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-citationFSP1 is a glutathione-independent ferroptosis suppressor
Doll, S., Freitas, F. P., Shah, R., Aldrovandi, M., da Silva, M. C., Ingold, I., Goya Grocin, A., Xavier da Silva, T. N., Panzilius, E., Scheel, C. H., et al. (2019) · Nature · doi:10.1038/s41586-019-1707-0 · Cited by 3,341
Dixon, S. J., Patel, D. N., Welsch, M., Skouta, R., Lee, E. D., Hayano, M., Thomas, A. G., Gleason, C. E., Tatonetti, N. P., Slusher, B. S., et al. (2014) · eLife · doi:10.7554/elife.02523 · Cited by 2,088
Self-citationDHODH-mediated ferroptosis defence is a targetable vulnerability in cancer
Mao, C., Liu, X., Zhang, Y., Lei, G., Yan, Y., Lee, H., Koppula, P., Wu, S., Zhuang, L., Fang, B., et al. (2021) · Nature · doi:10.1038/s41586-021-03539-7 · Cited by 2,028
Dependency of a therapy-resistant state of cancer cells on a lipid peroxidase pathway
Viswanathan, V. S., Ryan, M. J., Dhruv, H. D., Gill, S., Eichhoff, O. M., Seashore-Ludlow, B., Kaffenberger, S. D., Eaton, J. K., Shimada, K., Aguirre, A. J., et al. (2017) · Nature · doi:10.1038/nature23007 · Cited by 2,011
Yang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876
Drug-tolerant persister cancer cells are vulnerable to GPX4 inhibition
Hangauer, M. J., Viswanathan, V. S., Ryan, M. J., Bole, D., Eaton, J. K., Matov, A., Galeas, J., Dhruv, H. D., Berens, M. E., Schreiber, S. L., et al. (2017) · Nature · doi:10.1038/nature24297 · Cited by 1,799
Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis
Ingold, I., Berndt, C., Schmitt, S., Doll, S. G., Poschmann, G., Buday, K., Roveri, A., Peng, X., Freitas, F. P., Seibt, T., et al. (2017) · Cell · doi:10.1016/j.cell.2017.11.048 · Cited by 1,712
Dolma, S., Lessnick, S. L., Hahn, W. C., & Stockwell, B. R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00050-3 · Cited by 1,446
GTP Cyclohydrolase 1/Tetrahydrobiopterin Counteract Ferroptosis through Lipid Remodeling
Kraft, V. A. N., Bezjian, C. T., Pfeiffer, S., Ringelstetter, L., Müller, C., Zandkarimi, F., Merl‐Pham, J., Bao, X., Anastasov, N., Kössl, J., et al. (2019) · ACS Central Science · doi:10.1021/acscentsci.9b01063 · Cited by 1,367
Intercellular interaction dictates cancer cell ferroptosis via NF2–YAP signalling
Wu, J., Minikes, A. M., Gao, M., Bian, H., Li, Y., Stockwell, B. R., Chen, Z.-N., & Jiang, X. (2019) · Nature · doi:10.1038/s41586-019-1426-6 · Cited by 1,110
Tsoi, J., Robert, L., Paraiso, K., Galvan, C., Sheu, K. M., Lay, J., Wong, D. J. L., Atefi, M., Shirazi, R., Wang, X., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.017 · Cited by 938
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916
Correlating chemical sensitivity and basal gene expression reveals mechanism of action
Rees, M. G., Seashore-Ludlow, B. A., Cheah, J. H., Adams, D., Price, E. V., Gill, S., Javaid, S., Coletti, M. E., Jones, V., Bodycombe, N. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1986 · Cited by 883
Basu, A. B., Bodycombe, N. E., Cheah, J. H., Price, E. V., Liu, K., Schaefer, G. I., Ebright, R. Y., Stewart, M. L., Ito, D., Wang, S. Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.003 · Cited by 828
Reelin Is a Ligand for Lipoprotein Receptors
D'Arcangelo, G., Homayouni, R., Keshvara, L., Rice, D. S., Sheldon, M., & Curran, T. (1999) · Neuron · doi:10.1016/s0896-6273(00)80860-0 · Cited by 808
Metabolic determinants of cancer cell sensitivity to canonical ferroptosis inducers
Soula, M., Weber, R. A., Zilka, O., Alwaseem, H., La, K., Yen, F. S., Molina, H., García‐Bermúdez, J., Pratt, D. A., & Birsoy, K. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0613-y · Cited by 774
Debnath, J., Mills, K. R., Collins, N. L., Reginato, M. J., Muthuswamy, S. K., & Brugge, J. S. (2002) · Cell · doi:10.1016/s0092-8674(02)01001-2 · Cited by 763
Regulation of Selenium Metabolism and Transport
Burk, R. F., & Hill, K. E. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034250 · Cited by 662
Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A. G., Williams, C. C., Li, G., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 650
Dixon, S. J., & Stockwell, B. R. (2018) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055844 · Cited by 607
Self-citationThe Hippo Pathway Effector TAZ Regulates Ferroptosis in Renal Cell Carcinoma
Yang, W., Ding, C. C., Sun, T., Rupprecht, G., Lin, C., Hsu, D. S., & Chi, J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.107 · Cited by 459
Mechanisms and functions of ribosome-associated protein quality control
Joazeiro, C. A. P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0118-2 · Cited by 456
Ribosome pausing and stacking during translation of a eukaryotic mRNA.
