doi:10.1016/0020-711x(94)90097-3 · Cited by 20
Biphasic changes in phospholipid hydroperoxide levels during renal ischemia/reperfusion
Beckman, J. K., Yoshioka, T., Knobel, S. M., & Greene, H. L. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90148-v · Cited by 20
1H-NMR studies of lipid extracts of rat liver mitochondria
Pollesello, P., Eriksson, O., Kvam, B. J., Paoletti, S., & Saris, N.-E. L. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91904-q · Cited by 20
A prospective therapeutic strategy: GPX4-targeted ferroptosis mediators
Qian, J.-Y., Lou, C.-Y., Chen, Y., Ma, L., Hou, W., & Zhan, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117015 · Cited by 20
Zhang, W., Qiao, W., & Zuo, L. (2022) · Tissue and Cell · doi:10.1016/j.tice.2022.101828 · Cited by 19
Emerging Potential Therapeutic Targets of Ferroptosis in Skeletal Diseases
Liu, X., Wang, T., Wang, W., Liang, X., Mu, Y., Xu, Y., Bai, J., & Geng, D. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3112388 · Cited by 18
Microenvironment immune response induced by tumor ferroptosis—the application of nanomedicine
Tian, Y., Liu, Z., Wang, J., Wang, R., Zhu, L., Zhu, Z. G., & Wang, X. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1019654 · Cited by 19
Cheng, Y., Wang, X., Huang, S., Zhang, L., Lan, B., Li, X., Chen, X., Liu, Z., Su, Y., Xi, L., et al. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.102063 · Cited by 20
Ferroptosis: a dual-edged sword in tumour growth
Zhao, X., Li, X., & Xu, Y. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1330910 · Cited by 21
Oxidative Stress, Selenium Redox Systems Including GPX/TXNRD Families
Ingold, I., & Conrad, M. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_6 · Cited by 19
Reduction of polyunsaturated fatty acid hydroperoxides by human brain glutathione peroxidase
Kaplan, E., & Ansari, K. A. (1984) · Lipids · doi:10.1007/bf02534472 · Cited by 19
Tirmenstein, M. A., & Reed, D. J. (1989) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(89)90077-0 · Cited by 19
Ferroptosis in Ischemic Stroke and Related Traditional Chinese Medicines
Ma, R., Sun, X., Liu, Z., Zhang, J., Yang, G., Tian, J., & Wang, Y. (2024) · Molecules · doi:10.3390/molecules29184359 · Cited by 20
Albiñana, V., Recio-Poveda, L., González‐Peramato, P., Martínez‐Piñeiro, L., Botella, L. M., & Cuesta, Á. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031325 · Cited by 18
Ferroptosis, Acyl Starvation, and Breast Cancer
Bobiński, R., Dutka, M., Pizon, M., Waksmańska, W., & Pielesz, A. (2022) · Molecular Pharmacology · doi:10.1124/molpharm.122.000607 · Cited by 20
Review of ferroptosis in colorectal cancer: Friends or foes?
