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@ARTICLE{Stroo:257883,
      author       = {Stroo, Esther and Janssen, Leen and Sin, Olga and Hogewerf,
                      Wytse and Koster, Mirjam and Harkema, Liesbeth and Youssef,
                      Sameh A and Beschorner, Natalie and Wolters, Anouk Hg and
                      Bakker, Bjorn and Becker, Lore and Garrett, Lilian and
                      Marschall, Susan and Hoelter, Sabine M and Wurst, Wolfgang
                      and Fuchs, Helmut and Gailus-Durner, Valerie and Hrabe de
                      Angelis, Martin and Thathiah, Amantha and Foijer, Floris and
                      van de Sluis, Bart and van Deursen, Jan and Jucker, Matthias
                      and de Bruin, Alain and Nollen, Ellen Aa},
      title        = {{D}eletion of {SERF}2 in mice delays embryonic development
                      and alters amyloid deposit structure in the brain.},
      journal      = {Life science alliance},
      volume       = {6},
      number       = {7},
      issn         = {2575-1077},
      address      = {Heidelberg},
      publisher    = {EMBO Press},
      reportid     = {DZNE-2023-00511},
      pages        = {e202201730},
      year         = {2023},
      abstract     = {In age-related neurodegenerative diseases, like Alzheimer's
                      and Parkinson's, disease-specific proteins become
                      aggregation-prone and form amyloid-like deposits. Depletion
                      of SERF proteins ameliorates this toxic process in worm and
                      human cell models for diseases. Whether SERF modifies
                      amyloid pathology in mammalian brain, however, has remained
                      unknown. Here, we generated conditional Serf2 knockout mice
                      and found that full-body deletion of Serf2 delayed embryonic
                      development, causing premature birth and perinatal
                      lethality. Brain-specific Serf2 knockout mice, on the other
                      hand, were viable, and showed no major behavioral or
                      cognitive abnormalities. In a mouse model for amyloid-β
                      aggregation, brain depletion of Serf2 altered the binding of
                      structure-specific amyloid dyes, previously used to
                      distinguish amyloid polymorphisms in the human brain. These
                      results suggest that Serf2 depletion changed the structure
                      of amyloid deposits, which was further supported by scanning
                      transmission electron microscopy, but further study will be
                      required to confirm this observation. Altogether, our data
                      reveal the pleiotropic functions of SERF2 in embryonic
                      development and in the brain and support the existence of
                      modifying factors of amyloid deposition in mammalian brain,
                      which offer possibilities for polymorphism-based
                      interventions.},
      keywords     = {Brain: embryology / Mice / Humans / Animals / Plaque,
                      Amyloid: metabolism / Brain: metabolism / Amyloid
                      beta-Peptides: metabolism / Mice, Knockout / Embryonic
                      Development: genetics / Mammals: metabolism / Intracellular
                      Signaling Peptides and Proteins: metabolism / Amyloid
                      beta-Peptides (NLM Chemicals) / SERF2 protein, human (NLM
                      Chemicals) / Intracellular Signaling Peptides and Proteins
                      (NLM Chemicals) / Serf2 protein, mouse (NLM Chemicals)},
      cin          = {AG Wurst},
      ddc          = {570},
      cid          = {I:(DE-2719)1140001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37130781},
      pmc          = {pmc:PMC10155860},
      doi          = {10.26508/lsa.202201730},
      url          = {https://pub.dzne.de/record/257883},
}