% 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{Liedgens:874920,
      author       = {Liedgens, Linda and Zimmermann, Jannik and Wäschenbach,
                      Lucas and Geissel, Fabian and Laporte, Hugo and Gohlke,
                      Holger and Morgan, Bruce and Deponte, Marcel},
      title        = {{Q}uantitative assessment of the determinant structural
                      differences between redox-active and inactive glutaredoxins},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2020-01704},
      pages        = {1725},
      year         = {2020},
      abstract     = {Class I glutaredoxins are enzymatically active,
                      glutathione-dependent oxidoreductases, whilst class II
                      glutaredoxins are typically enzymatically inactive, Fe-S
                      cluster-binding proteins. Enzymatically active glutaredoxins
                      harbor both a glutathione-scaffold site for reacting with
                      glutathionylated disulfide substrates and a
                      glutathione-activator site for reacting with reduced
                      glutathione. Here, using yeast ScGrx7 as a model protein, we
                      comprehensively identified and characterized key residues
                      from four distinct protein regions, as well as the
                      covalently bound glutathione moiety, and quantified their
                      contribution to both interaction sites. Additionally, we
                      developed a redox-sensitive GFP2-based assay, which allowed
                      the real-time assessment of glutaredoxin structure-function
                      relationships inside living cells. Finally, we employed this
                      assay to rapidly screen multiple glutaredoxin mutants,
                      ultimately enabling us to convert enzymatically active and
                      inactive glutaredoxins into each other. In summary, we have
                      gained a comprehensive understanding of the mechanistic
                      underpinnings of glutaredoxin catalysis and have elucidated
                      the determinant structural differences between the two main
                      classes of glutaredoxins.},
      cin          = {NIC / JSC / IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$ /
                      Targeting spectrin redox switches to regulate the
                      mechanoproperties of red blood cells $(hdd19_20171101)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$ /
                      $G:(DE-Juel1)hdd19_20171101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32265442},
      UT           = {WOS:000526532500003},
      doi          = {10.1038/s41467-020-15441-3},
      url          = {https://juser.fz-juelich.de/record/874920},
}