The DOI matches its Crossref record; 67 of the 69 references it cites were found in a registry or an index.
Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability
Open accessPublished version of a preprint
Abstract
The selenoprotein glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid peroxides into nontoxic lipid alcohols. GPX4 has emerged as a promising therapeutic target for cancer treatment, but some cancer cells are resistant to ferroptosis triggered by GPX4 inhibition. Using a chemical-genetic screen, we identify LRP8 (also known as ApoER2) as a ferroptosis resistance factor that is upregulated in cancer. Loss of LRP8 decreases cellular selenium levels and the expression of a subset of selenoproteins. Counter to the canonical hierarchical selenoprotein regulatory program, GPX4 levels are strongly reduced due to impaired translation. Mechanistically, low selenium levels result in ribosome stalling at the inefficiently decoded GPX4 selenocysteine UGA codon, leading to ribosome collisions, early translation termination and proteasomal clearance of the N-terminal GPX4 fragment. These findings reveal rewiring of the selenoprotein hierarchy in cancer cells and identify ribosome stalling and collisions during GPX4 translation as ferroptosis vulnerabilities in cancer.
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?
The cited source says what the claim attributes to it.
In the citing paper
“LRP8 has been recently shown to affect ferroptosis by regulating the level of selenoprotein GPX4 in cancer cells (54–56).”
From Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis (2024) · cites this paper as [54]
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
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106
Cutadapt removes adapter sequences from high-throughput sequencing reads
Martin, M. (2011) · EMBnet.journal · doi:10.14806/ej.17.1.200 · Cited by 33,889
RSEM: accurate transcript quantification from RNA-Seq data with or without a reference genome
Li, B., & Dewey, C. N. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-323 · Cited by 22,179
Ultrafast and memory-efficient alignment of short DNA sequences to the human genome.
Langmead, B., Trapnell, C., Pop, M., & Salzberg, S. L. (2009) · Genome Biology · doi:10.1186/gb-2009-10-3-r25 · Cited by 21,849
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
Self-citationFerroptosis: mechanisms, biology and role in disease
Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,973
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
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
Self-citationGenome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
Self-citationThe CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis
Bersuker, K., Hendricks, J. M., Li, Z., Magtanong, L., Ford, B., Tang, P. H., Roberts, M. A., Tong, B., Maimone, T. J., Zoncu, R., et al. (2019) · Nature · doi:10.1038/s41586-019-1705-2 · Cited by 3,703
Self-citation
Cited by
Sorted by citations
The Cell Biology of Ferroptosis
Dixon, S. J., & Olzmann, J. A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00703-5 · Cited by 1,596
Self-citationGPX4 in cell death, autophagy, and disease
Xie, Y., Kang, R., Klionsky, D. J., & Tang, D. (2023) · Autophagy · doi:10.1080/15548627.2023.2218764 · Cited by 682
Regulation of ferroptosis by lipid metabolism
Pope, L. E., & Dixon, S. J. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.05.003 · Cited by 615
