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@ARTICLE{Stapper:147737,
      author       = {Z. A. Stapper$^*$ and T. Jahn$^*$},
      title        = {{C}hanges in {G}lutathione {R}edox {P}otential {A}re
                      {L}inked to {A}β42-{I}nduced {N}eurotoxicity.},
      journal      = {Cell reports},
      volume       = {24},
      number       = {7},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2019-02714},
      pages        = {1696 - 1703},
      year         = {2018},
      abstract     = {Glutathione is the major low-molecular weight thiol
                      of eukaryotic cells. It is central to one of the two major
                      NADPH-dependent reducing systems and is likely to play a
                      role in combating oxidative stress, a process suggested to
                      play a key role in Alzheimer's disease (AD). However, the
                      nature and relevance of redox changes in the onset and
                      progression of AD are still uncertain. Here, we combine
                      genetically encoded redox sensors with our Drosophila models
                      of amyloid-beta (Aβ) aggregation. We find that changes in
                      glutathione redox potential (EGSH) closely correlate with
                      disease onset and progression. We observe this redox
                      imbalance specifically in neurons, but not in glia cells.
                      EGSH changes and Aβ42 deposition are also accompanied by
                      increased JNK stress signaling. Furthermore, pharmacologic
                      and genetic manipulation of glutathione synthesis modulates
                      Aβ42-mediated neurotoxicity, suggesting a causal
                      relationship between disturbed glutathione redox homeostasis
                      and early AD pathology.},
      keywords     = {Amyloid beta-Peptides (NLM Chemicals) / Glutaredoxins (NLM
                      Chemicals) / Luminescent Proteins (NLM Chemicals) / Peptide
                      Fragments (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / amyloid beta-protein (1-42) (NLM Chemicals) /
                      fluorescent protein 583 (NLM Chemicals) / Green Fluorescent
                      Proteins (NLM Chemicals) / Glutathione Peroxidase (NLM
                      Chemicals) / Glutamate-Cysteine Ligase (NLM Chemicals) /
                      Glutathione (NLM Chemicals)},
      cin          = {B180},
      ddc          = {610},
      cid          = {I:(DE-He78)B180-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30110626},
      doi          = {10.1016/j.celrep.2018.07.052},
      url          = {https://inrepo02.dkfz.de/record/147737},
}