Wu, Z., Fang, Z.-X., Hou, Y.-Y., Wu, B., Deng, Y., Wu, H.-T., & Liu, J. (2023) · World Journal of Gastroenterology · doi:10.3748/wjg.v29.i3.469 · Cited by 19
Ferroptosis: potential targets and emerging roles in pancreatic diseases
Huang, Z., Ma, Y., Sun, Z., Cheng, L., & Wang, G. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03625-x · Cited by 19
Han, X., Fan, Z., Yu, Y., Liu, S., Hao, Y., Huo, R., & Wei, J. (2013) · IUBMB Life · doi:10.1002/iub.1220 · Cited by 18
Pihlanto, A., Johansson, T., & Mäkinen, S. (2012) · Engineering in Life Sciences · doi:10.1002/elsc.201100137 · Cited by 18
Bowyer, J. N., Rout-Pitt, N., Bain, P. A., Stone, D. A. J., & Schuller, K. A. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.04.002 · Cited by 18
Promotion of iron‐induced rat liver microsomal lipid peroxidation by copper
Beckman, J. K., Borowitz, S. M., Greene, H. L., & Burr, I. M. (1988) · Lipids · doi:10.1007/bf02535597 · Cited by 18
Tampo, Y., & Yonaha, M. (1990) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.1990.tb00744.x · Cited by 18
Daolio, S., Traldi, P., Ursini, F., Maiorino, M., & Gregolin, C. (1983) · Journal of Mass Spectrometry · doi:10.1002/bms.1200100904 · Cited by 18
Ferroptosis in radiation-induced brain injury: roles and clinical implications
Li, L., Liu, X., Han, C., Tian, L., Wang, Y., & Han, B. (2024) · BioMedical Engineering OnLine · doi:10.1186/s12938-024-01288-y · Cited by 17
Selenium and selenoproteins: key regulators of ferroptosis and therapeutic targets in cancer
Lee, J., & Roh, J. (2025) · Journal of Molecular Medicine · doi:10.1007/s00109-025-02563-8 · Cited by 17
SharathBabu, B. N., Shivangi, S., Valiyaveettil, A., Annaraj, B., & Mugesh, G. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.047 · Cited by 20
Deng, Y., Feng, Y., Lv, Z., He, J., Chen, X., Wang, C., Yuan, M., Xu, T., Gao, W., Chen, D., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.994130 · Cited by 17
Ironing out the details: ferroptosis and its relevance to diabetic cardiomyopathy
Gawargi, F. I., & Mishra, P. K. (2023) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00117.2023 · Cited by 18
Huang, X., Zhuang, P., ZHANG, L.-Z., Liu, J. Y., Zhang, T., Feng, G., & Zhao, F. (2014) · Journal of Applied Ichthyology · doi:10.1111/jai.12608 · Cited by 17
Li, Z., Huo, X., Zhang, S., Lü, J., Li, C., Guo, M., Fu, R., He, Z., Du, X., & Chen, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127355 · Cited by 16
Skin Burn Injury and Oxidative Stress in Liver and Lung Tissues of Rabbit Models
Sabeh, F., Boxter, C. R., & Norton, S. J. (1995) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1995.33.6.323 · Cited by 17
Sposito, C., Camargo, M., Tibaldi, D. S., Barradas, V., Cedenho, A. P., Nichi, M., Bertolla, R. P., & Spaine, D. M. (2017) · International braz j urol · doi:10.1590/s1677-5538.ibju.2016.0323 · Cited by 17
Protective Role of Glutathione, Thiols, and Analogues in Mutagenesis and Carcinogenesis
Jernström, B., Morgenstern, R., & Moldéus, P. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2984-2_13 · Cited by 17
Benazza, M., Halila, S., Viot, C., Danquigny, A., Pierru, C., & Demailly, G. (2004) · Tetrahedron · doi:10.1016/j.tet.2004.01.061 · Cited by 17
Biological and Biochemical Aspects of Selenium Compounds
Bhuyan, B. J., & Mugesh, G. (2011) · Wiley eBooks · doi:10.1002/9783527641949.ch9 · Cited by 17
Wientjens, C., Doverman, M., Zurkovic, J., More, T. H., Surendar, J., Nesic, S., Sarici, C., Utecht, T. D., Pohl, J., Pollock, J., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.11.018 · Cited by 17
Function and regulation of GPX4 in the development and progression of fibrotic disease
Li, Z., Zhu, Z., Liu, Y., Liu, Y., & Zhao, H. W. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30780 · Cited by 16
Wei, Z., Hao, C., Radeen, K. R., Zheng, H., Kettimuthu, K., Maner-Smith, K. M., Toyokuni, S., & Fan, X. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407842121 · Cited by 16
