Cited by 885Selenium in Biological SystemsRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

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

Ursini, F., Maiorino, M., Valente, M., Ferri, L., Gregolin, C.·1982·Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism

DOI 10.1016/0005-2760(82)90150-3

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/0005-2760(82)90150-3

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
Glutathione S-Transferases
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
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
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
Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system.
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

Show all 25 references

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

Sorted by citations

Items 601–700 of 885

Ferroptosis as an Emerging Target in Diabetic Osteoporosis
Li, C., Gong, H., Zhang, Y., Shi, P., Liu, S., & Zhang, Q. (2025) · The FASEB Journal · doi:10.1096/fj.202500415r · Cited by 13
Single-Molecule Observation of Selenoenzyme Intermediates in a Semisynthetic Seleno-α-Hemolysin Nanoreactor
Jiang, X., Pan, T., Lang, C., Zeng, C., Hou, J., Xu, J., Luo, Q., Hou, C., & Liu, J. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c01204 · Cited by 12
The potential role and mechanism of circRNAs in Ferroptosis: A comprehensive review
Arabpour, J., Rezaei, K., Khojini, J. Y., Razi, S., Hayati, M. J., & Hayat, S. M. G. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155203 · Cited by 13
Antiperoxidative potential of p-coumaric acid, a common dietary phenol, in adjuvant-induced arthritis in rats
Pragasam, S. J. (2012) · Journal of Chinese Integrative Medicine · doi:10.3736/jcim20120815 · Cited by 12
FeC2O4/g-C3N4 self-assemble nanorods regulate stimuli-responsive ferroptosis via photo-fenton mechanism
Cao, Z., Sun, D., Hu, H., Li, W., Xiong, Z., He, M., Cai, S., Fan, Y., Zheng, L., & Kang, S. (2022) · Applied Surface Science · doi:10.1016/j.apsusc.2022.155671 · Cited by 11
The ferroptosis inducer RSL3 triggers interictal epileptiform activity in mice cortical neurons
Giustizieri, M., Petrillo, S., D’Amico, J., Torda, C., Quatrana, A., Vigevano, F., Specchio, N., Piemonte, F., & Cherubini, E. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1213732 · Cited by 11
Ferrostatin-1 alleviates the damage of C2C12 myoblast and mouse pelvic floor muscle induced by mechanical trauma
He, Y., Huang, G., Hong, S., Zuo, X., Zhao, Z., & Li, H. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01482-2 · Cited by 11
Sodium aescinate induces renal toxicity by promoting Nrf2/GPX4-mediated ferroptosis
Zhu, H., Duan, Y., Yang, Y., Chen, E., Huang, H., Wang, X., & Zhou, J. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.110892 · Cited by 11
Research Progress on Ferroptosis in Multiple Myeloma
Li, P., & Lyu, T. (2024) · Current Treatment Options in Oncology · doi:10.1007/s11864-024-01250-z · Cited by 11
Ferroptosis Inhibition: A Key Opportunity for the Treatment of Ischemia/Reperfusion Injury in Liver Transplantation
Eggenhofer, E., & Proneth, B. (2024) · Transplantation · doi:10.1097/tp.0000000000005199 · Cited by 12
Exploring the role of ferroptosis in esophageal cancer: mechanisms and therapeutic implications
Zhao, D., Li, W., Han, Z., Wang, Z., Li, D., & Li, W. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02696-2 · Cited by 12
Dimers of glutaredoxin 2 as mitochondrial redox sensors in selenite-induced oxidative stress
Scalcon, V., Tonolo, F., Folda, A., Bindoli, A., & Rigobello, M. P. (2019) · Metallomics · doi:10.1039/c9mt00090a · Cited by 11
Partial Purification and Some Interesting Properties of Glutathione Peroxidase from Liver of Camel (Camelus dromedarius)
