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@ARTICLE{Pickhardt:138183,
      author       = {Pickhardt, Marcus and Neumann, Thomas and Schwizer, Daniel
                      and Callaway, Kari and Vendruscolo, Michele and Schenk, Dale
                      and St George-Hyslop, Peter and Mandelkow, Eva M and Dobson,
                      Christopher M and McConlogue, Lisa and Mandelkow, Eckhard
                      and Tóth, Gergely},
      title        = {{I}dentification of {S}mall {M}olecule {I}nhibitors of
                      {T}au {A}ggregation by {T}argeting {M}onomeric {T}au {A}s a
                      {P}otential {T}herapeutic {A}pproach for {T}auopathies.},
      journal      = {Current Alzheimer research},
      volume       = {12},
      number       = {9},
      issn         = {1567-2050},
      address      = {Hilversum},
      publisher    = {Bentham Science Publ. Ltd.},
      reportid     = {DZNE-2020-04505},
      pages        = {814-828},
      year         = {2015},
      abstract     = {A potential strategy to alleviate the aggregation of
                      intrinsically disordered proteins (IDPs) is to maintain the
                      native functional state of the protein by small molecule
                      binding. However, the targeting of the native state of IDPs
                      by small molecules has been challenging due to their
                      heterogeneous conformational ensembles. To tackle this
                      challenge, we applied a high-throughput chemical microarray
                      surface plasmon resonance imaging screen to detect the
                      binding between small molecules and monomeric full-length
                      Tau, a protein linked with the onset of a range of
                      Tauopathies. The screen identified a novel set of drug-like
                      fragment and lead-like compounds that bound to Tau. We
                      verified that the majority of these hit compounds reduced
                      the aggregation of different Tau constructs in vitro and in
                      N2a cells. These results demonstrate that Tau is a viable
                      receptor of drug-like small molecules. The drug discovery
                      approach that we present can be applied to other IDPs linked
                      to other misfolding diseases such as Alzheimer's and
                      Parkinson's diseases.},
      keywords     = {Animals / Benzothiazoles / Cell Line, Tumor / Cell
                      Survival: drug effects / Dose-Response Relationship, Drug /
                      Drug Evaluation, Preclinical / Fluorescent Dyes /
                      High-Throughput Screening Assays / Humans / Mice /
                      Microarray Analysis / Microscopy, Fluorescence / Molecular
                      Structure / Neuroprotective Agents: chemistry /
                      Neuroprotective Agents: pharmacology / Protein Aggregates:
                      drug effects / Protein Multimerization: drug effects /
                      Tauopathies: drug therapy / Tauopathies: metabolism /
                      Thiazoles / tau Proteins: genetics / tau Proteins:
                      metabolism / Benzothiazoles (NLM Chemicals) / Fluorescent
                      Dyes (NLM Chemicals) / MAPT protein, human (NLM Chemicals) /
                      Neuroprotective Agents (NLM Chemicals) / Protein Aggregates
                      (NLM Chemicals) / Thiazoles (NLM Chemicals) / tau Proteins
                      (NLM Chemicals) / thioflavin T (NLM Chemicals)},
      cin          = {AG Mandelkow 1 / AG Mandelkow 2},
      ddc          = {610},
      cid          = {I:(DE-2719)1013014 / 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:26510979},
      pmc          = {pmc:PMC4976804},
      doi          = {10.2174/156720501209151019104951},
      url          = {https://pub.dzne.de/record/138183},
}