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 701–800 of 885
Implications of mitochondrial phosphatidylethanolamine in neuronal health and neurodegeneration
Zuo, Y., Amireddy, N., & Cai, Q. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00201 · Cited by 6
Saad, . M., Salem, E. A., Elhussieny, O., Waheeb, T. S., & Elsayed, A. E. (2025) · European journal of medical research · doi:10.1186/s40001-025-03178-y · Cited by 5
Ferroptosis: The Pivotal Link in Cardiovascular Diseases Pathogenesis and Therapy
Guo, S., Liu, J., Hua, J., Ding, L., & Chen, Q. (2025) · International Journal of General Medicine · doi:10.2147/ijgm.s581227 · Cited by 8
Zhang, R., Ren, Y., Zhao, Y., Zheng, H., Luo, Y., Liu, Y., Wang, L., & Zhang, L. (2026) · Journal of Integrative Plant Biology · doi:10.1111/jipb.70235 · Cited by 5
Harnessing ferroptosis from multilayer defense networks to nanoplatforms for specific cancer therapy
Xu, X., Wang, X., Jiang, W., Kamaruddin, W. H. A., Fang, C., & Zhang, P. (2026) · BMEMat · doi:10.1002/bmm2.70080 · Cited by 5
Ferroptosis as a hero against oral cancer
Vijayarangam, V., Deviparasakthi, M. K. G., Balasubramanian, P., Palaniyandi, T., Ravindran, R., Suliman, M., Saeed, M., Natarajan, S., Sivaji, A., & Baskar, G. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155637 · Cited by 5
Enlightening the Mechanism of Ferroptosis in Epileptic Heart
Akyüz, E., Saleem, Q. H., Sarı, Ç., Auzmendi, J., & Lazarowski, A. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867330666230223103524 · Cited by 5
Morrow, J. P., Pizzi, D., Mazrad, Z. A. I., Bush, A. I., & Kempe, K. (2023) · Biomaterials Science · doi:10.1039/d2bm02087d · Cited by 5
Niu, J., Guo, W., Lu, A., Han, G., Wang, G., Peng, B., & Zhao, J. (2023) · Medicine · doi:10.1097/md.0000000000035002 · Cited by 5
Manipulating Redox Signaling to Block Tumor Angiogenesis
Mugoni, V., & Mattia, M. (2013) · InTech eBooks · doi:10.5772/54593 · Cited by 7
Purification and characterisation of chicken liver monomeric glutathione peroxidase
Miyazaki, S., & MOTOI, Y. (1996) · British Poultry Science · doi:10.1080/00071669608417894 · Cited by 5
Induction of cancer cell-specific ferroptosis by non-thermal plasma exposure
Okazaki, Y., & Toyokuni, S. (2020) · Japanese Journal of Applied Physics · doi:10.35848/1347-4065/abbc56 · Cited by 5
Daher, B., Meira, W., Durivault, J., Gotorbe, C., Pouysségur, J., & Vučetić, M. (2022) · Cancers · doi:10.3390/cancers14133154 · Cited by 5
Ferroptosis in Nervous System Diseases
Wan, J., Yang, X., & Wang, J. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_10 · Cited by 5
Yılmaz, S. (2000) · DergiPark (Istanbul University) · Cited by 5
Histochemical localization of oxidized glutathione-catalysing enzymes in human term placenta
Glazyrin, A. L., Kolesnikov, S. I., & Safronov, A. Y. (1993) · The Histochemical Journal · doi:10.1007/bf00161043 · Cited by 5
Morandat, S., Bortolato, M., Nicol, F., Arthur, J. R., Chauvet, J., & Roux, B. (2004) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2004.02.011 · Cited by 5
Mishima, E., & Conrad, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00009-7 · Cited by 5
Biological Systems Which Suppress Lipid Peroxidation
McCay, P. B., Lai, E. K., Gibson, D. D., Poyer, J. L., Powell, S. R., & Brueggemann, G. (1988) · Developments in cardiovascular medicine · doi:10.1007/978-1-4613-1743-2_2 · Cited by 5
Bast, A., & Haenen, G. R. M. M. (1990) · Springer eBooks · doi:10.1007/978-1-4684-7427-5_33 · Cited by 5
Does Cytochrome P-450 Mediate the Effects of Norepinephrine in the Hepatocyte?