Chafik, A., Essamadi, A., Çelik, S. Y., Solak, K., & Mavi, A. (2018) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162018010041 · Cited by 11
Cell Death-Osis of Dopaminergic Neurons and the Role of Iron in Parkinson's Disease
Lima, I. S., Pêgo, A. C., Barros, J. T., Prada, A. R., & Gozzelino, R. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8229 · Cited by 11
Treatment, oxidation and health aspects of fats and oils
Chow, C. K., & Gupta, M. K. (1994) · Springer eBooks · doi:10.1007/978-1-4615-2109-9_11 · Cited by 11
Tissue distribution of monomeric glutathione peroxidase in broiler chicks
Miyazaki, S., & MOTOI, Y. (1992) · Research in Veterinary Science · doi:10.1016/0034-5288(92)90083-e · Cited by 11
Glutathione Peroxidase 4
Maiorino, M., Bosello-Travain, V., Cozza, G., Miotto, G., Orian, L., Roveri, A., Toppo, S., Zaccarin, M., & Ursini, F. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_18 · Cited by 11
Cytoprotection against lipid hydroperoxides correlates with increased glutathione peroxidase activities, but not selenium uptake from different selenocompounds
Leist, M., Maurer, S., Schultz, M., Elsner, A., Gawlik, D., & Brigelius‐Flohé, R. (1999) · Biological Trace Element Research · doi:10.1007/bf02784404 · Cited by 11
Monohydroperoxides of linoleic acid in endoplasmic lipids of rats exposed to tetrachloromethane
Frank, H., Wiegand, M., Strecker, M., & Thiel, D. (1987) · Lipids · doi:10.1007/bf02533967 · Cited by 11
Emerging role of tumor microenvironmental nutrients and metabolic molecules in ferroptosis: Mechanisms and clinical implications
Li, D., Zhang, Z., & Wang, L. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117406 · Cited by 10
Decoding ferroptosis: transforming orthopedic disease management
Huo, G., Lin, Y., Liu, L., He, Y., Qu, Y., Liu, Y., Zhu, R., Wang, B., Gong, Q., Han, Z., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1509172 · Cited by 10
Targeting Programmed Cell Death in Acquired Sensorineural Hearing Loss: Ferroptosis, Necroptosis, and Pyroptosis
Zhang, S., Xiao, H., Lin, Y., Tang, X., Tong, W., Shao, B., Li, H., Xu, L., Ding, X., & Chai, R. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01370-y · Cited by 11
The peptide from C- Phycocyanin alleviates myocardial ischemia-reperfusion injury by suppressing ferroptosis via upregulating UCHL3.
Li, Z., Chen, R.-L., Qin, L.-N., Xu, X.-J., Wang, X.-Z., Zhang, G., Liu, Z.-J., Wang, B.-H., Li, B., & Chu, X.-M. (2025) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2025.05.419 · Cited by 10
Inhibition of TRPV4 attenuates ferroptosis against LPS-induced ALI via Ca2+ pathway
Cai, J., XU, G., LIN, Y., ZHOU, B., LUO, Z., YU, S., & LU, J. (2022) · TURKISH JOURNAL OF BIOLOGY · doi:10.55730/1300-0152.2632 · Cited by 10
Aquaporin 1 Facilitates Ferroptosis, M1 Polarization, Mitochondrial Dysfunction, and Autophagy Damage on Lipopolysaccharide-Induced Macrophage Through Down-Regulation of P53 Signaling Pathway
Lv, W., Liang, L., Liu, D., Li, C., Jia, L., & Jin, Y. (2023) · DNA and Cell Biology · doi:10.1089/dna.2023.0016 · Cited by 10
Comparative Aspects of Lipid Peroxidation and Antioxidant Protection in Avian Semen
Speake, B. K., Sparks, N. H. C., & Surai, P. F. (2003) · AOCS Publishing eBooks · doi:10.1201/9781439822234.ch15 · Cited by 10
STRUCTURE AND CATALYTIC MECHANISM OF GLUTATHIONE PEROXIDASE
Flohé, L. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-683275-4.50011-5 · Cited by 10
Dependence of Mouse Liver Phospholipid Hydroperoxide Glutathione Peroxidase on Dietary Selenium
Weitzel, F., Ursini, F., & Wendel, A. (1989) · Springer eBooks · doi:10.1007/978-3-642-74421-1_6 · Cited by 10
Ketogenic diet promotes tumor ferroptosis but induces relative corticosterone deficiency that accelerates cachexiaPreprint
