% 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{Espay:276274,
      author       = {Espay, Alberto J and Lees, Andrew J and Cardoso, Francisco
                      and Frucht, Steven J and Erskine, Daniel and Sandoval,
                      Ivette M and Bernal-Conde, Luis Daniel and Sturchio, Andrea
                      and Imarisio, Alberto and Hoffmann, Christian and
                      Montemagno, Kora T and Milovanovic, Dragomir and Halliday,
                      Glenda M and Manfredsson, Fredric P},
      title        = {{T}he α-synuclein seed amplification assay: {I}nterpreting
                      a test of {P}arkinson's pathology.},
      journal      = {Parkinsonism $\&$ related disorders},
      volume       = {131},
      issn         = {1353-8020},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {DZNE-2025-00253},
      pages        = {107256},
      year         = {2025},
      abstract     = {The α-synuclein seed amplification assay (αSyn-SAA)
                      sensitively detects Lewy pathology, the amyloid state of
                      α-synuclein, in the cerebrospinal fluid (CSF) of patients
                      with Parkinson's disease (PD). The αSyn-SAA harnesses the
                      physics of seeding, whereby a superconcentrated solution of
                      recombinant α-synuclein lowers the thermodynamic threshold
                      (nucleation barrier) for aggregated α-synuclein to act as a
                      nucleation catalyst ('seed') to trigger the precipitation
                      (nucleation) of monomeric α-synuclein into pathology. This
                      laboratory setup increases the signal for identifying a
                      catalyst if one is present in the tissue examined. The
                      result is binary: positive, meaning precipitation occurred,
                      and a catalyst is present, or negative, meaning no
                      precipitation, therefore no catalyst. Since protein
                      precipitation via seeding can only occur at a concentration
                      many-fold higher than the human brain, laboratory-elicited
                      seeding does not mean human brain seeding. We suggest that a
                      positive αSyn-SAA reveals the presence of pathological
                      α-synuclein but not the underlying etiology for the
                      precipitation of monomeric α-synuclein into its
                      pathological form. Thus, a positive αSyn-SAA supports a
                      clinical diagnosis of PD but cannot inform disease
                      pathogenesis, ascertain severity, predict the rate of
                      progression, define biology or biological subtypes, or
                      monitor treatment response.},
      subtyp        = {Review Article},
      keywords     = {alpha-Synuclein: cerebrospinal fluid / alpha-Synuclein:
                      metabolism / Humans / Parkinson Disease: diagnosis /
                      Parkinson Disease: cerebrospinal fluid / Parkinson Disease:
                      metabolism / Parkinson's disease (Other) / Seed
                      amplification assay (Other) / Seeding (Other) / α-synuclein
                      (Other) / alpha-Synuclein (NLM Chemicals)},
      cin          = {AG Milovanovic (Berlin)},
      ddc          = {610},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39794217},
      doi          = {10.1016/j.parkreldis.2024.107256},
      url          = {https://pub.dzne.de/record/276274},
}