Holtzman, J. L., Prasad, J. S., Erickson, R. R., Chen, N.-Q., Liu, Y.-X., & Srivastava, S. P. (1989) · Drug Metabolism Reviews · doi:10.3109/03602538909103566 · Cited by 5
Venekei, I. (1987) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(87)90112-3 · Cited by 5
Ursini, F., Maiorino, M., Roveri, A., Brigelius‐Flohé, R., Schuckelt, R., Wolf, B., & Flohé, L. (1991) · Elsevier eBooks · doi:10.1016/b978-0-08-041749-3.50111-x · Cited by 5
Advances in Ferroptosis in Chronic Inflammatory Diseases of the Upper and Lower Airways
Li, J., Li, J., Gao, Y., Zhang, L., & Zhang, Y. (2025) · International Archives of Allergy and Immunology · doi:10.1159/000547363 · Cited by 4
Ferroptosis in pain: evidence, challenges, and opportunities
Yan, Q., Wang, F., Liu, M., Mao, J., Zhao, Z., & Wang, B. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1673783 · Cited by 4
Selenoproteins: Minute yet vital players governing cellular fate
Xia, C., Wu, Y., Zhang, H., Qin, L., Hu, Y., & Fu, C. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101938 · Cited by 6
Schweizer, U., & Fabiano, M. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104083 · Cited by 7
Magarditchian, G., Berest, I., Ziogou, A., Matsushita, M., Reid, M. E., Othman, A., & Köpf, M. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2528153123 · Cited by 4
Ferroptosis: Physiological and pathophysiological aspects
Conrad, M., & da Silva, M. C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00010-9 · Cited by 4
Detection of Ferroptosis in Models of Brain Diseases
Shen, D., Yang, F., & Li, Q. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3433-2_21 · Cited by 4
Guo, C., Guo, Y. X., Zhang, J., Wang, J., Su, L., Ning, X., Chen, X., & Yan, H. (2025) · Experimental Eye Research · doi:10.1016/j.exer.2025.110421 · Cited by 5
Glutathione Peroxidase 4 and Ferroptosis
Angeli, J. P. F., Proneth, B., & Conrad, M. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_43 · Cited by 4
Li, J., Jia, W., Ma, G., Zhang, X., An, S., Wang, T., & Shi, S. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00122h · Cited by 4
Nonmetabolic role for CKB in ferroptosis
Mishima, E., & Conrad, M. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01104-0 · Cited by 4
Chlorobenzoquinones Aggravate RSL3-Induced Ferroptosis in ROS-Dependent Manner
Yu, X., Chen, S., & Wang, H. (2024) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.4c00100 · Cited by 4
Ineu, R. P., dos Santos, M. M., Barros, O. S. D. R., Nogueira, C. W., da Rocha, J. B. T., Zeni, G. R., & Pereira, M. E. (2012) · Cell Biology and Toxicology · doi:10.1007/s10565-012-9217-y · Cited by 4
Helmut Sies and the compartmentation of hydroperoxide metabolism
Flohé, L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.11.018 · Cited by 4
Zhang, J., Wang, Y., Fleishman, J. S., Zheng, W., Wang, Y., Meng, F., & Wang, Y. (2025) · Antioxidants and Redox Signaling · doi:10.1089/ars.2024.0807 · Cited by 3
Ng, S., Ng, A. C., Ng, M. C., Ng, S., Arcuri, F., Genega, E. M., Watkins, J. C., Roberts, D. J., House, M. D., O’Tierney-Ginn, P. F., et al. (2025) · Reproductive Sciences · doi:10.1007/s43032-025-01935-2 · Cited by 4