Wolin, S. L., & Walter, P. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03233.x · Cited by 454
Ribosome-associated protein quality control
Brandman, O., & Hegde, R. S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3147 · Cited by 445
ZNF598 Is a Quality Control Sensor of Collided Ribosomes
Juszkiewicz, S., Chandrasekaran, V., Lin, Z., Kraatz, S. H. W., Ramakrishnan, V., & Hegde, R. S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.037 · Cited by 427
Ribosome Footprint Profiling of Translation throughout the Genome
Ingolia, N. T. (2016) · Cell · doi:10.1016/j.cell.2016.02.066 · Cited by 424
Self-citationSystematic comparison of CRISPR/Cas9 and RNAi screens for essential genes
Morgens, D. W., Deans, R. M., Li, A., & Bassik, M. C. (2016) · Nature Biotechnology · doi:10.1038/nbt.3567 · Cited by 398
Self-citationHuman Apolipoprotein E Receptor 2
Kim, D.-H., Iijima, H., Goto, K., Sakai, J., Ishii, H., Kim, H.-J., Suzuki, H., Kondo, H., Saeki, S., & Yamamoto, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8373 · Cited by 384
Sundaramoorthy, E., Leonard, M., Mak, R., Liao, J., Fulzele, A., & Bennett, E. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.026 · Cited by 375
Genome-scale measurement of off-target activity using Cas9 toxicity in high-throughput screens
Morgens, D. W., Wainberg, M., Boyle, E. A., Ursu, O., Araya, C. L., Tsui, C. K., Haney, M. S., Hess, G. T., Han, K., Jeng, E. E., et al. (2017) · Nature Communications · doi:10.1038/ncomms15178 · Cited by 362
Self-citationJuszkiewicz, S., & Hegde, R. S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.11.039 · Cited by 331
Ribosome Collision Is Critical for Quality Control during No-Go Decay
Simms, C. L., Yan, L. L., & Zaher, H. S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.019 · Cited by 311
Olson, G. E., Winfrey, V. P., Nagdas, S. K., Hill, K. E., & Burk, R. F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611403200 · Cited by 246
Roadblocks and resolutions in eukaryotic translation
Schuller, A. P., & Green, R. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0011-4 · Cited by 245
The ASC-1 complex disassembles collided ribosomes
Juszkiewicz, S., Speldewinde, S. H., Wan, L., Svejstrup, J. Q., & Hegde, R. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.006 · Cited by 206
A genome-wide atlas of co-essential modules assigns function to uncharacterized genes
Wainberg, M., Kamber, R. A., Balsubramani, A., Meyers, R. M., Sinnott-Armstrong, N., Hornburg, D., Jiang, L., Chan, J., Jian, R., Gu, M., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00840-z · Cited by 204
Self-citationMegalin Mediates Selenoprotein P Uptake by Kidney Proximal Tubule Epithelial Cells
Olson, G. E., Winfrey, V. P., Hill, K. E., & Burk, R. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709945200 · Cited by 190
Takahashi, N., Cho, P., Selfors, L. M., Kuiken, H. J., Kaul, R., Fujiwara, T., Harris, I. S., Zhang, T., Gygi, S. P., & Brugge, J. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.010 · Cited by 187
Burk, R. F., Hill, K. E., Olson, G. E., Weeber, E. J., Motley, A. K., Winfrey, V. P., & Austin, L. M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1153-07.2007 · Cited by 184
Unger, C., Kramer, N., Walzl, A., Scherzer, M., Hengstschläger, M., & Dolznig, H. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.10.015 · Cited by 158
Misu, H., Takayama, H., Saito, Y., Mita, Y., Kikuchi, A., Ishii, K.-A., Chikamoto, K., Kanamori, T., Tajima, N., Lan, F., et al. (2017) · Nature Medicine · doi:10.1038/nm.4295 · Cited by 156
