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@ARTICLE{HoangGia:907384,
      author       = {Hoang Gia, Linh and Goßen, Jonas and Capelli, Riccardo and
                      Nguyen, Toan T. and Sun, Zhaoxi and Zuo, Ke and Schulz,
                      Jörg B. and Rossetti, Giulia and Carloni, Paolo},
      title        = {{M}ultiple {P}oses and {T}hermodynamics of {L}igands
                      {T}argeting {P}rotein {S}urfaces: {T}he {C}ase of
                      {F}urosemide {B}inding to mito{NEET} in {A}queous
                      {S}olution},
      journal      = {Frontiers in cell and developmental biology},
      volume       = {10},
      issn         = {2296-634X},
      address      = {Lausanne},
      publisher    = {Frontiers Media},
      reportid     = {FZJ-2022-02005},
      pages        = {886568},
      year         = {2022},
      abstract     = {Human NEET proteins, such as NAF-1 and mitoNEET, are
                      homodimeric, redox iron-sulfur proteins characterized by
                      triple cysteine and one histidine-coordinated [2Fe-2S]
                      cluster. They exist in an oxidized and reduced state.
                      Abnormal release of the cluster is implicated in a variety
                      of diseases, including cancer and neurodegeneration. The
                      computer-aided and structure-based design of ligands
                      affecting cluster release is of paramount importance from a
                      pharmaceutical perspective. Unfortunately, experimental
                      structural information so far is limited to only one
                      ligand/protein complex. This is the X-ray structure of
                      furosemide bound to oxidized mitoNEET. Here we employ an
                      enhanced sampling approach, Localized Volume-based
                      Metadynamics, developed by some of us, to identify binding
                      poses of furosemide to human mitoNEET protein in solution.
                      The binding modes show a high variability within the same
                      shallow binding pocket on the protein surface identified in
                      the X-ray structure. Among the different binding
                      conformations, one of them is in agreement with the crystal
                      structure’s one. This conformation might have been
                      overstabilized in the latter because of the presence of
                      crystal packing interactions, absent in solution. The
                      calculated binding affinity is compatible with experimental
                      data. Our protocol can be used in a straightforward manner
                      in drug design campaigns targeting this pharmaceutically
                      important family of proteins.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {5252 - Brain Dysfunction and Plasticity (POF4-525) / 5251 -
                      Multilevel Brain Organization and Variability (POF4-525) /
                      5111 - Domain-Specific Simulation Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / DFG project
                      291198853 - FOR 2518: Funktionale Dynamik von Ionenkanälen
                      und Transportern - DynIon -},
      pid          = {G:(DE-HGF)POF4-5252 / G:(DE-HGF)POF4-5251 /
                      G:(DE-HGF)POF4-5111 / G:(GEPRIS)291198853},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000795047600001},
      doi          = {10.3389/fcell.2022.886568},
      url          = {https://juser.fz-juelich.de/record/907384},
}