Toxoplasma gondii-induced ferroptosis contributes to acute lung injury in mice
Yuan, X., Liu, Z., Ma, Y., Liu, F., Bao, P., Du, B., Zhang, X., Gong, P., Zhang, N., Li, J., et al. (2025) · Parasites & Vectors · doi:10.1186/s13071-025-07207-x · Cited by 3
Tang, W., Qin, J., Teng, F., Dong, J., & Wei, Y. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157746 · Cited by 3
Liu, J., Wang, K., Hao, Z., Fan, Q., Ma, S., & Xu, L. (2026) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00736-2 · Cited by 3
Yuan, F., Han, Z., Yang, S., Chen, J., Li, R., Zhang, Z., Song, J., Wang, D., & Ban, Y. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1758041 · Cited by 5
Jia, H., Zhou, L.-Q., Wen, R.-B., Yu, Y., Wang, N., Zhang, T.-S., Zhi-ying, P., Chen, J.-F., Yu, G., & Zhang, W. (2026) · LabMed discovery. · doi:10.1016/j.lmd.2026.100119 · Cited by 3
Liu, Y., & Chang, Y.-Z. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104124 · Cited by 3
Liu, Y. (2026) · APOPTOSIS · doi:10.1007/s10495-026-02377-0 · Cited by 3
Li, J., Liu, P., Zhang, J., Tian, Y., Sun, G., Kang, X., Li, D., & Gu, Y. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105751 · Cited by 3
Yeni Bir Hücre Ölüm Şekli Olarak Ferroptozis
Çelenk, A. (2021) · Arşiv Kaynak Tarama Dergisi · doi:10.17827/aktd.980659 · Cited by 3
Ahmed, A. M. (2013) · Pakistan Journal of Zoology · Cited by 3
Jiu, M., Li, J., Gao, X., Wang, L., Wang, X., & Liu, S. (2015) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21225 · Cited by 3
Phospholipid-hydroperoxide glutathione peroxidase
(2006) · Springer eBooks · doi:10.1007/3-540-37704-2_28 · Cited by 3
The Role of Glutathione Pathways in the Prevention of Atherosclerosis
Holtzman, J. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-72347-1_9 · Cited by 3
Mouse Models for Glutathione Peroxidase 4 (GPx4)
Conrad, M. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_43 · Cited by 3
Enzyme Mimetic Chemistry of Organoselenium Compounds
Bhowmick, D., & Mugesh, G. (2013) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0726 · Cited by 3
Dissertation zur Erlangung des Doktorgrades der Fakultät für Biologie
München, L.-M.-U. (2013) · Cited by 3
Cytotoxic effects of selenium conjugated transferrins on leukemia cell lines
Goswami, D. (2014) · ThinkTech (Texas Tech University) · Cited by 3
Fifty years of selenoenzyme research: Discoveries, state-of-the-art and future directions
Flohé, L., Maiorino, M., & Ursini, F. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.03.011 · Cited by 3
Constitutive and Inducible Repair Systems in Oxidative Stress
Ryter, S. W., Pacifici, R. E., & Davies, K. J. A. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-584552-6.50031-8 · Cited by 3
He, M., Zhai, W., Wang, H., & Liu, H. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47050326 · Cited by 2
Crosstalk between autophagy and ferroptosis in diabetes
Xie, E., Wei, X., Zheng, Z., Yu, Q., Liu, M., Zhang, H., Jiang, Z., Gao, Y., & Yang, L. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101936 · Cited by 2
Redundant or resilient? A systems view of ferroptosis surveillance mechanisms
Liang, D., & Jiang, X. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2025.11.013 · Cited by 2
