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@ARTICLE{Burbulla:139516,
      author       = {Burbulla, Lena F and Song, Pingping and Mazzulli, Joseph R
                      and Zampese, Enrico and Wong, Yvette C and Jeon, Sohee and
                      Santos, David P and Blanz, Judith and Obermaier, Carolin D
                      and Strojny, Chelsee and Savas, Jeffrey N and Kiskinis,
                      Evangelos and Zhuang, Xiaoxi and Krüger, Rejko and
                      Surmeier, D James and Krainc, Dimitri},
      title        = {{D}opamine oxidation mediates mitochondrial and lysosomal
                      dysfunction in {P}arkinson's disease.},
      journal      = {Science / Science now},
      volume       = {357},
      number       = {6357},
      issn         = {0036-8075},
      address      = {Washington, DC},
      publisher    = {Assoc.60841},
      reportid     = {DZNE-2020-05838},
      pages        = {1255-1261},
      year         = {2017},
      abstract     = {Mitochondrial and lysosomal dysfunction have been
                      implicated in substantia nigra dopaminergic
                      neurodegeneration in Parkinson's disease (PD), but how these
                      pathways are linked in human neurons remains unclear. Here
                      we studied dopaminergic neurons derived from patients with
                      idiopathic and familial PD. We identified a time-dependent
                      pathological cascade beginning with mitochondrial oxidant
                      stress leading to oxidized dopamine accumulation and
                      ultimately resulting in reduced glucocerebrosidase enzymatic
                      activity, lysosomal dysfunction, and α-synuclein
                      accumulation. This toxic cascade was observed in human, but
                      not in mouse, PD neurons at least in part because of
                      species-specific differences in dopamine metabolism.
                      Increasing dopamine synthesis or α-synuclein amounts in
                      mouse midbrain neurons recapitulated pathological phenotypes
                      observed in human neurons. Thus, dopamine oxidation
                      represents an important link between mitochondrial and
                      lysosomal dysfunction in PD pathogenesis.},
      keywords     = {Animals / Antioxidants: pharmacology / Calcineurin
                      Inhibitors: pharmacology / Cell Line / Disease Models,
                      Animal / Dopamine: metabolism / Dopaminergic Neurons:
                      metabolism / Glucosylceramidase: deficiency / Humans /
                      Lysosomes: metabolism / Melanins: metabolism /
                      Mesencephalon: enzymology / Mesencephalon: metabolism / Mice
                      / Mice, Knockout / Mitochondria: drug effects /
                      Mitochondria: enzymology / Mitochondria: metabolism /
                      Oxidation-Reduction / Oxidative Stress: drug effects /
                      Parkinson Disease: enzymology / Parkinson Disease: genetics
                      / Parkinson Disease: metabolism / Protein Deglycase DJ-1:
                      genetics / Substantia Nigra: enzymology / Substantia Nigra:
                      metabolism / Tacrolimus: pharmacology / alpha-Synuclein:
                      metabolism / Antioxidants (NLM Chemicals) / Calcineurin
                      Inhibitors (NLM Chemicals) / Melanins (NLM Chemicals) /
                      alpha-Synuclein (NLM Chemicals) / neuromelanin (NLM
                      Chemicals) / PARK7 protein, human (NLM Chemicals) / Protein
                      Deglycase DJ-1 (NLM Chemicals) / Glucosylceramidase (NLM
                      Chemicals) / Dopamine (NLM Chemicals) / Tacrolimus (NLM
                      Chemicals)},
      cin          = {AG N.N. 3 / AG Gasser 1},
      ddc          = {320},
      cid          = {I:(DE-2719)1240015 / I:(DE-2719)1210000},
      pnm          = {345 - Population Studies and Genetics (POF3-345) / 344 -
                      Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-345 / G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28882997},
      pmc          = {pmc:PMC6021018},
      doi          = {10.1126/science.aam9080},
      url          = {https://pub.dzne.de/record/139516},
}