% 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”.

@ARTICLE{Geisler:136119,
      author       = {Geisler, Sven and Holmström, Kira M and Treis, Angela and
                      Skujat, Diana and Weber, Stephanie S and Fiesel, Fabienne C
                      and Kahle, Philipp and Springer, Wolfdieter},
      title        = {{T}he {PINK}1/{P}arkin-mediated mitophagy is compromised by
                      {PD}-associated mutations.},
      journal      = {Autophagy},
      volume       = {6},
      number       = {7},
      issn         = {1554-8627},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {DZNE-2020-02441},
      pages        = {871-878},
      year         = {2010},
      abstract     = {Mitochondrial dysfunction is an early sign of many
                      neurodegenerative diseases. Very recently, two Parkinson
                      disease (PD) associated genes, PINK1 and Parkin, were shown
                      to mediate the degradation of damaged mitochondria via
                      selective autophagy (mitophagy). PINK1 kinase activity is
                      needed for prompt and efficient Parkin recruitment to
                      impaired mitochondria. PD-associated Parkin mutations
                      interfere with the process of mitophagy at distinct steps.
                      Here we show that whole mitochondria are turned over via
                      macroautophagy. Moreover, disease-associated PINK1 mutations
                      also compromise the selective degradation of depolarized
                      mitochondria. This may be due to the decreased physical
                      binding activity of PD-linked PINK1 mutations to Parkin.
                      Thus, PINK1 mutations abrogate autophagy of impaired
                      mitochondria upstream of Parkin. In addition to compromised
                      PINK1 kinase activity, reduced binding of PINK1 to Parkin
                      leads to failure in Parkin mitochondrial translocation,
                      resulting in the accumulation of damaged mitochondria, which
                      may contribute to disease pathogenesis.},
      keywords     = {Animals / Autophagy: genetics / HEK293 Cells / HeLa Cells /
                      Humans / Mitochondria: pathology / Mitochondria: physiology
                      / Mutation / Parkinson Disease: genetics / Parkinson
                      Disease: pathology / Parkinson Disease: physiopathology /
                      Protein Kinases: genetics / Protein Kinases: metabolism /
                      RNA, Small Interfering: genetics / RNA, Small Interfering:
                      metabolism / Ubiquitin-Protein Ligases: genetics /
                      Ubiquitin-Protein Ligases: metabolism / RNA, Small
                      Interfering (NLM Chemicals) / Ubiquitin-Protein Ligases (NLM
                      Chemicals) / parkin protein (NLM Chemicals) / Protein
                      Kinases (NLM Chemicals) / PTEN-induced putative kinase (NLM
                      Chemicals)},
      cin          = {AG Kahle 2},
      ddc          = {570},
      cid          = {I:(DE-2719)1210000-4},
      pnm          = {345 - Population Studies and Genetics (POF3-345)},
      pid          = {G:(DE-HGF)POF3-345},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20798600},
      doi          = {10.4161/auto.6.7.13286},
      url          = {https://pub.dzne.de/record/136119},
}