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@ARTICLE{Eckei:830504,
      author       = {Eckei, Laura and Krieg, Sarah and Bütepage, Mareike and
                      Lehmann, Anne and Gross, Annika and Lippok, Barbara and
                      Grimm, Alexander R. and Kümmerer, Beate M. and Rossetti,
                      Giulia and Lüscher, Bernhard and Verheugd, Patricia},
      title        = {{T}he conserved macrodomains of the non-structural proteins
                      of {C}hikungunya virus and other pathogenic positive strand
                      {RNA} viruses function as mono-{ADP}-ribosylhydrolases},
      journal      = {Scientific reports},
      volume       = {7},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-04045},
      pages        = {41746 -},
      year         = {2017},
      abstract     = {Human pathogenic positive single strand RNA ((+)ssRNA)
                      viruses, including Chikungunya virus, pose severe health
                      problems as for many neither efficient vaccines nor
                      therapeutic strategies exist. To interfere with propagation,
                      viral enzymatic activities are considered potential targets.
                      Here we addressed the function of the viral macrodomains,
                      conserved folds of non-structural proteins of many (+)ssRNA
                      viruses. Macrodomains are closely associated with ADP-ribose
                      function and metabolism. ADP-ribosylation is a
                      post-translational modification controlling various cellular
                      processes, including DNA repair, transcription and stress
                      response. We found that the viral macrodomains possess broad
                      hydrolase activity towards mono-ADP-ribosylated substrates
                      of the mono-ADP-ribosyltransferases ARTD7, ARTD8 and ARTD10
                      (aka PARP15, PARP14 and PARP10, respectively), reverting
                      this post-translational modification both in vitro and in
                      cells. In contrast, the viral macrodomains possess only weak
                      activity towards poly-ADP-ribose chains synthesized by ARTD1
                      (aka PARP1). Unlike poly-ADP-ribosylglycohydrolase, which
                      hydrolyzes poly-ADP-ribose chains to individual ADP-ribose
                      units but cannot cleave the amino acid side chain -
                      ADP-ribose bond, the different viral macrodomains release
                      poly-ADP-ribose chains with distinct efficiency. Mutational
                      and structural analyses identified key amino acids for
                      hydrolase activity of the Chikungunya viral macrodomain.
                      Moreover, ARTD8 and ARTD10 are induced by innate immune
                      mechanisms, suggesting that the control of
                      mono-ADP-ribosylation is part of a host-pathogen conflict.},
      cin          = {IAS-5 / INM-9 / JSC},
      ddc          = {000},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121 /
                      I:(DE-Juel1)JSC-20090406},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000393651900001},
      pubmed       = {pmid:28150709},
      doi          = {10.1038/srep41746},
      url          = {https://juser.fz-juelich.de/record/830504},
}