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@ARTICLE{Majewski:452699,
      author       = {Majewski, Jaroslaw and Jones, Emmalee M. and Vander Zanden,
                      Crystal M. and Biernat, Jacek and Mandelkow, Eckhard and
                      Chi, Eva Y.},
      title        = {{L}ipid membrane templated misfolding and self-assembly of
                      intrinsically disordered tau protein},
      journal      = {Scientific reports},
      volume       = {10},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2020-04826},
      pages        = {13324},
      year         = {2020},
      abstract     = {The aggregation of the intrinsically disordered tau protein
                      into highly ordered β-sheet-rich fibrils is implicated in
                      the pathogenesis of a range of neurodegenerative disorders.
                      The mechanism of tau fibrillogenesis remains unresolved,
                      particularly early events that trigger the misfolding and
                      assembly of the otherwise soluble and stable tau. We
                      investigated the role the lipid membrane plays in modulating
                      the aggregation of three tau variants, the largest isoform
                      hTau40, the truncated construct K18, and a
                      hyperphosphorylation-mimicking mutant hTau40/3Epi. Despite
                      being charged and soluble, the tau proteins were also highly
                      surface active and favorably interacted with anionic lipid
                      monolayers at the air/water interface. Membrane binding of
                      tau also led to the formation of a macroscopic, gelatinous
                      layer at the air/water interface, possibly related to tau
                      phase separation. At the molecular level, tau assembled into
                      oligomers composed of ~ 40 proteins misfolded in a
                      β-sheet conformation at the membrane surface, as detected
                      by in situ synchrotron grazing-incidence X-ray diffraction.
                      Concomitantly, membrane morphology and lipid packing became
                      disrupted. Our findings support a general tau aggregation
                      mechanism wherein tau’s inherent surface activity and
                      favorable interactions with anionic lipids drive
                      tau-membrane association, inducing misfolding and
                      self-assembly of the disordered tau into β-sheet-rich
                      oligomers that subsequently seed fibrillation and deposition
                      into diseased tissues.},
      cin          = {DOOR ; HAS-User},
      ddc          = {600},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)D-BW1-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32770092},
      UT           = {WOS:000561428200001},
      doi          = {10.1038/s41598-020-70208-6},
      url          = {https://bib-pubdb1.desy.de/record/452699},
}