Ferrer, M., Mourikis, N., Davidson, E. E., Kleeman, S. O., Zaccaria, M., Habel, J., Rubino, R., Flint, T. R., Connell, C. M., Lukey, M. J., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.17.528937 · Cited by 10
Integrated ferroptosis, apoptosis, and pyroptosis for liver cancer treatment by an iron single atom-graphene oxide composite
Wang, L., Yin, P., Jing, Z., Zhou, Y., Yang, H. Q., & Chen, L. (2024) · Surfaces and Interfaces · doi:10.1016/j.surfin.2024.104147 · Cited by 9
The impact of ferroptosis and ferroptosis-related non-coding RNAs on breast cancer progression
Liu, W., Jiang, C., Ma, Y., Wang, W., Peng, J., Ma, W., Xu, S., & Wu, D. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1506492 · Cited by 9
Selective Small-Molecule Activator of Patient-Derived GPX4 Variant
Liu, H., Forouhar, F., Saneto, R. P., & Stockwell, B. R. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00158 · Cited by 9
Tumor cell-specific loss of GPX4 reprograms triacylglycerol metabolism to escape ferroptosis and impair antitumor immunity in non-small cell lung cancer
Wang, P., Zhang, S., Chen, X., Yang, X.-D., Huang, S., Yin, H., Duan, H.-Y., Zhou, F., Yu, J., Zhong, B., et al. (2025) · Protein & Cell · doi:10.1093/procel/pwaf101 · Cited by 9
Selenium in Food Chain in Relation to Human and Animal Nutrition and Health
Kurt, B. O., & Ozdemir, S. (2022) · Sustainable plant nutrition in a changing world · doi:10.1007/978-3-031-07063-1_19 · Cited by 8
Cloning, characterization, and expression analysis of goat (Capra hircus) phospholipid hydroperoxide glutathione peroxidase (PHGPx)
Shi, L., Xun, W., Yue, W., ZHANG, C.-X., Ren, Y., Wang, Q., Wu, X., Shi, L., Yang, R., & Lei, F. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.316 · Cited by 9
RETRACTED ARTICLE: Liquiritin reduces ferroptosis in doxorubicin-induced cardiotoxicity through targeting SLC7A11/GPX4 pathway
Wang, M., Liu, M., Tang, L., Shen, L., Xiao, J., & Li, R. (2023) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-023-02515-4 · Cited by 9
Retracted
Effects of phospholipid hydroperoxide glutathione peroxidase mRNA expression on meat quality of M. longissimus dorsi in pigs
Chen, W., Zeng, Y., Cui, J., Chen, Q., Du, J.-F., Yang, L., Hu, Y., YiPing, S., & Qian, Y. (2010) · European Food Research and Technology · doi:10.1007/s00217-010-1407-3 · Cited by 9
A glutathione peroxidase 4 (GPx4) homologue from southern bluefin tuna is a secreted protein: First report of a secreted GPx4 isoform in vertebrates
Bain, P. A., & Schuller, K. A. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.01.004 · Cited by 9
The role of selenium in critical illness: Basic science and clinical implications
Salama, A., Sakr, Y. L., & Reinhart, K. (2007) · Indian Journal of Critical Care Medicine · doi:10.4103/0972-5229.35086 · Cited by 9
The Antioxidant Effects of Glutathione and Ascorbic Acid
Meister, A. (1994) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-7424-3_11 · Cited by 9
Identification of an Endogenous Inhibitor of Arachidonate Metabolism in Human Epidermoid Carcinoma A431 Cells
Chang, W. (2003) · Journal of Biomedical Science · doi:10.1007/bf02256310 · Cited by 9
Molecular cloning of glutathione peroxidase cDNAs from Seriola lalandi and analysis of changes in expression in cultured fibroblast-like cells in response to tert-butyl hydroquinone
Bain, P. A., & Schuller, K. A. (2011) · Aquaculture · doi:10.1016/j.aquaculture.2011.10.027 · Cited by 9
Multiple forms of glutathione S-transferase from pig liver—Reaction with methyl linoleate hydroperoxides
Williamson, G. (1989) · International Journal of Biochemistry · doi:10.1016/0020-711x(89)90023-2 · Cited by 9
