The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors
Open accessAbstract
Key Points: Gpx4 is essential for preventing anemia in mice via inhibiting RIP3-dependent necroptosis in erythroid precursor cells. ROS accumulation and lipid peroxidation in erythroid precursor cells trigger receptor-independent activation of necroptosis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“GPx4 KO mice show impaired hematopoiesis without hemolysis (28), indicating that erythroid cells rather than adult RBCs are affected by deficient redox detoxification by GPx4.”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [28]
In the citing paper
“GPx4 KO mice show impaired hematopoiesis without hemolysis (28), indicating that erythroid cells rather than adult RBCs are affected by deficient redox detoxification by GPx4.”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [28]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732
Self-citationROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382
Self-citationAutophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis
Degenhardt, K., Mathew, R., Beaudoin, B., Bray, K., Anderson, D., Chen, G., Mukherjee, C., Shi, Y., Gélinas, C., Fan, Y., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.06.001 · Cited by 2,069
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
Cited by
Sorted by citations
Items 201–247 of 247
Andryszkiewicz, W., Cichowska, Z., Filipski, M., Szyda, K., Wietrzyk, A., Szpak, P., & Kulbacka, J. (2026) · Molecules · doi:10.3390/molecules31122072 · Cited by 5
Effects and mechanisms of Salmonella plasmid virulence gene spv on host-regulated cell death
Li, K., You, J., Li, Y., Huang, R., & Wu, S. (2024) · Current Microbiology · doi:10.1007/s00284-024-03612-0 · Cited by 6
Rademacher, M., Kühn, H., & Borchert, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157795 · Cited by 5
Regulation and Function of Autophagy During Ferroptosis
Tang, D., & Kang, R. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_3 · Cited by 5
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
Glutathione-driven redox decisions in cell survival and death
Zhang, R., Kang, R., & Tang, D. (2026) · Vita · doi:10.15302/vita.2026.06.0040 · Cited by 4
Increased ferroptosis of erythrocytes is associated with myelodysplastic syndromes
Zhang, M., Liu, M., Yang, L., Liu, Y., Niu, H., Yu, Y., Zhang, Y., Yang, J., Tang, P., Shao, Z., et al. (2024) · Annals of Hematology · doi:10.1007/s00277-024-05946-y · Cited by 4
Yang, R., Yu, D., Ren, J., Yin, J., Li, J. Y., Liu, X., & Lv, X. (2025) · The FASEB Journal · doi:10.1096/fj.202500228r · Cited by 4
Unconventional cell death in erythroid cells
Bruce, L. J., & Anstee, D. J. (2016) · Blood · doi:10.1182/blood-2015-11-677229 · Cited by 4
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
Ran, Q., & Mozolewska, P. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_6 · Cited by 4
Ferroptosis, free radicals, and cancer
Kang, R., & Tang, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819547-5.00014-6 · Cited by 4
Tang, D., & Kang, R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814208-0.00003-8 · Cited by 4
Antioxidant Nanozymes: From Rational Design to Biomedical Applications
Deng, Z., Zhang, R., Zhu, Y., Xu, C., Yang, M., Li, L., Cheng, Y., Shi, H., Dou, C., Zhang, M., et al. (2026) · Research · doi:10.34133/research.1318 · Cited by 3
Jarabicová, I., Horváth, C., Marciníková, A., & Adameová, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144280 · Cited by 4