Chothani, S. P., Adami, E., Ouyang, J. F., Viswanathan, S., Hübner, N., Cook, S. A., Schäfer, S., & Rackham, O. J. L. (2019) · Current Protocols in Molecular Biology · doi:10.1002/cpmb.108 · Cited by 152
Selenium Transport Mechanism via Selenoprotein P—Its Physiological Role and Related Diseases
Saito, Y. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.685517 · Cited by 128
McCann, J. C., & Ames, B. N. (2011) · The FASEB Journal · doi:10.1096/fj.11-180885 · Cited by 125
Translational Redefinition of UGA Codons Is Regulated by Selenium Availability
Howard, M. T., Carlson, B. A., Anderson, C. B., & Hatfield, D. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.481051 · Cited by 108
Detecting and Rescuing Stalled Ribosomes
Yip, M. C. J., & Shao, S. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.03.008 · Cited by 94
The ApoE receptors Vldlr and Apoer2 in central nervous system function and disease
Lane-Donovan, C., & Herz, J. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075507 · Cited by 94
Leung, K. K., Wilson, G. M., Kirkemo, L. L., Riley, N. M., Coon, J. J., & Wells, J. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917947117 · Cited by 83
Self-citationBrandes, C., Kahr, L., Stockinger, W., Hiesberger, T., Schneider, W. J., & Nimpf, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102662200 · Cited by 78
Upton, H. E., Ferguson, L., Temoche-Diaz, M. M., Liu, X., Pimentel, S. C., Ingolia, N. T., Schekman, R. W., & Collins, K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107900118 · Cited by 69
Self-citationAkahoshi, N., Anan, Y., Hashimoto, Y., Tokoro, N., Mizuno, R., Hayashi, S., Yamamoto, S., Shimada, K., Kamata, S., & Ishii, I. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.03.020 · Cited by 58
Linking Tumor Mutations to Drug Responses via a Quantitative Chemical–Genetic Interaction Map
Martins, M. M., Zhou, A. Y., Corella, A. N., Horiuchi, D., Yau, C. S. F., Rakhshandehroo, T., Gordan, J. D., Levin, R. S., Johnson, J. R., Jascur, J., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0552 · Cited by 55
Self-citationKurokawa, S., Bellinger, F. P., Hill, K. E., Burk, R. F., & Berry, M. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.549014 · Cited by 53
FIREWORKS: a bottom-up approach to integrative coessentiality network analysis
Amici, D. R., Jackson, J. M., Truica, M. I., Smith, R. S., Abdulkadir, S. A., & Mendillo, M. L. (2020) · Life Science Alliance · doi:10.26508/lsa.202000882 · Cited by 47
Targeting LRP8 inhibits breast cancer stem cells in triple-negative breast cancer
Lin, C.-C. A., Lo, M., Moody, R., Jiang, H., Harouaka, R. A., Stevers, N. O., Tinsley, S. L., Gasparyan, M., Wicha, M. S., & Sun, D. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.09.022 · Cited by 46
LRP8 is overexpressed in estrogen‐negative breast cancers and a potential target for these tumors
Maire, V., Mahmood, F., Rigaill, G. J., Ye, M., Brisson, A., Némati, F., Gentien, D., Tucker, G. C., Roman‐Roman, S., & Dubois, T. (2018) · Cancer Medicine · doi:10.1002/cam4.1923 · Cited by 23
HIF-2α drives an intrinsic vulnerability to ferroptosis in clear cell renal cell carcinomaPreprint
Zou, Y., Palte, M. J., Deik, A., Li, H., Eaton, J. K., Wang, W., Tseng, Y., Deasy, R., Alimova, M., Dančík, V., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/388041 · Cited by 11
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
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