Native specific activity of glutathione peroxidase (GPx‐1), phospholipid hydroperoxide glutathione peroxidase (PHGPx) and glutathione reductase (GR) does not differ between normo‐ and hypomotile human sperm samples
Ursini, F., & Maiorino, M. (2005) · International Journal of Andrology · doi:10.1111/j.1365-2605.2005.00493.x · Cited by 9
A non-nucleotide agonist that binds covalently to cysteine residues of STING
Matsumoto, K., Ni, S., Arai, H., Toyama, T., Saito, Y., Suzuki, T., Dohmae, N., Mukai, K., & Taguchi, T. (2022) · Cell Structure and Function · doi:10.1247/csf.22085 · Cited by 9
Ferroptosis defense mechanisms: The future and hope for treating osteosarcoma
Ma, Y., Cong, L., Shen, W., Yang, C., & Ye, K. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.4080 · Cited by 10
The metabolic code of ferroptosis: nutritional regulators of cell death
Tschuck, J., Skafar, V., Angeli, J. P. F., & Hadian, K. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.04.007 · Cited by 11
Ferroptosis in Pneumoconiosis: From Molecular and Cellular Mechanisms to Therapeutic Strategies
Yan, M., Zhang, J., Ji, G., Fang, X., & Mo, C. (2025) · Med Research · doi:10.1002/mdr2.70020 · Cited by 11
Role of Ferroptosis in the Redox Biology of Mycotoxins
Li, K., Zhou, R., Yin, Z., Ren, D., & Fan, S. (2025) · The FASEB Journal · doi:10.1096/fj.202501371r · Cited by 11
Research on the function of GPX4 in tumor-targeted treatment based on its molecular structure and features
Geng, H., Ma, L., Wu, L., Yao, C., Wang, C., Gan, X., Li, Y., & Chen, F. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1594234 · Cited by 9
Regulating Ferroptosis in Leukemic Stem Cells: From Stemness Preservation to Targeted Differentiation Strategies
Wang, Z., Yang, Q., Yang, Y., Liu, M., Zeng, J., Gan, L., Zhou, Q., Li, X., Yang, Z., Yang, Z., et al. (2025) · Stem Cell Reviews and Reports · doi:10.1007/s12015-025-11016-1 · Cited by 9
The interplay mechanisms between gut microbiota and ferroptosis in inflammatory bowel disease
Shi, Z., Zhang, S., Zhai, H., Wu, Q., Li, Y., Xu, H., & Zhang, S. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1753617 · Cited by 9
Ferroptosis: emerging roles in lung cancer and potential implications in biological compounds
Liang, Q., Wang, Y., Li, Y., Wang, J., Liu, C., & Li, Y. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1374182 · Cited by 8
The Effect of Deposition Se on the mRNA Expression Levels of GPxs in Goats from a Se-enriched County of China
Zhang, L., Zhou, Z.-Q., Li, G., & Fu, M. (2013) · Biological Trace Element Research · doi:10.1007/s12011-013-9830-5 · Cited by 8
Activation of CTP:phosphocholine cytidylyltransferase by hypochlorite-oxidized phosphatidylcholines
Drobnies, A. E., Venczel, E. A., & Cornell, R. B. (1998) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(98)00060-5 · Cited by 8
Glutathione peroxidase activity in surgical and autopsied human brains
Ansari, K. A., Bigelow, D. J., & Kaplan, E. (1985) · Neurochemical Research · doi:10.1007/bf00964408 · Cited by 8
OXIDATIVE DAMAGE & REPAIR: INTRODUCTION AND OVERVIEW
Davies, K. J. A. (1991) · Elsevier eBooks · doi:10.1016/b978-0-08-041749-3.50005-x · Cited by 8
Effects of aurothioglucose on iron‐induced rat liver microsomal lipid peroxidation
Beckman, J. K., & Greene, H. L. (1988) · Lipids · doi:10.1007/bf02536212 · Cited by 8
Oxygen Toxicity, Biological Defense Systems and Immunity—A Historical Perspective
Kang, C. R., Sweetser, S., Boylan, L. M., & Spallholz, J. E. (1994) · Journal of Nutritional Immunology · doi:10.1300/j053v03n02_05 · Cited by 8
Reduction of 13-Hydroperoxy-9,11-octadecadienoic Acid by Dopamine-Melanin
ȩ, K. S., Zajdel, A., Swierczek-Zieba, G., Wilczok, A., & Wilczok, T. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7678 · Cited by 8
