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@ARTICLE{Wegmann:136780,
      author       = {Wegmann, Susanne and Medalsy, Izhar D and Mandelkow,
                      Eckhard and Müller, Daniel J},
      title        = {{T}he fuzzy coat of pathological human {T}au fibrils is a
                      two-layered polyelectrolyte brush.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {110},
      number       = {4},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DZNE-2020-03102},
      pages        = {E313-E321},
      year         = {2013},
      abstract     = {The structure and properties of amyloid-like Tau fibrils
                      accumulating in neurodegenerative diseases have been debated
                      for decades. Although the core of Tau fibrils assembles from
                      short β-strands, the properties of the much longer
                      unstructured Tau domains protruding from the fibril core
                      remain largely obscure. Applying immunogold transmission EM,
                      and force-volume atomic force microscopy (AFM), we imaged
                      human Tau fibrils at high resolution and simultaneously
                      mapped their mechanical and adhesive properties. Tau fibrils
                      showed a ≈ 16-nm-thick fuzzy coat that resembles a
                      two-layered polyelectrolyte brush, which is formed by the
                      unstructured short C-terminal and long N-terminal Tau
                      domains. The mechanical and adhesive properties of the fuzzy
                      coat are modulated by electrolytes and pH, and thus by the
                      cellular environment. These unique properties of the fuzzy
                      coat help in understanding how Tau fibrils disturb cellular
                      interactions and accumulate in neurofibrillary tangles.},
      keywords     = {Adhesiveness / Biomechanical Phenomena / Electrolytes:
                      chemistry / Humans / Hydrogen-Ion Concentration /
                      Microscopy, Atomic Force / Microscopy, Immunoelectron /
                      Models, Molecular / Protein Interaction Domains and Motifs /
                      Protein Multimerization / Recombinant Proteins: chemistry /
                      Recombinant Proteins: genetics / Recombinant Proteins:
                      ultrastructure / tau Proteins: chemistry / tau Proteins:
                      genetics / tau Proteins: physiology / tau Proteins:
                      ultrastructure / Electrolytes (NLM Chemicals) / MAPT
                      protein, human (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / tau Proteins (NLM Chemicals)},
      cin          = {AG (Eckhard) Mandelkow},
      ddc          = {500},
      cid          = {I:(DE-2719)1013014},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23269837},
      pmc          = {pmc:PMC3557036},
      doi          = {10.1073/pnas.1212100110},
      url          = {https://pub.dzne.de/record/136780},
}