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@ARTICLE{Ramirez:257684,
      author       = {Ramirez, Lisa Marie and Zweckstetter, Markus},
      title        = {{M}olecular-level interplay between intrinsically
                      disordered clients and {H}sp90.},
      journal      = {Current opinion in chemical biology},
      volume       = {74},
      issn         = {1367-5931},
      address      = {London},
      publisher    = {Current Biology Ltd.},
      reportid     = {DZNE-2023-00481},
      pages        = {102304},
      year         = {2023},
      abstract     = {Proteostasis is maintained by a network of molecular
                      chaperones, a prominent member of which is the 90-kilodalton
                      heat shock protein Hsp90. The chaperone function of Hsp90
                      has been extensively reviewed previously, emphasizing its
                      ATPase activity and remodeling of folded client proteins.
                      Experimental evidence implicating Hsp90 in neurodegenerative
                      diseases has bolstered interest in the noncanonical
                      chaperoning of intrinsically disordered protein (IDPs),
                      however the interplay between Hsp90 and its disordered
                      clients remains poorly understood. In this review we
                      describe recent advances that have contributed to our
                      understanding of the intricate mechanisms characterizing
                      Hsp90-mediated chaperoning of the IDPs tau and α-synuclein
                      and survey emerging insights into the modulation of the
                      chaperone-client interplay in the context of
                      neurodegeneration.},
      subtyp        = {Review Article},
      keywords     = {Humans / HSP90 Heat-Shock Proteins: metabolism / Molecular
                      Chaperones / Proteostasis / Intrinsically Disordered
                      Proteins: metabolism / Neurodegenerative Diseases /
                      α-Synuclein (Other) / α-Synuclein (Other) / Alzheimer's
                      disease (Other) / Heat shock protein (Other) / Hsp90 (Other)
                      / Structure (Other) / Tau (Other) / α-Synuclein (Other) /
                      HSP90 Heat-Shock Proteins (NLM Chemicals) / Molecular
                      Chaperones (NLM Chemicals) / Intrinsically Disordered
                      Proteins (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {570},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37068388},
      doi          = {10.1016/j.cbpa.2023.102304},
      url          = {https://pub.dzne.de/record/257684},
}