Self-citationRibosome biogenesis in disease: new players and therapeutic targets
Jiao, L., Liu, Y., Yu, X., Pan, X., Zhang, Y., Tu, J., Song, Y., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01285-4 · Cited by 336
A guideline on the molecular ecosystem regulating ferroptosis
Dai, E., Chen, X., Linkermann, A., Jiang, X., Kang, R., Kagan, V. E., Bayır, H., Yang, W. S., García‐Sáez, A. J., Ioannou, M. S., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01360-8 · Cited by 327
Ferroptosis: when metabolism meets cell death
Zheng, J., & Conrad, M. (2024) · Physiological Reviews · doi:10.1152/physrev.00031.2024 · Cited by 286
Metabolic cell death in cancer: ferroptosis, cuproptosis, disulfidptosis, and beyond
Mao, C., Wang, M., Zhuang, L., & Gan, B. (2024) · Protein & Cell · doi:10.1093/procel/pwae003 · Cited by 237
Chen, X., Tsvetkov, A. S., Shen, H., Isidoro, C., Ktistakis, N. T., Linkermann, A., Koopman, W. J. H., Simon, H., Galluzzi, L., Luo, S., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2319901 · Cited by 240
Ferroptosis: A flexible constellation of related biochemical mechanisms
Dixon, S. J., & Pratt, D. A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.03.005 · Cited by 219
Self-citationAhola, S., Rivera-Mejías, P., Hermans, S., Chandragiri, S., Giavalisco, P., Nolte, H., & Langer, T. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.08.017 · Cited by 193
Recommendations for robust and reproducible research on ferroptosis
Mishima, E., Nakamura, T., Doll, S. G., Proneth, B., Fedorova, M., Pratt, D. A., Angeli, J. P. F., Dixon, S. J., Wahida, A., & Conrad, M. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00843-2 · Cited by 211
Self-citationExploiting ferroptosis vulnerabilities in cancer
Nakamura, T., & Conrad, M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01425-8 · Cited by 172
Ferroptosis: mechanisms and implications for cancer development and therapy response
dos Santos, A. F., Fazeli, G., da Silva, T. N. X., & Angeli, J. P. F. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.04.005 · Cited by 154
Human hematopoietic stem cell vulnerability to ferroptosis
Zhao, J., Jia, Y., Mahmut, D., Deik, A., Jeanfavre, S., Clish, C. B., & Sankaran, V. G. (2023) · Cell · doi:10.1016/j.cell.2023.01.020 · Cited by 147
Identification of structurally diverse FSP1 inhibitors that sensitize cancer cells to ferroptosis
Hendricks, J. M., Doubravsky, C. E., Wehri, E., Li, Z., Roberts, M. A., Deol, K. K., Lange, M., Lasheras-Otero, I., Momper, J. D., Dixon, S. J., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.04.007 · Cited by 129
Self-citationFerroptosis in mitochondrial cardiomyopathy
Ahola, S., & Langer, T. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.06.002 · Cited by 118
Koeberle, S. C., Kipp, A. P., Stuppner, H., & Koeberle, A. (2023) · Medicinal Research Reviews · doi:10.1002/med.21933 · Cited by 117
Selenoprotein P – Selenium transport protein, enzyme and biomarker of selenium status
Schomburg, L. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.08.022 · Cited by 110
PRDX6 dictates ferroptosis sensitivity by directing cellular selenium utilization
Ito, J., Nakamura, T., Toyama, T., Chen, D., Berndt, C., Poschmann, G., Mourão, A., Doll, S. G., Suzuki, M., Zhang, W., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.10.028 · Cited by 100