Emerging ferroptosis inhibitors as a novel therapeutic strategy for the treatment of neonatal hypoxic-ischemic encephalopathy
Huo, L., Fu, J., Wang, S., Wang, H., & Liu, X. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116453 · Cited by 8
Multi-omics Analysis Reveals the Propagation Mechanism of Ferroptosis in Acute Kidney Injury
Yu, H., An, Q., Wang, Z., Hu, B., Yang, Y., Zeng, R., & Yao, Y. (2025) · Inflammation · doi:10.1007/s10753-025-02311-7 · Cited by 8
Ferroptosis: The dawn of reversing drug resistance in digestive cancers
Chen, W., Han, L., Wang, J., & Song, L. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101873 · Cited by 8
Ferroptosis in Autoimmune Diseases: Research Advances and Therapeutic Strategies
He, Z., Liu, B., Xian, Z., Gong, A., & Jia, X. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110449 · Cited by 7
Metabolic Functions and Mechanisms of Selenium, Selenocysteine, and GPX4 Mediated Immune Regulation Through Autophagy in Solid Tumors
Yang, L., Yu, J., Wu, H., Sun, J., Huang, X., Hong, J., Zheng, B., & Zhu, J. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.71230 · Cited by 9
Tipping the balance: NRF2’s dual role in ferroptotic fate
de Souza, I., Teixeira, A. B. D. S., dos Santos, A. F., Angeli, J. P. F., & Rocha, C. R. R. (2026) · Oncogenesis · doi:10.1038/s41389-026-00630-4 · Cited by 9
Molecular characterization and functional analysis of two phospholipid hydroperoxide isoforms from Larimichthys crocea under Vibrio parahaemolyticus challenge
Xie, X., Chen, M., & Zhu, A. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.04.052 · Cited by 7
Protein-free domains in native and ferroptosis-driven oxidized cell membranes: a molecular dynamics study of biophysical properties and doxorubicin uptake
Shabanpour, Y., Verdom, B. H., Abdolmaleki, P., & Alipour, M. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1494257 · Cited by 7
Radish phospholipid hydroperoxide glutathione peroxidase provides protection against hydroperoxide-mediated injury in mouse 3T3 fibroblasts
Li, T., Liu, G.-L., Duan, M., & Liu, J. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.10.648 · Cited by 7
Short synthesis of hydroxylated thiolane and selenolane rings from mono-benzylated pentitols and aldoses dithioacetals bis-thionocarbonates as bis-electrophilic substrates
Danquigny, A., Meziane, M. A. A., Demailly, G., & Benazza, M. (2005) · Tetrahedron · doi:10.1016/j.tet.2005.05.008 · Cited by 7
The Peroxidase and Cyclooxygenase Activity of Prostaglandin H Synthase
Kudalkar, S. N., Rouzer, C. A., & Marnett, L. J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622628-00245 · Cited by 7
Purification and characterization of two glutathione peroxidases from embryo of the camel tick Hyalomma dromedarii
Ibrahim, M. A.-A., Mohamed, M. M., Ghazy, A.-H. M., El-Mogy, M. M., & Masoud, H. M. M. (2016) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162016030092 · Cited by 7
Reactive oxygen species and their influence on stallion semen fertility - a review
Pagl, R., Aurich, J., & Aurich, C. (2006) · Pferdeheilkunde Equine Medicine · doi:10.21836/pem20060217 · Cited by 9
Identification of two putative phospholipid hydroperoxide glutathione peroxidase genes and the induction of three environmental stresses in Neoseiulus barkeri (Acari: Phytoseiidae)
Tian, C. B., Zhang, G. H., Li, Y. Y., & Liu, H. (2017) · Journal of Asia-Pacific Entomology · doi:10.1016/j.aspen.2017.01.010 · Cited by 7
Control of Redox Homeostasis in Tick Blood Feeding
Sabadin, G. A., Xavier, M. A., & Vaz, I. D. S. (2019) · ACTA SCIENTIAE VETERINARIAE · doi:10.22456/1679-9216.94819 · Cited by 8
PHGPx overexpression induces an increase in COX-2 activity in colon carcinoma cells.
