% 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{Bruer:276150,
      author       = {Bräuer, Stefan and Schniewind, Inaki and Dinter, Elisabeth
                      and Falkenburger, Björn H},
      title        = {{R}ecursive seed amplification detects distinct
                      α-synuclein strains in cerebrospinal fluid of patients with
                      {P}arkinson's disease.},
      journal      = {Acta Neuropathologica Communications},
      volume       = {13},
      number       = {1},
      issn         = {2051-5960},
      address      = {London},
      publisher    = {Biomed Central},
      reportid     = {DZNE-2025-00222},
      pages        = {13},
      year         = {2025},
      abstract     = {Parkinson's disease (PD) is a heterogeneous
                      neurodegenerative disorder with a wide range of clinical
                      phenotypes. Pathologically, it is characterized by neuronal
                      inclusions containing misfolded, fibrillar alpha-synuclein
                      (aSyn). Prion-like properties of aSyn contribute to the
                      spread of aSyn pathology throughout the nervous system as
                      the disease progresses. Utilizing these properties, seed
                      amplification assays (SAA) enable the detection of aSyn
                      pathology in living patients. We hypothesized that
                      structurally distinct aSyn aggregates, or strains, may
                      underlie the clinical heterogeneity of PD. To test this
                      hypothesis, we recursively amplified aSyn fibrils from the
                      cerebrospinal fluid (CSF) of 54 patients (34 people with PD
                      and 20 controls). These fibrils were then characterized
                      regarding SAA kinetic properties and detergent resistance.
                      In addition, cultured cells were transfected with SAA
                      products, and the extent of seeded aSyn pathology was
                      quantified by staining for phosphorylated aSyn followed by
                      automated high-throughput microscopy and image analysis. We
                      found that fibrils, amplified from CSF by recursive SAA,
                      exhibit two types of distinct biophysical properties and
                      have different seeding capacities in cells. These properties
                      are associated with clinical parameters and may therefore
                      help explain the clinical heterogeneity in PD. Measuring
                      aSyn strains may be relevant for prognosis and for therapies
                      targeting aSyn pathology.},
      keywords     = {Humans / alpha-Synuclein: cerebrospinal fluid / Parkinson
                      Disease: cerebrospinal fluid / Female / Male / Aged / Middle
                      Aged / Aged, 80 and over / Alpha-synuclein (Other) /
                      Parkinson’s disease (Other) / RT-QuIC (Other) / Seed
                      amplification assay (Other) / Strains (Other) /
                      alpha-Synuclein (NLM Chemicals) / SNCA protein, human (NLM
                      Chemicals)},
      cin          = {AG Falkenburger},
      ddc          = {610},
      cid          = {I:(DE-2719)1710012},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39833972},
      pmc          = {pmc:PMC11749544},
      doi          = {10.1186/s40478-024-01923-8},
      url          = {https://pub.dzne.de/record/276150},
}