% 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{RodriguezMuela:157830,
      author       = {Rodriguez-Muela, Natalia},
      title        = {{A}utophagy in motor neuron diseases},
      journal      = {Progress in molecular biology and translational science},
      volume       = {172},
      issn         = {1877-1173},
      address      = {Amsterdam ˜[u.a.]œ},
      publisher    = {Elsevier},
      reportid     = {DZNE-2021-01287},
      pages        = {157-202},
      year         = {2020},
      abstract     = {Motor neuron diseases (MNDs) are a wide group of
                      neurodegenerative disorders characterized by the
                      degeneration of a specific neuronal type located in the
                      central nervous system, the motor neuron (MN). There are two
                      main types of MNs, spinal and cortical MNs and depending on
                      the type of MND, one or both types are affected. Cortical
                      MNs innervate spinal MNs and these control a variety of
                      cellular targets, being skeletal muscle their main one which
                      is also affected in MNDs. A correct functionality of
                      autophagy is necessary for the survival of all cellular
                      types and it is particularly crucial for neurons, given
                      their postmitotic and highly specialized nature. Numerous
                      studies have identified alterations of autophagy activity in
                      multiple MNDs. The scientific community has been
                      particularly prolific in reporting the role that autophagy
                      plays in the most common adult MND, amyotrophic lateral
                      sclerosis, although many studies have started to identify
                      physiological and pathological functions of this catabolic
                      system in other MNDs, such as spinal muscular atrophy and
                      spinal and bulbar muscular atrophy. The degradation of
                      selective cargo by autophagy and how this process is altered
                      upon the presence of MND-causing mutations is currently also
                      a matter of intense investigation, particularly regarding
                      the selective autophagic clearance of mitochondria. Thorough
                      reviews on this field have been recently published. This
                      chapter will cover the current knowledge on the
                      functionality of autophagy and lysosomal homeostasis in the
                      main MNDs and other autophagy-related topics in the MND
                      field that have risen special interest in the research
                      community.},
      subtyp        = {Review Article},
      keywords     = {Adult / Amyotrophic Lateral Sclerosis: genetics /
                      Amyotrophic Lateral Sclerosis: pathology / Animals /
                      Autophagy: drug effects / Autophagy: physiology /
                      Autophagy-Related Proteins: genetics / Autophagy-Related
                      Proteins: physiology / C9orf72 Protein: deficiency / C9orf72
                      Protein: genetics / C9orf72 Protein: physiology / DNA Repeat
                      Expansion / Disease Models, Animal / Endocytosis / Humans /
                      Mice, Transgenic / Motor Neuron Disease: genetics / Motor
                      Neuron Disease: pathology / Muscular Atrophy, Spinal:
                      genetics / Muscular Atrophy, Spinal: pathology / Mutation /
                      Neurodegenerative Diseases: genetics / Neurodegenerative
                      Diseases: pathology / Organelles / RNA-Binding Protein FUS:
                      deficiency / RNA-Binding Protein FUS: genetics / RNA-Binding
                      Protein FUS: physiology / TDP-43 Proteinopathies: genetics /
                      TDP-43 Proteinopathies: pathology},
      cin          = {AG Rodriguez-Muela},
      ddc          = {530},
      cid          = {I:(DE-2719)1713001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32620242},
      doi          = {10.1016/bs.pmbts.2020.03.009 },
      url          = {https://pub.dzne.de/record/157830},
}