PRDX6 contributes to selenocysteine metabolism and ferroptosis resistance
Chen, Z., Inague, A., Kaushal, K., Fazeli, G., Schilling, D., da Silva, T. N. X., dos Santos, A. F., Cheytan, T., Freitas, F. P., Yildiz, U., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.10.027 · Cited by 88
Targeting ferroptosis: Paving new roads for drug design and discovery
Gu, Y., Li, Y., Wang, J., Zhang, L., Zhang, J., & Wang, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.115015 · Cited by 88
LRP8‐mediated selenocysteine uptake is a targetable vulnerability in MYCN‐amplified neuroblastoma
Alborzinia, H., Chen, Z., Yildiz, U., Freitas, F. P., Vogel, F. C. E., Varga, J. P., Batani, J., Bartenhagen, C., Schmitz, W., Büchel, G., et al. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202318014 · Cited by 85
Parallel CRISPR-Cas9 screens identify mechanisms of PLIN2 and lipid droplet regulation
Roberts, M. A., Deol, K. K., Mathiowetz, A. J., Lange, M., Leto, D. E., Stevenson, J., Hashemi, S. H., Morgens, D. W., Easter, E., Heydari, K., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.07.001 · Cited by 81
Self-citationXiang, W., Zhang, T., Li, B., Li, S., Zhang, B., Fang, S., Chen, L., Gong, Y., Huang, B., Feng, D., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00907-0 · Cited by 82
Jia, C., Xiang, Z., Zhang, P., Liu, L., Zhu, X., Yu, R., Liu, Z., Wang, S., Liu, K., Wang, Z., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05067-1 · Cited by 71
Metabolism of Selenium, Selenocysteine, and Selenoproteins in Ferroptosis in Solid Tumor Cancers
Shimada, B. K., Swanson, S. M., Toh, P., & Seale, L. A. (2022) · Biomolecules · doi:10.3390/biom12111581 · Cited by 67
Zhang, H., Hu, B., Ye, Z.-P., Li, Z., Liu, S., Zhong, W.-Q., Du, T., Yang, D., Mai, J., Li, L., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adk0330 · Cited by 71
Self-citationProspects for ferroptosis therapies in cancer
Ubellacker, J. M., & Dixon, S. J. (2025) · Nature Cancer · doi:10.1038/s43018-025-01037-7 · Cited by 80
Self-citationMechanisms of ferroptosis sensitization and resistance
Lee, W. C., & Dixon, S. J. (2025) · Developmental Cell · doi:10.1016/j.devcel.2025.02.004 · Cited by 61
Self-citationLipid Quality Control and Ferroptosis: From Concept to Mechanism
Li, Z., Lange, M., Dixon, S. J., & Olzmann, J. A. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052521-033527 · Cited by 68
Self-citationGlycosaminoglycan-driven lipoprotein uptake protects tumours from ferroptosis
Calhoon, D., Sang, L., Ji, F., Bezwada, D., Hsu, S., Cai, F., Kim, N., Basu, A., Wu, R., Pimentel, A., et al. (2025) · Nature · doi:10.1038/s41586-025-09162-0 · Cited by 64
Selenoproteins and tRNA-Sec: regulators of cancer redox homeostasis
DeAngelo, S. L., Győrffy, B., Koutmos, M., & Shah, Y. M. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.08.003 · Cited by 50
Role of ferroptosis in pregnancy related diseases and its therapeutic potential
Xu, J., Zhou, F., Wang, X., & Mo, C. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1083838 · Cited by 45
Peroxiredoxin 6 suppresses ferroptosis in lung endothelial cells
Torres-Velarde, J. M., Allen, K. N., Salvador‐Pascual, A., Leija, R. G., Luong, D., Moreno-Santillán, D. D., Ensminger, D. C., & Vázquez‐Medina, J. P. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.04.208 · Cited by 44
Epigenetic Regulation of Ferroptosis in Central Nervous System Diseases