Wu, X., Wang, Y., Chen, B., Liu, Y., Li, F., Ou, Y., Zhang, H., Wu, X., Li, X., Wang, L., et al. (2023) · Advanced Science · doi:10.1002/advs.202303555 · Cited by 3
El-Shaarawy, E. A. A., Ahmed, S. H., Nasrallah, M. M., Mousa, A. K., & Fattah, S. A. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155212 · Cited by 2
Aoyama, Y., Yamazaki, H., & Inoue, D. (2025) · Experimental Hematology · doi:10.1016/j.exphem.2025.105346 · Cited by 3
Hou, Q., Cheng, S., Li, Z., Lei, C., Chen, Y., Ma, M., Liu, J., Chen, X., Wang, L., Xue, Q., et al. (2025) · Journal of Virology · doi:10.1128/jvi.02310-24 · Cited by 2
Nanozyme-synbiotics to improve iron-deficiency anemia
Wu, A., Li, X., Kuang, Z., Gu, K., Luo, Y., Chen, D., & Wang, X. (2025) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2025.114960 · Cited by 2
Nazem, S., Mirzaei, A., Tavakoli‐Yaraki, M., Najafi, T., Salami, S., Bashash, D., & Shahsavari, Z. (2022) · Gene Reports · doi:10.1016/j.genrep.2022.101506 · Cited by 2
Ferroptosis Is a Potential Therapeutic Target for Pulmonary Infectious Diseases
Zhang, Y., Qian, D., Bai, X., & Sun, S. (2023) · Cellular Microbiology · doi:10.1155/2023/3875897 · Cited by 2
Modulation of Antioxidant Enzyme Expression of In Vitro Culture-Derived Reticulocytes
Langlands, H. D., Shoemark, D. K., & Toye, A. M. (2024) · Antioxidants · doi:10.3390/antiox13091070 · Cited by 2
Redox Modulation of Erythropoiesis by Selenoproteins
Gong, H., Paulson, R. F., & Prabhu, K. S. (2025) · Biological Trace Element Research · doi:10.1007/s12011-025-04923-4 · Cited by 1
Evaluation of urine glutathione peroxidase 4 in cats with chronic kidney disease
Hsu, W.-L., Huang, S.-H., Hseu, Z.-Y., Wu, V., Chen, Y., & Lee, Y.-J. (2026) · Frontiers in Veterinary Science · doi:10.3389/fvets.2025.1756038 · Cited by 1
Xie, Z., Wang, H., You, B., Li, M., Li, D., & Wu, H. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1753386 · Cited by 1
The Protective Effect of Vitamin D Against Necroptosis in Preeclampsia
Putri, A. S., Irwinda, R., & Wibowo, N. (2026) · Journal of Pregnancy · doi:10.1155/jp/4106792 · Cited by 1
Mohan, K., Ntambi, J. M., & Moussaieff, A. (2026) · Journal of Lipid Research · doi:10.1016/j.jlr.2026.101036 · Cited by 2
Ten controversies defining the boundaries of ferroptosis
Tang, D., & Kang, R. (2026) · Element · doi:10.20517/element.2026.07 · Cited by 1
Liu, M., Cao, X., Li, S., Guo, Y., Li, X., & Li, J. (2026) · Environmental Pollution · doi:10.1016/j.envpol.2026.129001 · Cited by 1
Matei, E., Enciu, M., Roșu, M. C., Voinea, F., Mitroi, A. F., Deacu, M., Bălţătescu, G. I., Nicolau, A.-A., Chisoi, A., Aşchie, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179329 · Cited by 1
Liao, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814208-0.00005-1 · Cited by 1
BIOCHEMICAL MECHANISMS OF FERROPTOSIS
Nikolaev, A. A. (2023) · Molekulyarnaya Meditsina (Molecular medicine) · doi:10.29296/24999490-2023-02-03 · Cited by 1
Subba, B., Toufiq, M., Omi, F., Yurieva, M., Khan, T., Rinchai, D., Palucka, K., & Chaussabel, D. (2024) · Research Square · doi:10.21203/rs.3.rs-4397623/v1 · Cited by 1
Mohammed, S., Nicklas, E. H., Thadathil, N., Selvarani, R., Royce, G. H., Richardson, A. G., & Deepa, S. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.17.254888
Chen, H.-Y., Goldman, A. R., Zayas-Bazan, D., Reyes-Uribe, P., Guterres, A. N., Lipchick, B. C., Basu, S., Yin, X.-F., Axelrod, M., Lu, Y.-L., et al. (2021) · bioRxiv · doi:10.1101/2021.04.07.438684
