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@ARTICLE{Chakraborty:264175,
      author       = {Chakraborty, Pijush and Rivière, Gwladys and Hebestreit,
                      Alina and de Opakua, Alain Ibáñez and Vorberg, Ina M and
                      Andreas, Loren B and Zweckstetter, Markus},
      title        = {{A}cetylation discriminates disease-specific tau
                      deposition.},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2023-00955},
      pages        = {5919},
      year         = {2023},
      abstract     = {Pathogenic aggregation of the protein tau is a hallmark of
                      Alzheimer's disease and several other tauopathies.
                      Tauopathies are characterized by the deposition of specific
                      tau isoforms as disease-related tau filament structures. The
                      molecular processes that determine isoform-specific
                      deposition of tau are however enigmatic. Here we show that
                      acetylation of tau discriminates its isoform-specific
                      aggregation. We reveal that acetylation strongly attenuates
                      aggregation of four-repeat tau protein, but promotes amyloid
                      formation of three-repeat tau. We further identify
                      acetylation of lysine 298 as a hot spot for isoform-specific
                      tau aggregation. Solid-state NMR spectroscopy demonstrates
                      that amyloid fibrils formed by unmodified and acetylated
                      three-repeat tau differ in structure indicating that
                      site-specific acetylation modulates tau structure. The
                      results implicate acetylation as a critical regulator that
                      guides the selective aggregation of three-repeat tau and the
                      development of tau isoform-specific neurodegenerative
                      diseases.},
      keywords     = {Humans / 14-3-3 Proteins / Acetylation / Alzheimer Disease
                      / tau Proteins / Tauopathies / 14-3-3 Proteins (NLM
                      Chemicals) / tau Proteins (NLM Chemicals) / MAPT protein,
                      human (NLM Chemicals)},
      cin          = {AG Zweckstetter / AG Vorberg},
      ddc          = {500},
      cid          = {I:(DE-2719)1410001 / I:(DE-2719)1013004},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37739953},
      pmc          = {pmc:PMC10517010},
      doi          = {10.1038/s41467-023-41672-1},
      url          = {https://pub.dzne.de/record/264175},
}