Januel, C., Hentati, F. E., Carreras, M., Arthur, J. R., Calzada, C., Lagarde, M., & Véricel, E. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.07.015 · Cited by 16
Schaffroth, C., Bogacz, M., Dirdjaja, N., Nißen, A., & Krauth‐Siegel, R. L. (2015) · Molecular Microbiology · doi:10.1111/mmi.13223 · Cited by 16
Yu, H., Liu, J., Liu, X., Zang, T., Luo, G., & Shen, J. (2005) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpc.2005.05.003 · Cited by 16
Brigelius‐Flohé, R., Maiorino, M., Flohé, L., & Ursini, F. (2001) · CRC Press eBooks · doi:10.1201/9780203904046.pt9 · Cited by 16
Ramasarma, T., Muakkassah-Kelly, S. F., & Hochstein, P. (1984) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(84)90124-3 · Cited by 16
Wang, J., Tian, Q., Liu, Y., Cai, C., Fu, S., Li, J., Guan, Y., Liao, X., Su, D., Sun, T., et al. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02414-7 · Cited by 18
Wei, H., Peng, Z., Chen, Y., Guo, J., Chen, L., & Shao, K. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.04.003 · Cited by 15
Lipid Metabolic Alterations in KRAS Mutant Tumors: Unmasking New Vulnerabilities for Cancer Therapy
Saliakoura, M., & Konstantinidou, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021793 · Cited by 15
Ferroptosis: An Emerging Target for Bladder Cancer Therapy
Shan, Z., Tang, W., Shi, Z., & Shan, T. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45100517 · Cited by 18
Screening of potential key ferroptosis-related genes in Chronic Obstructive Pulmonary Disease
Cao, Y., Pan, H., Yang, Y., Zhou, J., & Zhang, G. (2023) · International Journal of COPD · doi:10.2147/copd.s422835 · Cited by 15
Li, N., Jiang, X., Zhang, Q., Huang, Y., Wei, J., Zhang, H., & Luo, H. (2024) · Journal of Ovarian Research · doi:10.1186/s13048-024-01366-8 · Cited by 15
Hu, Z., Lee, K. S., Choo, Y. M., Yoon, H. J., Kim, I., Wei, Y., Gui, Z. Z., Zhang, G. Z., Sohn, H. D., & Jin, B. R. (2009) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2009.09.010 · Cited by 15
Flohé, L. (2011) · Advanced topics in science and technology in China · doi:10.1007/978-3-642-22236-8_1 · Cited by 15
Hochstein, P. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90112-8 · Cited by 15
Scimeca, M. S., Lisk, D. J., Prolla, T. A., & Lei, X. G. (2005) · Experimental Biology and Medicine · doi:10.1177/153537020523001003 · Cited by 15
Barja, G. (1996) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4613-0325-1_9 · Cited by 15
Effects of dietary fat and 1,2-dimethylhydrazine on microsomal lipid peroxidation
Kuratko, C. N. (1994) · The Journal of Nutritional Biochemistry · doi:10.1016/0955-2863(94)90020-5 · Cited by 15
Targeting ferroptosis in cancer stem cells: A novel strategy to improve cancer treatment
Wang, L., Zhu, Y., Huang, C., Pan, Q., Wang, J., Li, H., Huang, Y., Yi, G., Li, Z., Qi, S., et al. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101678 · Cited by 14
Lv, D., Shi, Y., Kou, L., Zhang, D., Guo, Y., & Zhao, S. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107915 · Cited by 14
From pathogenesis to treatment: the emerging role of ferroptosis in Parkinson’s disease
Tu, R., Han, Z., Zhang, H., Jia, X., Sun, T., Liu, H., Li, J., Tang, M., & Wang, S. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1709561 · Cited by 15
Wu, C., Bao, S., Sun, H., Chen, X., Yang, L., Li, R., & Peng, Y. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-023-04895-w · Cited by 14
Fluorescence and Lifetime Imaging of Endoplasmic Reticulum Polarity Change During Ferroptosis
Li, M., Chen, Y., He, W., & Guo, Z. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202401285 · Cited by 14
Sciaccotta, R., Gangemi, S., Penna, G., Giordano, L., Pioggia, G., & Allegra, A. (2024) · Antioxidants · doi:10.3390/antiox13040475 · Cited by 15
