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@ARTICLE{Oroz:139178,
      author       = {Oroz, Javier and Kim, Jin Hae and Chang, Bliss J and
                      Zweckstetter, Markus},
      title        = {{M}echanistic basis for the recognition of a misfolded
                      protein by the molecular chaperone {H}sp90.},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {24},
      number       = {4},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2020-05500},
      pages        = {407-413},
      year         = {2017},
      abstract     = {The critical toxic species in over 40 human diseases are
                      misfolded proteins. Their interaction with molecular
                      chaperones such as Hsp90, which preferentially interacts
                      with metastable proteins, is essential for the blocking of
                      disease progression. Here we used nuclear magnetic resonance
                      (NMR) spectroscopy to determine the three-dimensional
                      structure of the misfolded cytotoxic monomer of the
                      amyloidogenic human protein transthyretin, which is
                      characterized by the release of the C-terminal β-strand and
                      perturbations of the A-B loop. The misfolded transthyretin
                      monomer, but not the wild-type protein, binds to human
                      Hsp90. In the bound state, the Hsp90 dimer predominantly
                      populates an open conformation, and transthyretin retains
                      its globular structure. The interaction surface for the
                      transthyretin monomer comprises the N-terminal and middle
                      domains of Hsp90 and overlaps with that of the
                      Alzheimer's-disease-related protein tau. Taken together, the
                      data suggest that Hsp90 uses a mechanism for the recognition
                      of aggregation-prone proteins that is largely distinct from
                      those of other Hsp90 clients.},
      keywords     = {HSP90 Heat-Shock Proteins: chemistry / HSP90 Heat-Shock
                      Proteins: metabolism / Humans / Imaging, Three-Dimensional /
                      Intrinsically Disordered Proteins: chemistry / Intrinsically
                      Disordered Proteins: metabolism / Magnetic Resonance
                      Spectroscopy / Models, Biological / Models, Molecular /
                      Molecular Chaperones: chemistry / Molecular Chaperones:
                      metabolism / Prealbumin: chemistry / Prealbumin: metabolism
                      / Protein Binding / Protein Conformation / Protein Folding /
                      Protein Multimerization / tau Proteins: chemistry / tau
                      Proteins: metabolism / HSP90 Heat-Shock Proteins (NLM
                      Chemicals) / Intrinsically Disordered Proteins (NLM
                      Chemicals) / Molecular Chaperones (NLM Chemicals) /
                      Prealbumin (NLM Chemicals) / tau Proteins (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {570},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28218749},
      doi          = {10.1038/nsmb.3380},
      url          = {https://pub.dzne.de/record/139178},
}