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@ARTICLE{Lorenz:864631,
      author       = {Lorenz, Charlotte and Ince, Semra and Zhang, Tao and
                      Cousin, Anneliese and Batra‐Safferling, Renu and
                      Nagel‐Steger, Luitgard and Herrmann, Christian and
                      Stadler, Andreas M.},
      title        = {{F}arnesylation of human guanylate‐binding protein 1 as
                      safety mechanism preventing structural rearrangements and
                      uninduced dimerization},
      journal      = {The FEBS journal},
      volume       = {287},
      number       = {3},
      issn         = {1742-4658},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2019-04336},
      pages        = {496-514},
      year         = {2020},
      abstract     = {Human guanylate‐binding protein 1 (hGBP1) belongs to the
                      family of dynamin‐like proteins and is activated by
                      addition of nucleotides, leading to protein oligomerization
                      and stimulated GTPase activity. In vivo, hGBP1 is
                      post‐translationally modified by attachment of a farnesyl
                      group yielding farn‐hGBP1. In this study, hydrodynamic
                      differences in farn‐hGBP1 and unmodified hGBP1 were
                      investigated using dynamic light scattering (DLS),
                      analytical ultracentrifugation (AUC) and analytical
                      size‐exclusion chromatography (SEC). In addition, we
                      performed small‐angle X‐ray scattering (SAXS)
                      experiments coupled with a SEC setup (SEC‐SAXS) to
                      investigate structural properties of nonmodified hGBP1 and
                      farn‐hGBP1 in solution. SEC‐SAXS measurements revealed
                      that farnesylation keeps hGBP1 in its inactive monomeric and
                      crystal‐like conformation in nucleotide‐free solution,
                      whereas unmodified hGBP1 forms a monomer–dimer equilibrium
                      both in the inactive ground state in nucleotide‐free
                      solution as well as in the activated state that is trapped
                      by addition of the nonhydrolysable GTP analogue GppNHp.
                      Nonmodified hGBP1 is structurally perturbed as compared to
                      farn‐hGBP. In particular, GppNHp binding leads to large
                      structural rearrangements and higher conformational
                      flexibility of the monomer and the dimer. Structural changes
                      observed in the nonmodified protein are prerequisites for
                      further oligomer assemblies of farn‐hGBP1 that occur in
                      the presence of nucleotides.},
      cin          = {JCNS-1 / ICS-1 / ICS-6},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31330084},
      UT           = {WOS:000479584400001},
      doi          = {10.1111/febs.15015},
      url          = {https://juser.fz-juelich.de/record/864631},
}