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@ARTICLE{Zabelskii:888237,
      author       = {Zabelskii, Dmitrii and Alekseev, Alexey and Kovalev, Kirill
                      and Rankovic, Vladan and Balandin, Taras and Soloviov,
                      Dmytro and Bratanov, Dmitry and Savelyeva, Ekaterina and
                      Podolyak, Elizaveta and Volkov, Dmytro and Vaganova,
                      Svetlana and Astashkin, Roman and Chizhov, Igor and Yutin,
                      Natalia and Rulev, Maksim and Popov, Alexander and
                      Eria-Oliveira, Ana-Sofia and Rokitskaya, Tatiana and Mager,
                      Thomas and Antonenko, Yuri and Rosselli, Riccardo and
                      Armeev, Grigoriy and Shaitan, Konstantin and Vivaudou,
                      Michel and Büldt, Georg and Rogachev, Andrey and
                      Rodriguez-Valera, Francisco and Kirpichnikov, Mikhail and
                      Moser, Tobias and Offenhäusser, Andreas and Willbold,
                      Dieter and Koonin, Eugene and Bamberg, Ernst and Gordeliy,
                      Valentin},
      title        = {{V}iral rhodopsins 1 are an unique family of light-gated
                      cation channels},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2020-04786},
      pages        = {5707},
      year         = {2020},
      abstract     = {Phytoplankton is the base of the marine food chain as well
                      as oxygen and carbon cycles and thus plays a global role in
                      climate and ecology. Nucleocytoplasmic Large DNA Viruses
                      that infect phytoplankton organisms and regulate the
                      phytoplankton dynamics encompass genes of rhodopsins of two
                      distinct families. Here, we present a functional and
                      structural characterization of two proteins of viral
                      rhodopsin group 1, OLPVR1 and VirChR1. Functional analysis
                      of VirChR1 shows that it is a highly selective,
                      Na+/K+-conducting channel and, in contrast to known cation
                      channelrhodopsins, it is impermeable to Ca2+ ions. We show
                      that, upon illumination, VirChR1 is able to drive neural
                      firing. The 1.4 Å resolution structure of OLPVR1 reveals
                      remarkable differences from the known channelrhodopsins and
                      a unique ion-conducting pathway. Thus, viral rhodopsins 1
                      represent a unique, large group of light-gated channels
                      (viral channelrhodopsins, VirChR1s). In nature, VirChR1s
                      likely mediate phototaxis of algae enhancing the host
                      anabolic processes to support virus reproduction, and
                      therefore, might play a major role in global phytoplankton
                      dynamics. Moreover, VirChR1s have unique potential for
                      optogenetics as they lack possibly noxious Ca2+
                      permeability.},
      cin          = {IBI-7 / IBI-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBI-3-20200312},
      pnm          = {581 - Biotechnology (POF3-581) / 552 - Engineering Cell
                      Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-581 / G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33177509},
      UT           = {WOS:000593975100009},
      doi          = {10.1038/s41467-020-19457-7},
      url          = {https://juser.fz-juelich.de/record/888237},
}