% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Zeng:856050,
      author       = {Zeng, Juan and Guareschi, Riccardo and Damre, Mangesh and
                      Cao, Ruyin and Kless, Achim and Neumaier, Bernd and Bauer,
                      Andreas and Giorgetti, Alejandro and Carloni, Paolo and
                      Rossetti, Giulia},
      title        = {{S}tructural {P}rediction of the {D}imeric {F}orm of the
                      {M}ammalian {T}ranslocator {M}embrane {P}rotein {TSPO}: {A}
                      {K}ey {T}arget for {B}rain {D}iagnostics},
      journal      = {International journal of molecular sciences},
      volume       = {19},
      number       = {9},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2018-05717},
      pages        = {2588 -},
      year         = {2018},
      abstract     = {Positron emission tomography (PET) radioligands targeting
                      the human translocatormembrane protein (TSPO) are broadly
                      used for the investigations of neuroinflammatory
                      conditionsassociated with neurological disorders. Structural
                      information on the mammalian proteinhomodimers—the
                      suggested functional state of the protein—is limited to a
                      solid-state nuclearmagnetic resonance (NMR) study and to a
                      model based on the previously-deposited solution
                      NMRstructure of the monomeric mouse protein. Computational
                      studies performed here suggest thatthe NMR-solved structure
                      in the presence of detergents is not prone to dimer
                      formation and isfurthermore unstable in its native membrane
                      environment. We, therefore, propose a new modelof the
                      functionally-relevant dimeric form of the mouse protein,
                      based on a prokaryotic homologue.The model, fully consistent
                      with solid-state NMR data, is very different from the
                      previous predictions.Hence, it provides, for the first time,
                      structural insights into this pharmaceutically-important
                      targetwhich are fully consistent with experimental data.},
      cin          = {INM-9 / INM-5 / INM-2 / IAS-5 / JSC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)INM-5-20090406 /
                      I:(DE-Juel1)INM-2-20090406 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {573 - Neuroimaging (POF3-573) / 531 - Condensed Matter and
                      Molecular Building Blocks (POF3-531) / 571 - Connectivity
                      and Activity (POF3-571) / 511 - Computational Science and
                      Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-573 / G:(DE-HGF)POF3-531 /
                      G:(DE-HGF)POF3-571 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30200318},
      UT           = {WOS:000449988100124},
      doi          = {10.3390/ijms19092588},
      url          = {https://juser.fz-juelich.de/record/856050},
}