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@ARTICLE{Jucker:140231,
      author       = {Jucker, Mathias and Walker, Lary C},
      title        = {{P}ropagation and spread of pathogenic protein assemblies
                      in neurodegenerative diseases.},
      journal      = {Nature reviews / Neuroscience},
      volume       = {21},
      number       = {10},
      issn         = {1097-6256},
      address      = {London},
      publisher    = {Nature Publ. Group58142},
      reportid     = {DZNE-2020-06553},
      pages        = {1341-1349},
      year         = {2018},
      abstract     = {Many neurodegenerative diseases, such as Alzheimer's
                      disease, Parkinson's disease, and amyotrophic lateral
                      sclerosis, are characterized by the progressive appearance
                      of abnormal proteinaceous assemblies in the nervous system.
                      Studies in experimental systems indicate that the assemblies
                      originate from the prion-like seeded aggregation of specific
                      misfolded proteins that proliferate and amass to form the
                      intracellular and/or extracellular lesions typical of each
                      disorder. The host in which the proteopathic seeds arise
                      provides the biochemical and physiological environment that
                      either supports or restricts their emergence, proliferation,
                      self-assembly, and spread. Multiple mechanisms influence the
                      spatiotemporal spread of seeds and the nature of the
                      resulting lesions, one of which is the cellular uptake,
                      release, and transport of seeds along neural pathways and
                      networks. The characteristics of cells and regions in the
                      affected network govern their vulnerability and thereby
                      influence the neuropathological and clinical attributes of
                      the disease. The propagation of pathogenic protein
                      assemblies within the nervous system is thus determined by
                      the interaction of the proteopathic agent and the host
                      milieu.},
      subtyp        = {Review Article},
      keywords     = {Animals / Cell Communication / Humans / Neurodegenerative
                      Diseases: metabolism / Neurodegenerative Diseases: pathology
                      / Prions: metabolism / Prions: pathogenicity / Prions (NLM
                      Chemicals)},
      cin          = {AG Jucker / Tübingen Pre 2020},
      ddc          = {570},
      cid          = {I:(DE-2719)1210001 / I:(DE-2719)6000018},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30258241},
      pmc          = {pmc:PMC6375686},
      doi          = {10.1038/s41593-018-0238-6},
      url          = {https://pub.dzne.de/record/140231},
}