Barrière, G., Rabinovitch-Chable, H., Cook‐Moreau, J., Faucher, K., Rigaud, M., & Sturtz, F. G. (2004) · PubMed · Cited by 7
Acute endotoxemia during gestation induces organ dysfunction and tissue damage in mouse offspring.
Ebaid, H., Ajarem, J. S., & Abu-Taweel, G. M. (2012) · Pakistan Journal of Zoology · Cited by 7
Toxic levels of selenium in enzymes and selenium uptake in tissues of a marine fish
Tallandini, L., Cecchi, R., Boni, S. D., Galassini, S., Ghermandi, G., Gialanella, G., Liu, N., Moro, R., Turchetto, M., & Zhang, Y. (1996) · Biological Trace Element Research · doi:10.1007/bf02790152 · Cited by 7
EFFECT OF POSTMORTEM AGE OF FLOUNDER SARCOPLASMIC RETICULUM ON INHIBITION OF ENZYMIC LIPID PEROXIDATION BY CYTOSOL
Borhan, M., Hultin, H. O., & Rasco, B. (1990) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.1990.tb00843.x · Cited by 7
Development of the cytosolic defence system against microsomal lipid peroxidation in rat liver
Fairhurst, S., Barber, D. J., Clark, B., & Horton, A. A. (1983) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(83)90281-3 · Cited by 7
Purification of phospholipid hydroperoxide glutathione peroxidase from bovine retina
Lam, K., Wang, L., Hong, B., & Treble, D. (1993) · Current Eye Research · doi:10.3109/02713689308999490 · Cited by 7
New perspective for pathomechanism and clinical applications of animal toxins: Programmed cell death
Sun, J., Liu, J., Liu, M., Bi, X., & Huang, C. (2024) · Toxicon · doi:10.1016/j.toxicon.2024.108071 · Cited by 6
GSTO2 ameliorates human neuroblastoma cell apoptosis, inflammation, ferroptosis, and oxidative stress by upregulating GPX4 expression in intracerebral hemorrhage
Liu, C., Tian, W., & Lei, D. (2024) · Drug Development Research · doi:10.1002/ddr.22245 · Cited by 6
Targeting ferroptosis in the neurovascular unit: A promising approach for treating diabetic cognitive impairment
Zhang, W., Yan, Y., Yi, C., Jiang, X., Guo, L., Huang, S., Xia, T., Huang, F., Jiao, Y., Li, H., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113146 · Cited by 6
Jun modulates endoplasmic reticulum stress-associated ferroptosis in dorsal root ganglia neurons during neuropathic pain by regulating Timp1
Lin, Z., Wang, Y., Deng, Y., Lü, L., Cao, Y. Q., Wang, S., Zhang, X., Ding, G., Cheng, J., Tang, S., et al. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105877 · Cited by 6
U2AF65 mediated circPVT1 promotes NSCLC cell proliferation and inhibits ferroptosis through the miR-338-3p/GPX4 axis
He, L., Zhou, Z., Wang, J., Jiang, J., & Liu, S. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10028-4 · Cited by 6
The intersection of mitochondria, lipids, and ferroptosis: a new avenue for dry age-related macular degeneration
Dohl, J., Burns, G., & Singh, M. K. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02165-2 · Cited by 7
Metabolic cell deaths in head and neck cancer: mechanisms, therapeutic potential, and challenges
Wang, T., Li, X., Huang, X., Wang, Z., Zhang, Y., Lei, J., Qian, X., Lu, C., & Liu, Z. (2025) · Annals of Medicine · doi:10.1080/07853890.2025.2582906 · Cited by 7
Loss of NLN suppresses lung cancer progression by inducing ferroptosis through downregulating m6A methylation of GPX4
Liu, L., Ni, Y., Yang, Y., Zhang, G., Mao, S., Chao, N., Yao, M., Wang, C., & Zhang, L. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103928 · Cited by 6
Ferroptosis: a novel pathogenesis and therapeutic strategies for Parkinson disease: A review
Jiao, D., Yang, Y., Wang, K., & Wang, Y. (2025) · Medicine · doi:10.1097/md.0000000000041218 · Cited by 8
Supression thioredoxin reductase 3 exacerbates the progression of liver cirrhosis via activation of ferroptosis pathway.
