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@ARTICLE{Bickel:864930,
      author       = {Bickel, David and Gohlke, Holger},
      title        = {{C}-terminal {M}odulators of {H}eat {S}hock {P}rotein of 90
                      k{D}a ({HSP}90): {S}tate of {D}evelopment and {M}odes of
                      {A}ction},
      journal      = {Bioorganic $\&$ medicinal chemistry},
      volume       = {27},
      number       = {21},
      issn         = {0968-0896},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2019-04533},
      pages        = {115080},
      year         = {2019},
      abstract     = {Cells constantly need to adopt to changing environmental
                      conditions, maintaining homeostasis and proteostasis. Heat
                      shock proteins are a diverse class of molecular chaperones
                      that assist proteins in folding to prevent stress-induced
                      misfolding and aggregation. The heat shock protein of 90 kDa
                      (HSP90) is the most abundant heat shock protein. While basal
                      expression of HSP90 is essential for cell survival, in many
                      tumors elevated HSP90 levels are found, which is often
                      associated with bad prognosis. Therefore, HSP90 has emerged
                      as a major target in tumor therapy. The HSP90 machinery is
                      very complex in that it involves large conformational
                      changes during the chaperoning cycle and a variety of
                      co-chaperones. At the same time, this complexity offers a
                      plethora of possibilities to interfere with HSP90 function.
                      The best characterized class of HSP90 modulators are
                      competitive inhibitors targeting the N-terminal ATP-binding
                      pocket. Nineteen compounds of this class entered clinical
                      trials. However, due to severe adverse effects, including
                      induction of the heat shock response, no N-terminal
                      inhibitor has been approved by the FDA so far. As
                      alternatives, compounds commonly referred to as
                      “C-terminal inhibitors” have been developed, either as
                      natural product-based analogues or by rational design, which
                      employ multiple mechanisms to modulate HSP90 function,
                      including modulation of the interaction with co-chaperones,
                      induction of conformational changes that influence the
                      chaperoning cycle, or inhibition of C-terminal dimerization.
                      In this review, we summarize the current development state
                      of characteristic C-terminal inhibitors, with an emphasis on
                      their (proposed) molecular modes of action and binding
                      sites.},
      cin          = {JSC / NIC / ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31519378},
      UT           = {WOS:000488203800001},
      doi          = {10.1016/j.bmc.2019.115080},
      url          = {https://juser.fz-juelich.de/record/864930},
}