Hereditary anemias: more complex than ever
van Vuren, A. J. (2022) · Utrecht University Repository (Utrecht University) · doi:10.33540/429
Mai, L. T., Swaminathan, S., Nguyen, T. H., Charpentier, T., Loucif, H., Carmona‐Pérez, L., Lamarre, A., Heinonen, K. M., Fritz, J. H., & Stäger, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.29.577789
Identification and validation of oxidative stress-related genes in patients with atrial fibrillationPreprint
Dong, S., Yan, A., Zhang, J., & Ning, B. (2024) · Research Square · doi:10.21203/rs.3.rs-4505292/v1
Allen, R. D., Farzand, R., Chandrasekharan, G., Watkins, K. E., Agarwal, P., & Unnikrishnan, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.30.685513
Wu, Y., Chen, D., Li, J., Shen, K., Zhou, S., He, L., Qin, Y., He, J., & 修明慧 (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121229
RNA‐Binding Proteins and Ferroptosis in Cancer: Mechanism and Therapeutic Implications
Chang, L., Lu, B., Shang, H., Ding, W., Wei, C., Qi, X., & He, P. (2026) · MedComm – Oncology · doi:10.1002/mog2.70053
Rôle de l'histone désacétylase HDAC6 au cours de l'érythropoïèse humaine
Vong, P. (2022) · theses.fr (ABES) · doi:10.70675/699e8d9bz5404z43f6zabe7zdd0f0b6c8c42
Characterising the role of alpha synuclein in Ferroptosis, in the context of Parkinson's Disease
Mahoney‐Sanchez, L. (2022) · theses.fr (ABES) · doi:10.70675/a7f080d0z9ffaz4e1ez9550z0e29c4958e66
Du, G., Yuan, Q., Liu, R., Liang, J., Yang, M., Gao, Y., Liu, X., Lin, S., Zhang, R., Wang, B., et al. (2026) · Journal of Environmental Sciences · doi:10.1016/j.jes.2026.05.025
Zheng, Y., Yin, S., Zou, Y., Zhang, Z., Li, J., Chen, J., Zheng, W., Liu, Y., Zhang, Y., Yin, P., et al. (2026) · Materials Today Bio · doi:10.1016/j.mtbio.2026.103403
Jang, S., Kim, S., Kim, G., Hong, J., Park, I., & Jin, H. (2026) · Pharmacology Research & Perspectives · doi:10.1002/prp2.70330
Metadata
- Authors
- Canli, Ö., Alankuş, Y. B., Grootjans, S., Vegi, N., Hültner, L., Hoppe, P. S., Schroeder, T., Vandenabeele, P., Bornkamm, G. W., & Greten, F. R.
- Affiliations
- Georg Speyer Haus (DE)
- TUM Klinikum (DE)
- Ghent University (BE)
- Institute of Experimental Cancer Research, Comprehensive Cancer Center and University Hospital Ulm, Ulm, Germany;
- Helmholtz Munich (DE)
- ETH Zurich (CH)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2016-01-07
- Volume
- 127
- Issue
- 1
- Pages
- 139-148
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC4705604
- OpenAlex
- W2285203836
- Cited by
- 247
- References
- 53
- Citations by year
- 2026: 15 · 2025: 18 · 2024: 29 · 2023: 35 · 2022: 35 · 2021: 37 · 2020: 21 · 2019: 21 · 2018: 8 · 2017: 10 · 2016: 18
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Keywords
- GPX4, necroptosis, erythroid precursors, RIPK3, caspase-8, glutathionylation, oxidative stress, reactive oxygen species, lipid peroxidation, lipid hydroperoxides, reticulocyte maturation, anemia, hematopoietic cells, redox homeostasis
- MeSH terms
- Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Cell Differentiation, Cells, Cultured, Flow Cytometry, Glutathione Peroxidase, Humans, Immunoenzyme Techniques, Necrosis, Blotting, Western, Apoptosis, Reactive Oxygen Species, Mice, Knockout, Oxidative Stress, Erythroid Cells, Cell Proliferation, Mice, Receptor-Interacting Protein Serine-Threonine Kinases
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
