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@ARTICLE{Mashaghi:182844,
      author       = {A. Mashaghi and F. Moayed and E. J. Koers and Y. Zheng and
                      K. Till and G. Kramer$^*$ and M. P. Mayer and S. J. Tans},
      title        = {{D}irect observation of {H}sp90-induced compaction in a
                      protein chain.},
      journal      = {Cell reports},
      volume       = {41},
      number       = {9},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2022-02969},
      pages        = {111734},
      year         = {2022},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {The chaperone heat shock protein 90 (Hsp90) is well known
                      to undergo important conformational changes, which depend on
                      nucleotide and substrate interactions. Conversely, how the
                      conformations of its unstable and disordered substrates are
                      affected by Hsp90 is difficult to address experimentally yet
                      is central to its function. Here, using optical tweezers, we
                      find that Hsp90 promotes local contractions in unfolded
                      chains that drive their global compaction down to dimensions
                      of folded states. This compaction has a gradual nature while
                      showing small steps, is stimulated by ATP, and performs
                      mechanical work against counteracting forces that expand the
                      chain dimensions. The Hsp90 interactions suppress the
                      formation of larger-scale folded, misfolded, and aggregated
                      structures. The observations support a model in which Hsp90
                      alters client conformations directly by promoting local
                      intra-chain interactions while suppressing distant ones. We
                      conjecture that chain compaction may be central to how Hsp90
                      protects unstable clients and cooperates with Hsp70.},
      keywords     = {CP: Molecular biology (Other) / HSP90 (Other) / chaperone
                      (Other) / conformational heterogeneity (Other) / optical
                      tweezers (Other) / protein chain compaction (Other)},
      cin          = {A250},
      ddc          = {610},
      cid          = {I:(DE-He78)A250-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36450251},
      doi          = {10.1016/j.celrep.2022.111734},
      url          = {https://inrepo02.dkfz.de/record/182844},
}