% 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{Krger:138382,
      author       = {Krüger, Lars and Mandelkow, Eva Maria},
      title        = {{T}au neurotoxicity and rescue in animal models of human
                      {T}auopathies.},
      journal      = {Current opinion in neurobiology},
      volume       = {36},
      issn         = {0959-4388},
      address      = {Philadelphia, Pa.},
      publisher    = {Current Biology},
      reportid     = {DZNE-2020-04704},
      pages        = {52-58},
      year         = {2016},
      abstract     = {Pathological Tau is a hallmark of various neuronal
                      disorders and spreads in the brain of Alzheimer patients in
                      a well-defined manner. Beside Tau's main function in
                      stabilizing microtubules for axonal transport, a variety of
                      novel functions for neurons and glia have emerged recently.
                      Tau regulates the susceptibility to hyperexcitation and
                      plays a role in neuron-glia contact formation. Studies
                      implicate soluble oligomeric species of Tau, rather than
                      insoluble aggregates, as more detrimental to proper neuronal
                      function. Tau is not exclusively intracellular; instead Tau
                      can be released into the extracellular space. This has led
                      to the hypothesis of a prion-disease like mechanism to
                      explain the stereotypical progression of Tau. Targeting
                      pathological Tau with antibodies or aggregation inhibitors
                      may help to prevent pathology.},
      subtyp        = {Review Article},
      keywords     = {Animals / Antibodies: pharmacology / Brain: metabolism /
                      Brain: physiopathology / Disease Models, Animal / Disease
                      Susceptibility / Humans / Mice / Presynaptic Terminals:
                      metabolism / Protein Aggregates: drug effects / Protein
                      Aggregation, Pathological: metabolism / Protein Aggregation,
                      Pathological: physiopathology / Tauopathies: metabolism /
                      Tauopathies: physiopathology / tau Proteins: metabolism /
                      Antibodies (NLM Chemicals) / Protein Aggregates (NLM
                      Chemicals) / tau Proteins (NLM Chemicals)},
      cin          = {TT / AG Mandelkow 2},
      ddc          = {610},
      cid          = {I:(DE-2719)1030028 / I:(DE-2719)1013015},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26431808},
      doi          = {10.1016/j.conb.2015.09.004},
      url          = {https://pub.dzne.de/record/138382},
}