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@ARTICLE{Ingold:139754,
      author       = {Ingold, Irina and Berndt, Carsten and Schmitt, Sabine and
                      Doll, Sebastian and Poschmann, Gereon and Buday, Katalin and
                      Roveri, Antonella and Peng, Xiaoxiao and Porto Freitas,
                      Florencio and Seibt, Tobias and Mehr, Lisa and Aichler,
                      Michaela and Walch, Axel and Lamp, Daniel and Jastroch,
                      Martin and Miyamoto, Sayuri and Wurst, Wolfgang and Ursini,
                      Fulvio and Arnér, Elias S J and Fradejas-Villar, Noelia and
                      Schweizer, Ulrich and Zischka, Hans and Friedmann Angeli,
                      José Pedro and Conrad, Marcus},
      title        = {{S}elenium {U}tilization by {GPX}4 {I}s {R}equired to
                      {P}revent {H}ydroperoxide-{I}nduced {F}erroptosis.},
      journal      = {Cell},
      volume       = {172},
      number       = {3},
      issn         = {0092-8674},
      address      = {New York, NY},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-06076},
      pages        = {409-422.e21},
      year         = {2018},
      abstract     = {Selenoproteins are rare proteins among all kingdoms of life
                      containing the 21st amino acid, selenocysteine.
                      Selenocysteine resembles cysteine, differing only by the
                      substitution of selenium for sulfur. Yet the actual
                      advantage of selenolate- versus thiolate-based catalysis has
                      remained enigmatic, as most of the known selenoproteins also
                      exist as cysteine-containing homologs. Here, we demonstrate
                      that selenolate-based catalysis of the essential mammalian
                      selenoprotein GPX4 is unexpectedly dispensable for normal
                      embryogenesis. Yet the survival of a specific type of
                      interneurons emerges to exclusively depend on
                      selenocysteine-containing GPX4, thereby preventing fatal
                      epileptic seizures. Mechanistically, selenocysteine
                      utilization by GPX4 confers exquisite resistance to
                      irreversible overoxidation as cells expressing a cysteine
                      variant are highly sensitive toward peroxide-induced
                      ferroptosis. Remarkably, concomitant deletion of all
                      selenoproteins in Gpx4cys/cys cells revealed that
                      selenoproteins are dispensable for cell viability provided
                      partial GPX4 activity is retained. Conclusively, 200 years
                      after its discovery, a specific and indispensable role for
                      selenium is provided.},
      keywords     = {Animals / Apoptosis / Cell Survival / Cells, Cultured /
                      Female / Glutathione Peroxidase: genetics / Glutathione
                      Peroxidase: metabolism / HEK293 Cells / Humans / Hydrogen
                      Peroxide: toxicity / Interneurons: metabolism / Lipid
                      Peroxidation / Male / Mice / Mice, Inbred C57BL /
                      Phospholipid Hydroperoxide Glutathione Peroxidase /
                      Seizures: etiology / Seizures: metabolism / Selenium:
                      metabolism / Hydrogen Peroxide (NLM Chemicals) /
                      Phospholipid Hydroperoxide Glutathione Peroxidase (NLM
                      Chemicals) / Glutathione Peroxidase (NLM Chemicals) /
                      glutathione peroxidase 4, mouse (NLM Chemicals) / Selenium
                      (NLM Chemicals)},
      cin          = {AG Wurst},
      ddc          = {610},
      cid          = {I:(DE-2719)1140001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29290465},
      doi          = {10.1016/j.cell.2017.11.048},
      url          = {https://pub.dzne.de/record/139754},
}