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@ARTICLE{Pesce:838842,
      author       = {Pesce, Luca and Calandrini, Vania and Marjault,
                      Henri-Baptiste and Lipper, Colin H. and Rossetti, Giulia and
                      Mittler, Ron and Jennings, Patricia Ann and Nechushtai,
                      Rachel and Carloni, Paolo and Bauer, Andreas},
      title        = {{M}olecular {D}ynamics {S}imulations of the [2{F}e-2{S}]
                      {C}luster-{B}inding {D}omain of {NEET} {P}roteins {R}eveal
                      {K}ey {M}olecular {D}eterminants {T}hat {I}nduce {T}heir
                      {C}luster {T}ransfer/{R}elease},
      journal      = {The journal of physical chemistry / B},
      volume       = {121},
      number       = {47},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-07352},
      pages        = {10648–10656},
      year         = {2017},
      abstract     = {The NEET proteins are a novel family of iron-sulfur
                      proteins characterized by an unusual 3 cysteine and one
                      histidine coordinated [2Fe-2S] cluster. Aberrant cluster
                      release, dictated by the breakage of the Fe-N bond, is
                      implicated in a variety of human diseases, including cancer
                      and neurodegenerative diseases. Here molecular dynamics in
                      the multi-μs timescale, along with quantum chemical
                      calculations, on two representative members of the family
                      (the human NAF-1 and mitoNEET proteins) show that the loss
                      of the cluster is associated with a dramatic decrease of
                      secondary and tertiary structure. In addition, the
                      calculations provide a mechanism for cluster release and
                      clarify, for the first time, crucial differences existing
                      between the two proteins, which are reflected in the
                      experimentally observed difference in pH-dependent cluster
                      reactivity. The reliability of our conclusions is
                      established by an extensive comparison with NMR data of the
                      proteins in solution, in part measured in this work.},
      cin          = {IAS-5 / INM-9 / JARA-HPC / JSC / INM-2},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      $I:(DE-82)080012_20140620$ / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)INM-2-20090406},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511) /
                      Predicting the apo-structure of a NEET protein involved in
                      health and disease $(jias57_20161101)$},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511 /
                      $G:(DE-Juel1)jias57_20161101$},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000417228600006},
      doi          = {10.1021/acs.jpcb.7b10584},
      url          = {https://juser.fz-juelich.de/record/838842},
}