Lan, T., Sun, T., Wei, C., Cheng, T., Yang, F., Zhang, J.-N., & Li, Q. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03267-1 · Cited by 35
Redox regulation of the NLRP3-mediated inflammation and pyroptosis
Rusetskaya, N. Y., Loginova, N. Y., Pokrovskaya, E. P., Chesovskikh, Y. S., & Titova, L. E. (2023) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20236906333 · Cited by 34
A guide to ferroptosis in cancer
Yapici, F. I., Bebber, C. M., & von Karstedt, S. (2024) · Molecular Oncology · doi:10.1002/1878-0261.13649 · Cited by 35
Organic Selenium induces ferroptosis in pancreatic cancer cells
Noè, R., Inglese, N., Romani, P., Serafini, T., Paoli, C., Calciolari, B., Fantuz, M., Zamborlin, A., Surdo, N. C., Spada, V., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102962 · Cited by 30
Hijacking Extracellular Targeted Protein Degrader–Drug Conjugates for Enhanced Drug Delivery
Zhao, F., Wu, Y., Schaefer, K., Zhang, Y., Miao, K., Yao, Z. W., Ganjave, S. D., Kumru, K. S., Peters-Clarke, T. M., Inague, A., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c15047 · Cited by 32
Self-citationNatural Flavonoids and Ferroptosis: Potential Therapeutic Opportunities for Human Diseases
Zhou, Z., Li, J., & Zhang, X. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c08128 · Cited by 27
Reprogramming of iron metabolism confers ferroptosis resistance in ECM-detached cells
He, J., Abikoye, A. M., McLaughlin, B. P., Middleton, R. S., Sheldon, R. D., Jones, R. G., & Schafer, Z. T. (2023) · iScience · doi:10.1016/j.isci.2023.106827 · Cited by 25
Kobayashi, H., Yoshimoto, C., Matsubara, S., Shigetomi, H., & Imanaka, S. (2023) · Cancer Drug Resistance · doi:10.20517/cdr.2023.49 · Cited by 25
Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis
More, S., Bonnereau, J., Wouters, D., Spotbeen, X., Karras, P., Rizzollo, F., Killian, T., Venken, T., Naulaerts, S., Vervoort, E., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp6164 · Cited by 25
Decoding GPX4 regulation in ferroptosis: mechanisms and therapeutic implications
Chen, X. (2026) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2026.01.008 · Cited by 25
Santesmasses, D., & Gladyshev, V. N. (2022) · Biomolecules · doi:10.3390/biom12081049 · Cited by 25
A novel microtubule inhibitor promotes tumor ferroptosis by attenuating SLC7A11/GPX4 signaling
Ning, N., Shang, Z., Liu, Z., Xia, Z., Li, Y., Ren, R., Wang, H., & Zhang, Y. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01713-6 · Cited by 25
Selenocysteine tRNA methylation promotes oxidative stress resistance in melanoma metastasis
Nease, L. A., Church, K. P., Delclaux, I., Murakami, S., Astorkia, M., Zerhouni, M., Cascio, G., Hughes, R. O., Aguirre, K. N., Zumbo, P., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00844-8 · Cited by 25
Ren, M., Liang, S., Lin, S., Huang, R.-Z., Chen, Y., Zhang, Y., & Xü, Y. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107733 · Cited by 23
Metabolic adaptations in cancer progression
Peng‐Winkler, Y., & Fendt, S. (2025) · Physiological Reviews · doi:10.1152/physrev.00037.2024 · Cited by 25
Organic-inorganic covalent selenium reversing ischemic reperfusion injury
Xiong, Z., Huang, G., Huang, J., Liu, Y., He, L., & Chen, T. (2025) · Nature Communications · doi:10.1038/s41467-025-62986-2 · Cited by 24
Ferroptosis Signaling Pathways: Alzheimer's Disease
Maheshwari, S. (2023) · Hormone and Metabolic Research · doi:10.1055/a-2084-3561 · Cited by 23
