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@ARTICLE{Reichhart:860976,
      author       = {Reichhart, Nadine and Schöberl, Simon and Keckeis, Susanne
                      and Alfaar, Ahmad S. and Roubeix, Christophe and Cordes,
                      Magdalena and Crespo-Garcia, Sergio and Haeckel, Akvile and
                      Kociok, Norbert and Föckler, Renate and Fels, Gabriele and
                      Mataruga, Anja and Rauh, Robert and Milenkovic, Vladimir M.
                      and Zühlke, Kerstin and Klussmann, Enno and Schellenberger,
                      Eyk and Strauß, Olaf},
      title        = {{A}noctamin-4 is a bona fide {C}a2+-dependent non-selective
                      cation channel},
      journal      = {Scientific reports},
      volume       = {9},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2019-01609},
      pages        = {2257},
      year         = {2019},
      abstract     = {Changes in cell function occur by specific patterns of
                      intracellular Ca2+, activating Ca2+-sensitive proteins. The
                      anoctamin (TMEM16) protein family has Ca2+-dependent ion
                      channel activity, which provides transmembrane ion
                      transport, and/or Ca2+-dependent phosphatidyl-scramblase
                      activity. Using amino acid sequence analysis combined with
                      measurements of ion channel function, we clarified the so
                      far unknown Ano4 function as Ca2+-dependent, non-selective
                      monovalent cation channel; heterologous Ano4 expression in
                      HEK293 cells elicits Ca2+ activated conductance with weak
                      selectivity of K+ > Na+ > Li+. Endogenously
                      expressed Ca2+-dependent cation channels in the retinal
                      pigment epithelium were identified as Ano4 by KO
                      mouse-derived primary RPE cells and siRNA against Ano4.
                      Exchanging a negatively charged amino acid in the putative
                      pore region (AA702–855) into a positive one (E775K) turns
                      Ano4-elicited currents into Cl− currents evidencing its
                      importance for ion selectivity. The molecular identification
                      of Ano4 as a Ca2+-activated cation channel advances the
                      understanding of its role in Ca2+ signaling.},
      cin          = {ICS-4},
      ddc          = {600},
      cid          = {I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30783137},
      UT           = {WOS:000459092800027},
      doi          = {10.1038/s41598-018-37287-y},
      url          = {https://juser.fz-juelich.de/record/860976},
}