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@ARTICLE{Outeiro:279886,
      author       = {Outeiro, Tiago F and Vieira, Tuane C R G},
      title        = {{P}reface to the {S}pecial {I}ssue '{H}istory, {B}iology
                      and {P}athobiology of {P}rions: {A} {F}ield of {R}enewed
                      {H}opes'.},
      journal      = {Journal of neurochemistry},
      volume       = {169},
      number       = {7},
      issn         = {0022-3042},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {DZNE-2025-00853},
      pages        = {e70156},
      year         = {2025},
      abstract     = {Research in the field of prion diseases has not only shed
                      light on the mechanisms underlying transmissible spongiform
                      encephalopathies (TSEs) but has also influenced the broader
                      understanding of protein misfolding disorders, including
                      Alzheimer's disease (AD), Parkinson's disease (PD), and
                      other tauopathies and synucleinopathies. Although prion
                      diseases are rare and invariably fatal, they have provided
                      an invaluable conceptual framework for the study of
                      age-associated neurodegenerative disorders. On the occasion
                      of the 'Prion 2023' meeting in Faro, Portugal, which brought
                      together leading experts in prion biology and
                      neurodegeneration to discuss emerging data and evolving
                      concepts, we put together a special issue on the topic to
                      discuss new structural insights, diagnostic technologies,
                      and the increasing recognition of prion-like mechanisms in a
                      wide range of proteinopathies. This Special Issue features
                      six comprehensive review articles that highlight key
                      advances and ongoing challenges in the study of prions and
                      related disorders.},
      subtyp        = {Editorial},
      keywords     = {Humans / Prion Diseases: pathology / Prion Diseases:
                      metabolism / Prion Diseases: genetics / Prions: metabolism /
                      Animals / alpha‐synuclein (Other) / amyloid (Other) /
                      beta‐amyloid (Other) / cancer (Other) / neurodegeneration
                      (Other) / p53 (Other) / prion (Other) / prion diseases
                      (Other) / protein aggregation (Other) / Prions (NLM
                      Chemicals)},
      cin          = {AG Fischer},
      ddc          = {610},
      cid          = {I:(DE-2719)1410002},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40653717},
      doi          = {10.1111/jnc.70156},
      url          = {https://pub.dzne.de/record/279886},
}