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@ARTICLE{Prince:256516,
      author       = {Prince, Prabhu Rajaiah and Hochmair, Janine and Brognaro,
                      Hévila and Gevorgyan, Susanna and Franck, Maximilian and
                      Schubert, Robin and Lorenzen, Kristina and Yazici, Selin and
                      Mandelkow, Eckhard and Wegmann, Susanne and Betzel,
                      Christian},
      title        = {{I}nitiation and modulation of {T}au protein phase
                      separation by the drug suramin.},
      journal      = {Scientific reports},
      volume       = {13},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {DZNE-2023-00340},
      pages        = {3963},
      year         = {2023},
      note         = {CC BY},
      abstract     = {Tau is an intrinsically disordered neuronal protein in the
                      central nervous system. Aggregated Tau is the main component
                      of neurofibrillary tangles observed in Alzheimer's disease.
                      In vitro, Tau aggregation can be triggered by polyanionic
                      co-factors, like RNA or heparin. At different concentration
                      ratios, the same polyanions can induce Tau condensates via
                      liquid-liquid phase separation (LLPS), which over time
                      develop pathological aggregation seeding potential. Data
                      obtained by time resolved Dynamic Light Scattering
                      experiments (trDLS), light and electron microscopy show that
                      intermolecular electrostatic interactions between Tau and
                      the negatively charged drug suramin induce Tau condensation
                      and compete with the interactions driving and stabilizing
                      the formation of Tau:heparin and Tau:RNA coacervates, thus,
                      reducing their potential to induce cellular Tau aggregation.
                      Tau:suramin condensates do not seed Tau aggregation in a HEK
                      cell model for Tau aggregation, even after extended
                      incubation. These observations indicate that
                      electrostatically driven Tau condensation can occur without
                      pathological aggregation when initiated by small anionic
                      molecules. Our results provide a novel avenue for
                      therapeutic intervention of aberrant Tau phase separation,
                      utilizing small anionic compounds.},
      keywords     = {Humans / tau Proteins: metabolism / Suramin: pharmacology /
                      Alzheimer Disease: metabolism / Heparin / RNA: metabolism /
                      tau Proteins (NLM Chemicals) / Suramin (NLM Chemicals) /
                      Heparin (NLM Chemicals) / RNA (NLM Chemicals)},
      cin          = {AG Wegmann / AG Mandelkow 1},
      ddc          = {600},
      cid          = {I:(DE-2719)1810006 / I:(DE-2719)1013014},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36894559},
      pmc          = {pmc:PMC9997437},
      doi          = {10.1038/s41598-023-29846-9},
      url          = {https://pub.dzne.de/record/256516},
}