Liu, B., Bukhari, I., Li, F., Ren, F., Xue, X., Hu, B., Liu, H., Meyer, T. F., Marshall, B. J., Tay, C. Y., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.04.002 · Cited by 24
High throughput drug screening identifies resveratrol as suppressor of hepatic SELENOP expression
Hackler, J., Demircan, K., Chillon, T. S., Sun, Q., Geisler, N., Schupp, M., Renko, K., & Schomburg, L. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102592 · Cited by 21
Dysregulated ribosome quality control in human diseases
McGirr, T., Onar, O., & Jafarnejad, S. M. (2024) · FEBS Journal · doi:10.1111/febs.17217 · Cited by 22
A new strategy for the treatment of intracerebral hemorrhage: Ferroptosis
Sun, K. Y., Bai, X. Y., Zhang, L., ZHANG, X. Y., Hu, Q., Song, Y., Qiang, R. R., Zhang, N., Zou, J. L., Yang, Y. L., et al. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114961 · Cited by 22
The crosstalk between ferroptosis and autophagy in cancer
Lv, X., Wang, B., Dong, M., Wang, W., Tang, W., Qin, J., Gao, Y., & Wei, Y. (2023) · Autoimmunity · doi:10.1080/08916934.2023.2289362 · Cited by 18
Dong, Y., Liang, W., & Yi, L. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c09215 · Cited by 19
Ferroptosis: biology and role in liver disease
Hino, K., Nishina, S., & Yanatori, I. (2025) · Journal of Gastroenterology · doi:10.1007/s00535-025-02300-5 · Cited by 21
Protocol for performing pooled CRISPR-Cas9 loss-of-function screens
Mathiowetz, A. J., Roberts, M. A., Morgens, D. W., Olzmann, J. A., & Li, Z. (2023) · STAR Protocols · doi:10.1016/j.xpro.2023.102201 · Cited by 19
Self-citationVarlamova, E. G. (2025) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2025.127620 · Cited by 20
Wang, J., Shi, H., Yang, Y. S., & Gong, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1505794 · Cited by 21
Molecular Highway Patrol for Ribosome Collisions
Iyer, K. V., Müller, M., Tittel, L. S., & Winz, M. (2023) · ChemBioChem · doi:10.1002/cbic.202300264 · Cited by 18
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
Translational response to mitochondrial stresses is orchestrated by tRNA modificationsPreprint
Rashad, S., Al-Mesitef, S., Mousa, A., Zhou, Y., Ando, D., Sun, G., Fukuuchi, T., Iwasaki, Y., Xiang, J., Byrne, S. R., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.14.580389 · Cited by 17
Lamperis, S. M., McMahon, K. M., Calvert, A. E., Rink, J. S., Vasan, K., Pandkar, M. R., Crentsil, E. U., Chalmers, Z. R., McDonald, N. R., Kosmala, C. J., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2502876122 · Cited by 15
Mechanisms and therapeutic potential of disulphidptosis in cancer
Li, Y., Zhang, H., Yang, F., Zhu, D., Chen, S., Wang, Z., Wei, Z., Yang, Z., Jia, J., Zhang, Y., et al. (2024) · Cell Proliferation · doi:10.1111/cpr.13752 · Cited by 15
Demircan, K., Bengtsson, Y., Chillon, T. S., Vallon‐Christersson, J., Sun, Q., Larsson, C., Malmberg, M., Saal, L. H., Rydén, L., Borg, Å., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04502-y · Cited by 13
MUC1-C is a target of salinomycin in inducing ferroptosis of cancer stem cells
Daimon, T., Bhattacharya, A., Wang, K., Haratake, N., Nakashoji, A., Ozawa, H., Morimoto, Y., Yamashita, N., Kosaka, T., Oya, M., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-023-01772-9 · Cited by 12
Co-targeting ferroptosis and immune evasion through small molecules in breast cancer