Kim, S. Y., Tang, M., Lu, T., Chih, S. Y., & Li, W. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149045 · Cited by 17
Understanding the Mechanism of Ferroptosis in Neurodegenerative Diseases
Ma, J., Liu, J., Chen, S., Zhang, W., Wang, T., Cao, M., Yang, Y., Du, Y., Cui, G., & Du, Z. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2908291 · Cited by 15
Fundamental mechanisms of cell death for polycystic ovary syndrome
Li, Y., Peng, Y., Yang, Y., Xu, N., Shi, T., Liu, R., Luan, Y., & Yin, C.-H. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102043 · Cited by 14
How exercise induces oxidative eustress
Cobley, J. N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00023-7 · Cited by 14
Self-assembled nanomaterials for ferroptosis-based cancer theranostics
Ma, G., Wang, K., Pang, X., Xu, S., Gao, Y. Z., Liang, Y., Yang, J., Zhang, X., Sun, X. J., & Dong, J. (2023) · Biomaterials Science · doi:10.1039/d2bm02000a · Cited by 14
Purification of rat liver plasma membrane glutathione transferase
Horbach, M., Sies, H., & Akerboom, T. P. M. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18845.x · Cited by 14
Funk, C. D., Boubez, W., & Powell, W. S. (1987) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(87)90021-x · Cited by 14
Yukawa, O., Nakajima, T., Miura, Y., Ueda, J., & Ozawa, T. (2005) · International Journal of Radiation Biology · doi:10.1080/09553000500401445 · Cited by 14
Wang, Z., Wang, F., Duan, R., & Liu, J. (2007) · BMB Reports · doi:10.5483/bmbrep.2007.40.3.412 · Cited by 14
Scholz, R. W., Graham, K., Wynn, M. K., & Reddy, C. C. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-584552-6.50027-6 · Cited by 14
Human Cytochrome P450′ are Pro-oxidants in Iron/Ascorbate-Initiated Microsomal Lipid Peroxidation
Lambert, N., Chambers, S. J., Plumb, G. W., & Williamson, G. (1996) · Free Radical Research · doi:10.3109/10715769609088015 · Cited by 14
Gromadzka, G., Tarnacka, B., & Cieślik, M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27010522 · Cited by 19
Saito, Y., Noguchi, N., & Niki, E. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.12.011 · Cited by 13
Research progress of ferroptosis and inflammatory bowel disease
Ma, B., Hu, X., Ai, X., & Zhang, Y. (2024) · BioMetals · doi:10.1007/s10534-024-00604-2 · Cited by 14
RETRACTED ARTICLE: Regulating ferroptosis by non-coding RNAs in hepatocellular carcinoma
Sun, L., Cao, H., Wang, Y., & Wang, H. (2024) · Biology Direct · doi:10.1186/s13062-024-00530-w · Cited by 14
RetractedWang, Y., Fleishman, J. S., Li, Y., Cao, Y., Wei, H., Zhang, Z., Chen, J., & Ding, M. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5714 · Cited by 13
Li, X., Xu, H., Liu, K., Shi, M., Zeng, X., & Liu, X. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114322 · Cited by 15
Maiorino, M., Bosello-Travain, V., Cozza, G., Roveri, A., Toppo, S., & Ursini, F. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_14 · Cited by 13
Expression of Phospholipid Hydroperoxide Glutathione Peroxidase(PHGPx) mRNA in Rat Testes.
Mori, H., Nomura, T., Seno, M., Miki, Y., Kimura, T., Kogami, T., & Sasaki, J. (2001) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.34.25 · Cited by 13
The underlying pathological mechanism of ferroptosis in the development of cardiovascular disease
Zhang, L.-L., Tang, R., & Yang, Y. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.964034 · Cited by 14
Cardiolipin drives the catalytic activity of GPX4 on membranes: Insights from the R152H mutant
Roveri, A., Giacinto, F. D., Rossetto, M., Cozza, G., Cheng, Q., Miotto, G., Zennaro, L., Paolo, M. L. D., Arnér, E. S. J., Spirito, M. D., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102806 · Cited by 14
Advances in neutrophil extracellular traps and ferroptosis in sepsis-induced cardiomyopathy
Zeng, M., Niu, Y., Huang, J., & Deng, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1590313 · Cited by 15
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