% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@INBOOK{Hatfield:144578,
      author       = {Conrad, Marcus},
      editor       = {Hatfield, Dolph L. and Berry, Marla J. and Gladyshev, Vadim
                      N.},
      title        = {{M}ouse {M}odels for {G}lutathione {P}eroxidase 4 ({GP}x4)},
      address      = {New York, NY},
      publisher    = {Springer New York},
      reportid     = {DZNE-2020-00090},
      pages        = {547-559},
      year         = {2012},
      comment      = {Selenium / Hatfield, Dolph L. (Editor) ; New York, NY :
                      Springer New York, 2012, Chapter 43 ; ISBN:
                      978-1-4614-1024-9 ; doi:10.1007/978-1-4614-1025-6},
      booktitle     = {Selenium / Hatfield, Dolph L. (Editor)
                       ; New York, NY : Springer New York,
                       2012, Chapter 43 ; ISBN:
                       978-1-4614-1024-9 ;
                       doi:10.1007/978-1-4614-1025-6},
      abstract     = {The selenoperoxidase glutathione peroxidase 4 (GPx4 –
                      also frequently referred to as phospholipid hydroperoxide
                      glutathione peroxidase, PHGPx) is one of the eight
                      glutathione peroxidases in mammals, but the only one known
                      to be essential for early mouse development. GPx4 is
                      emerging as one of the most central selenoproteins, and thus
                      has attracted considerable interest in recent years. Key
                      insights into GPx4 function came from the numerous
                      transgenic and knockout mouse studies performed mainly
                      during the last couple of years, which are summarized here.
                      These investigations not only firmly established a crucial
                      role for GPx4 in male fertility and neuroprotection, but
                      also indicated a major regulatory role of GPx4 in oxidative
                      stress-induced cell death signaling. Beyond this, lipid
                      hydroperoxides (LOOH), downstream of GPx4 inactivation, have
                      been recently shown to control receptor tyrosine kinase
                      (RTK) signaling, thus adding a new layer of complexity to
                      the multifaceted roles of GPx4 in cell signaling and disease
                      development.},
      cin          = {AG Wurst},
      cid          = {I:(DE-2719)1140001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)7},
      doi          = {10.1007/978-1-4614-1025-6_43},
      url          = {https://pub.dzne.de/record/144578},
}