Zhou, J., Yang, W., Tang, H., Zou, Y., Zhou, Z., Peng, C., & Peng, F. (2025) · Journal of Translational Internal Medicine · doi:10.1515/jtim-2025-0093 · Cited by 11
Ferroptosis: A Frontier in Osteoporosis
Maheshwari, S., Singh, A., & Verma, A. (2024) · Hormone and Metabolic Research · doi:10.1055/a-2230-2664 · Cited by 11
Wang, T., Zhou, X., Yin, X., Zhang, A., Fan, Y., Chen, K., Tao, H., Tang, Z., Zhang, P., He, X., et al. (2025) · International Journal of Oncology · doi:10.3892/ijo.2025.5781 · Cited by 12
Bi, G., Liang, J., Bian, Y., Shan, G., Ren, S., Shi, H., Huang, X., Zhu, J., Wang, Q., Jiang, W., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63687-6 · Cited by 14
Wang, L., Liu, H., Liu, H., Li, X., Tang, T., Wang, K.-J., Wei, G.-R., Tian, J., Zhang, Y., & Luo, X. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123625 · Cited by 10
Dehdari, A., Poon, J., & Pratt, D. A. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c14856 · Cited by 9
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
Strategies for the Development of Donors and Precursors of Hydrogen Selenide (H2Se)
Hu, J., Liang, W., & Yi, L. (2025) · Chemistry - An Asian Journal · doi:10.1002/asia.202500842 · Cited by 9
Regulation of apoptosis, ferroptosis, and pyroptosis mediated by acetylation
Lu, W., Deng, Y., Liu, M., Hu, Y., Yang, K., Wang, B., Li, Y., wang, G., Ma, L., LIU, J., et al. (2026) · Cell Death Discovery · doi:10.1038/s41420-025-02859-1 · Cited by 9
Ferroptosis as an approach to leverage cancer metabolism
Jin, J., Hu, J., Li, M., Gu, W., Jiang, X., & Stockwell, B. R. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.03.008 · Cited by 8
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
Ni, F.-X., Chen, H., Ze-Bo, J., & Huang, D.-H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1630969 · Cited by 9
Ferroptosis in hematological malignancies: molecular mechanisms and therapeutic potential
Liu, J., Liu, R., Miao, J., & He, A. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01142-w · Cited by 7
Current Status and Future Directions of Ferroptosis Research in Breast Cancer: Bibliometric Analysis
Luo, J., Deng, Y.-L., Lu, S. M., Chen, S., He, R., Qin, D., Chi, B., Chen, G., Yang, X., & Peng, W. (2025) · Interactive Journal of Medical Research · doi:10.2196/66286 · Cited by 6
MITF Is Regulated by Redox Signals Controlled by the Selenoprotein Thioredoxin Reductase 1
Kline, C. D., Anderson, M., Bassett, J. W., Kent, G., Berryman, R., Honeggar, M., Ito, S., Wakamatsu, K., Indra, A. K., Moos, P. J., et al. (2022) · Cancers · doi:10.3390/cancers14205011 · Cited by 6
Ferguson, L., Upton, H. E., Pimentel, S. C., Jeans, C., Ingolia, N. T., & Collins, K. (2024) · RNA · doi:10.1261/rna.080318.124 · Cited by 5
Self-citationMartinelli, A. W., Wu, C.-P., Vornbäumen, T., Coates, H. W., Jordon, L., Wit, N., Sia, J. J., Speak, A. O., & Nathan, J. A. (2025) · Science Advances · doi:10.1126/sciadv.adw9095 · Cited by 5
Kang, H., Hoang, D. H., Valerio, M., Pathak, K. V., Graff, W., LeVee, A. A., Wu, J., LaBarge, M. A., Frankhouser, D. E., Rockne, R. C., et al. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01668-4 · Cited by 5
Chen, K., Zhong, C., Wang, Y., Liu, T., Chen, H., Wu, R., Qiu, G., Zheng, S., Gao, Y., Ping, Y., et al. (2025) · Cancer Cell International · doi:10.1186/s12935-025-04114-0 · Cited by 4
The intersection between metabolism and translation through a subcellular lens.
