% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Akoury:148122,
      author       = {Akoury, E. and Gajda, M. J. and Pickhardt, M. and Biernat,
                      J. and Pornsuwan, S. and Griesinger, Ch. and Mandelkow, E.
                      and Zweckstetter, M. and DESY},
      title        = {{I}nhibition of tau filament formation by conformational
                      modulation},
      journal      = {Journal of the American Chemical Society},
      volume       = {135},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PHPPUBDB-26150},
      pages        = {2853-2862},
      year         = {2013},
      abstract     = {Antiaggregation drugs play an important role in therapeutic
                      approaches for Alzheimer's disease. Although a large number
                      of small molecules that inhibit the aggregation of the tau
                      protein have been identified, little is known about their
                      mode of action. Here, we reveal the mechanism and the nature
                      of tau species that are generated by interaction of tau with
                      the organic compound pthalocyanine tetrasulfonate (PcTS). We
                      demonstrate that PcTS interferes with tau filament formation
                      by targeting the protein into soluble oligomers. A
                      combination of NMR spectroscopy, electron paramagnetic
                      resonance, and small-angle X-ray scattering reveals that the
                      soluble tau oligomers contain a dynamic, noncooperatively
                      stabilized core with a diameter of 30-40 nm that is distinct
                      from the core of tau filaments. Our results suggest that
                      specific modulation of the conformation of tau is a viable
                      strategy for reduction of pathogenic tau deposits.},
      cin          = {HASYLAB / MPG / EMBL},
      ddc          = {540},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$ /
                      $I:(DE-H253)MPG_-2012_-20120307$ /
                      $I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {DORIS Beamline D1.2 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-D1.2-20130405},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23360400},
      UT           = {WOS:000315373000066},
      doi          = {10.1021/ja312471h},
      url          = {https://bib-pubdb1.desy.de/record/148122},
}