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@ARTICLE{deBoni:270708,
      author       = {de Boni, Laura and Wallis, Amber and Hays Watson, Aurelia
                      and Ruiz-Riquelme, Alejandro and Leyland, Louise-Ann and
                      Bourinaris, Thomas and Hannaway, Naomi and Wüllner, Ullrich
                      and Peters, Oliver and Priller, Josef and Falkenburger,
                      Björn H and Wiltfang, Jens and Bähr, Mathias and Zerr,
                      Inga and Bürger, Katharina and Perneczky, Robert and
                      Teipel, Stefan and Löhle, Matthias and Hermann, Wiebke and
                      Schott, Björn-Hendrik and Brockmann, Kathrin and Spottke,
                      Annika and Haustein, Katrin and Breuer, Peter and Houlden,
                      Henry and Weil, Rimona S and Bartels, Tim},
      title        = {{A}ggregation-resistant alpha-synuclein tetramers are
                      reduced in the blood of {P}arkinson's patients.},
      journal      = {EMBO molecular medicine},
      volume       = {16},
      number       = {7},
      issn         = {1757-4676},
      address      = {Heidelberg},
      publisher    = {EMBO Press},
      reportid     = {DZNE-2024-00880},
      pages        = {1657 - 1674},
      year         = {2024},
      abstract     = {Synucleinopathies such as Parkinson's disease (PD) are
                      defined by the accumulation and aggregation of the
                      α-synuclein protein in neurons, glia and other tissues. We
                      have previously shown that destabilization of α-synuclein
                      tetramers is associated with familial PD due to SNCA
                      mutations and demonstrated brain-region specific alterations
                      of α-synuclein multimers in sporadic PD patients following
                      the classical Braak spreading theory. In this study, we
                      assessed relative levels of disordered and higher-ordered
                      multimeric forms of cytosolic α-synuclein in blood from
                      familial PD with G51D mutations and sporadic PD patients. We
                      used an adapted in vitro-cross-linking protocol for human
                      EDTA-whole blood. The relative levels of higher-ordered
                      α-synuclein tetramers were diminished in blood from
                      familial PD and sporadic PD patients compared to controls.
                      Interestingly, the relative amount of α-synuclein tetramers
                      was already decreased in asymptomatic G51D carriers,
                      supporting the hypothesis that α-synuclein multimer
                      destabilization precedes the development of clinical PD. Our
                      data, therefore suggest that measuring α-synuclein
                      tetramers in blood may have potential as a facile biomarker
                      assay for early detection and quantitative tracking of PD
                      progression.},
      keywords     = {Humans / alpha-Synuclein: metabolism / alpha-Synuclein:
                      blood / Parkinson Disease: blood / Parkinson Disease:
                      metabolism / Parkinson Disease: genetics / Aged / Male /
                      Female / Middle Aged / Protein Multimerization / Protein
                      Aggregates / Parkinson’s disease (Other) / Alpha-synuclein
                      (Other) / Blood (Other) / Human (Other) / Parkinson’s
                      disease (Other) / Tetramer (Other) / alpha-Synuclein (NLM
                      Chemicals) / Protein Aggregates (NLM Chemicals) / SNCA
                      protein, human (NLM Chemicals)},
      cin          = {AG Wüllner / AG Peters / AG Priller / AG Falkenburger / AG
                      Wiltfang / Clinical Dementia Research (Göttingen) / AG Zerr
                      / Clinical Research (Munich) / AG Teipel / AG Storch / AG
                      Fischer / AG Gasser / AG Spottke},
      ddc          = {610},
      cid          = {I:(DE-2719)1011302 / I:(DE-2719)5000000 /
                      I:(DE-2719)5000007 / I:(DE-2719)1710012 / I:(DE-2719)1410006
                      / I:(DE-2719)1440015 / I:(DE-2719)1440011-1 /
                      I:(DE-2719)1111015 / I:(DE-2719)1510100 / I:(DE-2719)5000014
                      / I:(DE-2719)1410002 / I:(DE-2719)1210000 /
                      I:(DE-2719)1011103},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 352 -
                      Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC11250827},
      pubmed       = {pmid:38839930},
      doi          = {10.1038/s44321-024-00083-5},
      url          = {https://pub.dzne.de/record/270708},
}