Santoro, M. M. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.05.003 · Cited by 6
Eutopic macrophages facilitate endometriosis progression via ferroptosis-mediated release of S100A9
Ye, C., Ma, P., Li, N., Zhang, R., Wang, J., Zhou, Z., Wu, J., Liu, D., Sun, J., Pan, W., et al. (2025) · Molecular Human Reproduction · doi:10.1093/molehr/gaaf027 · Cited by 4
Schweizer, U., & Fabiano, M. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104083 · Cited by 7
Learning chemical sensitivity reveals mechanisms of cellular response
Connell, W., Garcia, K., Goodarzi, H., & Keiser, M. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06865-4 · Cited by 4
The role of ferroptosis resistance in lymph-associated tumour metastasis
Li, X., Tian, M., Yu, L., Qian, J., Yang, J., Wang, X., Lu, C., Xiao, C., & Liu, Y. (2024) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2024.189200 · Cited by 4
Zhao, F., Wu, Y., Schaefer, K., Zhang, Y., Miao, K., Yao, Z. W., Ganjave, S. D., Kumru, K. S., Peters-Clarke, T. M., Inague, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.06.658366 · Cited by 4
Self-citationCai, Z., Zhang, Y., He, L., Cui, M., Zhang, W., Lingling, E., Yang, H., Ling, Q., Hoffmann, P. R., He, J., et al. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c12515 · Cited by 3
Gao, F., Yang, X., Zhu, X., Wu, Y., Liu, B., Zheng, W., Ding, S., Zheng, L., Hu, W., Yang, X., et al. (2026) · Poultry Science · doi:10.1016/j.psj.2026.106469 · Cited by 3
GPX4-dependent ferroptosis governs ILC2 homeostasis and colitis progression
Liu, G., Wang, Y., Huang, H., Wang, J., Yang, J., Wu, J., Cao, H., Zhang, Y., Jing, Y., Zhou, P., et al. (2026) · Cellular and Molecular Immunology · doi:10.1038/s41423-026-01388-w · Cited by 3
Fu, Y., Wang, Z., Wang, W., Xie, Y., Lin, C., Tan, L., & Liu, M. (2026) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2026.101148 · Cited by 3
Adding a Chemical Biology Twist to CRISPR Screening
Huang, S., & Baskin, J. M. (2022) · Israel Journal of Chemistry · doi:10.1002/ijch.202200056 · Cited by 3
Selenium Metabolic Pathway in Ferroptotic Cell Death
Kalishwaralal, K., Ajmani, A., Keerthana, C. K., Rayginia, T. P., Swetha, M., Aiswarya, S. U. D., Arivalagan, J., Bava, S. V., Firer, M. A., & Anto, R. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-39171-2_17 · Cited by 3
Bee Pollen Potential to Modulate Ferroptosis: Phytochemical Insights for Age-Related Diseases
Kacemi, R., & Campos, M. G. (2025) · Antioxidants · doi:10.3390/antiox14030265 · Cited by 3
Metadata
- Authors
- Li, Z., Ferguson, L., Deol, K. K., Roberts, M. A., Magtanong, L., Hendricks, J. M., Mousa, G. A., Kilinc, S., Schaefer, K., Wells, J. A., Bassik, M. C., Goga, A., Dixon, S. J., Ingolia, N. T., & Olzmann, J. A.
- Affiliations
- University of California, Berkeley (US)
- Stanford University (US)
- University of California, San Francisco (US)
- Chan Zuckerberg Biohub San Francisco (US)
- Corresponding author
- Olzmann, James A.
- ORCID
- Venue
- Nature Chemical Biology
- Published
- 2022-05-30
- Volume
- 18
- Issue
- 7
- Pages
- 751-761
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC9469796
- OpenAlex
- W4281664411
- Cited by
- 134
- References
- 69
- Citations by year
- 2026: 28 · 2025: 38 · 2024: 29 · 2023: 31 · 2022: 8
- FWCI
- 15.55
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Nature Chemical Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- American Cancer Society (RSG-19-192-01)
- Melanoma Research Alliance (620458)
- U.S. Department of Health & Human Services | National Institutes of Health (R01GM112948, T32GM007232, F31DK121477, 2T32CA108462, R01CA223817, 1R01GM122923)
- Chan Zuckerberg Biohub, Miller Institute
- United States Department of Defense | United States Army | Army Medical Command | Congressionally Directed Medical Research Programs (W81XWH-18-1-0713)
- Mark Foundation
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
- Keywords
- ribosome stalling, selenoprotein translation, GPX4, ferroptosis, ferroptosis resistance, LRP8, ApoER2, selenocysteine, UGA codon, selenium deficiency, cancer, chemical genetic screen, proteasomal degradation
- MeSH terms
- Ferroptosis, Phospholipid Hydroperoxide Glutathione Peroxidase, Ribosomes, Selenium, Selenoproteins
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