Liu, Q., Xu, L.-M., Ren, G., Zhao, J.-Z., Shao, Y., & Lu, T.-Y. (2023) · Life Science · doi:10.1016/j.lfs.2023.121591 · Cited by 6
Effects of diphenyl diselenide and diphenyl ditellurite on chicken embryo development
Prauchner, C. A., Prestes, A. D. S., Nogueira, C. W., & da Rocha, J. B. T. (2013) · Toxicology Mechanisms and Methods · doi:10.3109/15376516.2013.834015 · Cited by 6
Rat, caprine, equine and bovine erythrocyte ghosts exposed to t-butyl hydroperoxide as a model to study lipid peroxidation using a chemiluminescence assay
Iglesias, B. F., & Catalá, Á. (2004) · Research in Veterinary Science · doi:10.1016/j.rvsc.2004.10.004 · Cited by 6
The reference genome of the selfing fish Kryptolebias hermaphroditus: Identification of phases I and II detoxification genes
Choi, B., Park, J. C., Kim, M., Han, J., Kim, D., Hagiwara, A., Sakakura, Y., Hwang, U.-K., Lee, B., & Lee, J. (2020) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2020.100684 · Cited by 5
Wound Healing Potential of Intermittent Negative Pressure under Limited Access Dressing in Burn Patients: Biochemical and Histopathological Study.
Honnegowda, T. M., Kumar, P., & Govindarama, P. U. E. (2018) · Europe PMC (PubMed Central) · Cited by 6
Molecular characterization of glutathione peroxidase gene from the liver of silver carp, bighead carp and grass carp
Li, G., Liang, X., Yao, W., Liao, W., & Zhu, W. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.3.204 · Cited by 6
PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE
Maiorino, M., Roveri, A., & Ursini, F. (1988) · Phosphorous and Sulfur and the Related Elements · doi:10.1080/03086648808079699 · Cited by 6
Lipid peroxidation: a novel enzymatic mechanism of protective effect of α-tocopherol in biological membranes
Dmitriev, L. F. (1995) · Redox Report · doi:10.1080/13510002.1995.11747001 · Cited by 6
Glucagon activation of the thiol:Protein disulfide oxidoreductase in isolated, rat, hepatic microsomes
McConkey, D. J., Crankshaw, D. L., & Holtzman, J. L. (1986) · Life Sciences · doi:10.1016/0024-3205(86)90213-4 · Cited by 6
Ferritin1-mediated ferroptosis participates in granular acini degeneration of Haemaphysalis longicornis salivary glands
Yuan, D., Chen, S., Zhou, Y., Cao, J., Zhang, H., Wang, Y., & Zhou, J. (2025) · Ticks and Tick-borne Diseases · doi:10.1016/j.ttbdis.2025.102464 · Cited by 5

Authors: Ursini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C.
Affiliations: University of Padua (IT)
ORCID: Ursini, F.
Maiorino, M.
Valente, M.
Gregolin, C.
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)
DOI: 10.1016/0005-2760(82)90150-3
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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

Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks