Jiang, X., Stockwell, B. R. & Conrad, M. Ferroptosis: mechanisms, biology and role in disease. Nat. Rev. Mol. Cell Biol. 22, 266–282 (2021).
Mao, C. et al. DHODH-mediated ferroptosis defence is a targetable vulnerability in cancer. Nature 593, 586–590 (2021).
Doll, S. et al. FSP1 is a glutathione-independent ferroptosis suppressor. Nature 575, 693–698 (2019).
Zhang, L. et al. Recent advances of human dihydroorotate dehydrogenase inhibitors for cancer therapy: current development and future perspectives. Eur. J. Med. Chem. 232, 114176 (2022).
Baumgartner, R. et al. Dual binding mode of a novel series of DHODH inhibitors. J. Med. Chem. 49, 1239–1247 (2006).
Mishima, E. et al. A non-canonical vitamin K cycle is a potent ferroptosis suppressor. Nature 608, 778–783 (2021).
Seiler, A. et al. Glutathione peroxidase 4 senses and translates oxidative stress into 12/15-lipoxygenase dependent- and AIF-mediated cell death. Cell Metab. 8, 237–248 (2008).
Wu, J. et al. Intercellular interaction dictates cancer cell ferroptosis via NF2-YAP signalling. Nature 572, 402–406 (2019).
Chen, Y. et al. Quantitative profiling of protein carbonylations in ferroptosis by an aniline-derived probe. J. Am. Chem. Soc. 140, 4712–4720 (2018).
Moreno, S. G., Laux, G., Brielmeier, M., Bornkamm, G. W. & Conrad, M Testis-specific expression of the nuclear form of phospholipid hydroperoxide glutathione peroxidase (PHGPx). Biol. Chem. 384, 635–643 (2005).
Schneider, M. et al. Embryonic expression profile of phospholipid hydroperoxide glutathione peroxidase. Gene Expr. Patterns 6, 489–494 (2006).
Liang, H. et al. Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions. J. Biol. Chem. 284, 30836–30844 (2009).
Conrad, M. et al. The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. Mol. Cell. Biol. 25, 7637–7644 (2005).
Schneider, M. et al. Mitochondrial glutathione peroxidase 4 disruption causes male infertility. FASEB J. 23, 3233–3242 (2009).
Wu, S. et al. A ferroptosis defense mechanism mediated by glycerol-3-phosphate dehydrogenase 2 in mitochondria. Proc. Natl Acad. Sci. USA 119, e2121987119 (2022).
Walse, B. et al. The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites. Biochemistry 47, 8929–8936 (2008).
Christian, S. et al. The novel dihydroorotate dehydrogenase (DHODH) inhibitor BAY 2402234 triggers differentiation and is effective in the treatment of myeloid malignancies. Leukemia 33, 2403–2415 (2019).
Varadi, M. et al. AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Res. 50, D439–D444 (2022).
Feng, Y. et al. Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature 491, 478–482 (2012).