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@ARTICLE{Fischer:277807,
      author       = {Fischer, Anna-Lisa and Schmitz, Matthias and Thom, Tobias
                      and Zafar, Saima and Younas, Neelam and da Silva Correia,
                      Susana and Silva-Correia, Susana and Canaslan, Sezgi and
                      Zerr, Inga},
      title        = {{A}lpha-{S}ynuclein {D}emonstrates {V}arying {B}inding
                      {A}ffinities {W}ith {D}ifferent {T}au {I}soforms.},
      journal      = {Journal of neurochemistry},
      volume       = {169},
      number       = {4},
      issn         = {0022-3042},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {DZNE-2025-00479},
      pages        = {e70053},
      year         = {2025},
      abstract     = {The hallmark of various neurodegenerative diseases is the
                      accumulation and aggregation of amyloidogenic proteins, such
                      as amyloid-beta (Aβ) and tau in Alzheimer's disease (AD)
                      and alpha-synuclein (aSyn) in synucleinopathies. Many
                      neurodegenerative diseases express mixed pathology. For
                      instance, Lewy bodies are reported in tauopathies and
                      neurofibrillary tau-tangles are detected in
                      synucleinopathies, suggesting a potential co-existence or
                      crosstalk of misfolded aSyn and tau. In the present study,
                      we investigated the binding characteristics of monomeric
                      aSyn with different tau isoforms by using surface plasmon
                      resonance (SPR) spectroscopy allowing monitoring direct
                      protein-protein interactions and their potential
                      co-localization using SH-SY5Y cells. The calculation of the
                      binding parameters (association and dissociation rate
                      constants) indicated the strongest binding affinity between
                      aSyn and tau isoform 1N3R followed by tau 2N3R and tau 2N4R.
                      Co-localization studies in SH-SY5Y cells, treated with aSyn
                      and all six tau isoforms revealed an intracellular
                      co-localization of aSyn with different isoforms of tau.
                      Subcellular fractionation confirmed the cellular uptake and
                      colocalization of tau and aSyn in the same compartment,
                      showing their expression in membrane, nuclear, and
                      cytoskeletal fractions. Understanding the intricate
                      interplay between aSyn and tau is crucial for unraveling the
                      pathophysiology of PD, AD, and related neurodegenerative
                      disorders, ultimately paving the way for the development of
                      effective treatments targeting this interaction. In
                      conclusion, our data indicate that aSyn and tau are direct
                      interaction partners with varying binding affinities
                      depending on the tau isoform. This interaction may be
                      significant for understanding the pathophysiology of
                      dementia with mixed pathologies.},
      keywords     = {Humans / tau Proteins: metabolism / alpha-Synuclein:
                      metabolism / Protein Isoforms: metabolism / Protein Binding:
                      physiology / Cell Line, Tumor / Surface Plasmon Resonance /
                      Alzheimer's disease (Other) / Parkinson's disease (Other) /
                      alpha‐synuclein (Other) / interaction (Other) /
                      synucleinopathies (Other) / tau (Other) / tauopathies
                      (Other) / tau Proteins (NLM Chemicals) / alpha-Synuclein
                      (NLM Chemicals) / Protein Isoforms (NLM Chemicals)},
      cin          = {AG Zerr},
      ddc          = {610},
      cid          = {I:(DE-2719)1440011-1},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40165586},
      doi          = {10.1111/jnc.70053},
      url          = {https://pub.dzne.de/record/277807},
}