Mitochondria setting the stage for ferroptosis
Ahola, S. (2026) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2026.06.006 · Cited by 2
Chen, Y., Yang, X. Y., Lv, D., Tang, L., & Liu, Y.-W. (2024) · Clinical & Translational Oncology · doi:10.1007/s12094-024-03617-y · Cited by 2
Troubling bonds: lipid unsaturation promotes selenium dependency and sensitivity to ferroptosis
dos Santos, A. F., & Angeli, J. P. F. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00150-x · Cited by 2
Liao, C., Guo, J., Li, S., Rui, J., Gao, K., Lao, J., & Zhou, Y. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00499 · Cited by 2
Immunometabolism in macrophage cell death
Cahill, S. E., Stine, L., & Humphries, F. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-15447-8.00004-0 · Cited by 2
Effect of pH and glutathione on lipid peroxidation in tocopherol-enriched liposomes
Dmitriev, L. F., Ivanova, M. V., & Lebedev, A. V. (1995) · Bulletin of Experimental Biology and Medicine · doi:10.1007/bf02445013 · Cited by 2
Antioxidant Defenses in the Vascular Wall
Stocker, R. (2000) · Developments in cardiovascular medicine · doi:10.1007/978-1-4615-4649-8_3 · Cited by 2
Elbessoumy, A. M., Ghareeb, D. A., & Khalil, A. A. (2010) · Cited by 2
Edens, F. W., & Sefton, A. E. (2016) · Journal of Applied Animal Nutrition · doi:10.1017/jan.2016.6 · Cited by 2
Synthetic Mimics of Selenoproteins
Bhabak, K. P., & Mugesh, G. (2011) · Advanced topics in science and technology in China · doi:10.1007/978-3-642-22236-8_14 · Cited by 2
Li, M., Gong, J., Liu, Q., & Wu, W. (2024) · Experimental Dermatology · doi:10.1111/exd.15114 · Cited by 2
Peng, T., & Li, M. (2024) · International Urology and Nephrology · doi:10.1007/s11255-024-04302-3 · Cited by 2
THE ROLE OF GLUTATHIONE PEROXIDASE IN THE ANTI‐OXIDANT SYSTEM OF ERYTHROCYTES
Fujii, S. (1988) · British Journal of Haematology · doi:10.1111/j.1365-2141.1988.tb06200.x · Cited by 2
Ferroptosis in female reproductive diseases: from potential pathogenesis to therapyPreprint
Zhang, J., Chen, G., Zhang, M., Wang, J., Xing, Q., Zhang, W., He, X., Xu, Y., Cao, Y., & Wang, T. (2023) · doi:10.22541/au.167367791.15223634/v1 · Cited by 2
Mechanisms of triggering antitumor immunity: from photodynamic effects to immunogenic cell death
Sleptsova, E. E., Redkin, T. S., Saviuk, M. O., & Turubanova, V. D. (2024) · Genes and Cells · doi:10.17816/gc546129 · Cited by 1
Ferroptosis in biliary tract cancer: Molecular mechanisms and therapeutic applications (Review)
Zou, R.-Q., Dai, Y.-S., Yang, S., Hu, H., Li, F., & Liu, F. (2025) · International Journal of Oncology · doi:10.3892/ijo.2025.5819 · Cited by 2
Lin, Y.-H., Wang, X.-W., Li, Y.-A., Chen, T.-Y., Lian, W., Wang, F., Lan, M.-Y., Liou, C.-W., & Lin, T. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102132 · Cited by 2
Yuping, Z., Xiangmei, L., Ruiyang, W., Wenbo, Z., & Huaqi, W. (2026) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1080/15412555.2025.2602632 · Cited by 1
Soleimani, A., Khalilian, S., Fathi, M., Tajik, Z., & Ghafouri-Fard, S. (2026) · Human Gene · doi:10.1016/j.humgen.2026.201541
