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@ARTICLE{Schmitz:256605,
      author       = {Schmitz, Matthias and Candelise, Niccolò and Canaslan,
                      Sezgi and Altmeppen, Hermann C and Matschke, Jakob and
                      Glatzel, Markus and Younas, Neelam and Zafar, Saima and
                      Hermann, Peter and Zerr, Inga},
      title        = {α-{S}ynuclein conformers reveal link to clinical
                      heterogeneity of α-synucleinopathies.},
      journal      = {Translational neurodegeneration},
      volume       = {12},
      number       = {1},
      issn         = {2047-9158},
      address      = {London},
      publisher    = {Biomed Central},
      reportid     = {DZNE-2023-00357},
      pages        = {12},
      year         = {2023},
      note         = {CC BY},
      abstract     = {α-Synucleinopathies, such as Parkinson's disease (PD),
                      dementia with Lewy bodies (DLB) and multiple system atrophy,
                      are a class of neurodegenerative diseases exhibiting
                      intracellular inclusions of misfolded α-synuclein (αSyn),
                      referred to as Lewy bodies or oligodendroglial cytoplasmic
                      inclusions (Papp-Lantos bodies). Even though the specific
                      cellular distribution of aggregated αSyn differs in PD and
                      DLB patients, both groups show a significant pathological
                      overlap, raising the discussion of whether PD and DLB are
                      the same or different diseases. Besides clinical
                      investigation, we will focus in addition on methodologies,
                      such as protein seeding assays (real-time quaking-induced
                      conversion), to discriminate between different types of
                      α-synucleinopathies. This approach relies on the seeding
                      conversion properties of misfolded αSyn, supporting the
                      hypothesis that different conformers of misfolded αSyn may
                      occur in different types of α-synucleinopathies.
                      Understanding the pathological processes influencing the
                      disease progression and phenotype, provoked by different
                      αSyn conformers, will be important for a personalized
                      medical treatment in future.},
      subtyp        = {Review Article},
      keywords     = {Humans / alpha-Synuclein: genetics / alpha-Synuclein:
                      metabolism / Synucleinopathies: diagnosis /
                      Synucleinopathies: genetics / Synucleinopathies: metabolism
                      / Parkinson Disease: diagnosis / Parkinson Disease: genetics
                      / Parkinson Disease: metabolism / Lewy Bodies: pathology /
                      Multiple System Atrophy: diagnosis / Multiple System
                      Atrophy: genetics / Multiple System Atrophy: pathology /
                      α-synuclein (Other) / Protein strains (Other) / RT-QuIC
                      (Other) / α-synuclein (Other) / α-synucleinopathies
                      (Other) / alpha-Synuclein (NLM Chemicals) /
                      α-synucleinopathies (Other)},
      cin          = {AG Zerr / Ext UMG Zerr / Clinical Dementia Research
                      Göttingen},
      ddc          = {570},
      cid          = {I:(DE-2719)1440011-1 / I:(DE-2719)5000037 /
                      I:(DE-2719)1440015},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36915212},
      pmc          = {pmc:PMC10012698},
      doi          = {10.1186/s40035-023-00342-4},
      url          = {https://pub.dzne.de/record/256605},
}