Tan, Y.-F., Chen, X., Wang, C., Liang, A.-L., Lu, W.-Y., Feng, L.-M., Huang, Q., Jiang, Y., Liu, S., Xia, X.-B., et al. (2026) · Phytochemistry · doi:10.1016/j.phytochem.2026.114855 · Cited by 1
Li, J., Xia, X., Wang, K., Xu, X., & Li, C. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1785916 · Cited by 1
Kim, K., Lee, C.-H., Kim, C.-E., Park, E.-Y., Hwang, J.-S., & Oh, Y. S. (2026) · Antioxidants · doi:10.3390/antiox15060755 · Cited by 1
Ferroptosis in depression: mechanisms, association, and therapeutic strategies
Zhang, C., Chen, S. Y., Yan, C., Jiang, Y., Wang, Y., Yu, Z., Xie, T., Tian, M., Yao, G., Yan, Y., et al. (2026) · Journal of Neural Transmission · doi:10.1007/s00702-026-03248-3 · Cited by 1
Wang, F., Zhou, H., KONG, B., FAN, J., CHEN, H., & LIU, J. (2007) · Chemical Research in Chinese Universities · doi:10.1016/s1005-9040(07)60123-8 · Cited by 1
Synthesis of Poly(amidoamine) Dendrimer with a Diphenyl Diselenide Core
Tajima, T., Yamaguchi, Y., Shiomoto, Y.-H., & Takaguchi, Y. (2010) · Phosphorus, sulfur, and silicon and the related elements · doi:10.1080/10426501003767102 · Cited by 1
de Fisiologia, D. (2009) · Cited by 1
The Role of Apelin and Protamine Sulfate in Bile Duct Ligation-Induced Liver Fibrosis in Rats
Moursi, S. M. M., Bahaie, E. E., Abdelhamid, A. M., & El-sayed, S. F. (2023) · Pharmaceutical Chemistry Journal · doi:10.1007/s11094-023-02995-x · Cited by 1
Zhao, M., Xu, J., Zhu, S., & Li, P. (2023) · Journal of Biomedical Research & Environmental Sciences · doi:10.37871/jbres1854 · Cited by 1
Li, L., Yang, F., Liu, H., Zhang, R., Liang, R., Xu, W., Li, Y., Luo, M., Zhai, Z., Zhuang, J., et al. (2024) · Rheumatology & autoimmunity · doi:10.1002/rai2.12133 · Cited by 1
Nakanishi, T., Uchiyama, T., Uchida, M., Erickson, L., & Kawahara, S. (2024) · British Poultry Science · doi:10.1080/00071668.2024.2412167 · Cited by 1
Dan, Z., Liu, W., Zhang, H., Shi, X., Zhu, R., Yang, M., Wang, Y., & Zhu, H. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112080 · Cited by 1
Role of Oxidized Lipids in Atherosclerosis
Garelnabi, M., Kakumanu, S., & Litvinov, D. Y. (2012) · InTech eBooks · doi:10.5772/32999 · Cited by 2
Overcoming Therapeutic Challenges for Pancreatic Ductal Adenocarcinoma with xCT Inhibitors
Vučetić, M., Daher, B., Cassim, S., Parks, S. K., & Pouysségur, J. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_2 · Cited by 1
In vivo functions of mammalian glutaredoxin 2
Lönn, M. E. (2008) · Figshare · Cited by 1
Seiler, A. (2007) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.9432 · Cited by 1
Tocopherol stability in bell pepper microsomal membranes during short‐term storage
Erickson, M. C., Wang, G. D., Cowart, D. M., & Shewfelt, R. L. (1995) · Phytochemical Analysis · doi:10.1002/pca.2800060107 · Cited by 1
Contreras‐Chova, F. (2011) · Institutional Repository of the University of Granada (University of Granada) · Cited by 1
Oxidative Stress and Radiation-Induced Late Normal Tissue Injury
Robbins, M. E. C., & Zhao, W. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50146-0 · Cited by 1
Götz, M. E., Künig, G., Riederer, P. F., & Youdim, M. B. H. (1996) · Elsevier eBooks · doi:10.1016/b978-044482529-2/50039-1 · Cited by 1
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