@article{12925,
  abstract     = {Normal function of organs and cells is tightly linked to the cytoarchitecture. Control of the cell volume is therefore vital for the organism. A widely established strategy of cells to counteract swelling is the activation of chloride and potassium channels, which leads to a net efflux of salt followed by water - a process termed regulatory volume decrease. Since there is evidence for swelling-dependent chloride channels (IClswell) being activated also during pathological processes, the identification of the molecular entity underlying IClswell is of utmost importance. Several proteins are discussed as the channel forming IClswell, i.e. phospholemman, p-glycoprotein, CLC-3 and ICln. In this review we would like to focus on the properties of ICln, a protein cloned from a Madin Darby canine kidney (MDCK) cell library whose expression in Xenopus laevis oocytes resulted in a nucleotide sensitive outwardly rectifying chloride current closely resembling the biophysical properties of IClswell.},
  author       = {Fürst, Johannes and Jakab, Martin and König, Matthias and Ritter, Markus and Gschwentner, Martin and Rudzki, Jakob and Danzl, Johann G and Mayer, Michael and Burtscher, Carmen M. and Schirmer, Julia and Maier, Brigitte and Nairz, Manfred and Chwatal, Sabine and Paulmichl, Markus},
  issn         = {1015-8987},
  journal      = {Cellular Physiology and Biochemistry},
  keywords     = {Physiology},
  number       = {5-6},
  pages        = {329--334},
  publisher    = {S. Karger AG},
  title        = {{Structure and Function of the Ion Channel ICln}},
  doi          = {10.1159/000016374},
  volume       = {10},
  year         = {2000},
}

@article{3473,
  abstract     = {Sixteen different K+ channel subtypes have been cloned from mammalian tissue. Considering their sequence homology to Drosophila Shaker, Shab, Shaw and Shal channels, they were classified into four corresponding classes Kv1-4. All K+ channels belonging to these classes consist of four subunits with each six hydrophobic segments (S1-S6) and a characteristic structure-function relationship of certain domains in their amino acid sequence. These domains are, the inactivation gate in the N-terminal region of the sequence, the voltage sensor in the fourth hydrophobic segment (S4), and the pore-region in the H5 segment between S5 and S6. In some functional properties K+ channels cloned from the mammalian brain, however, differ from Drosophila K+ channels. These are pharmacological differences, differences in the threshold of activation and in regulation of inactivation. Part of these differences are important to understand their physiological role in the brain. Based on their functional characteristics the expression pattern of cloned K+ channels in the rat brain can be correlated with the properties of K+ currents measured in central neurones.},
  author       = {Ruppersberg, Peter and Ermler, Mamfred and Knopf, Martin and Kues, Wilfried and Jonas, Peter M and Koenen, Michael},
  issn         = {1015-8987},
  journal      = {Cellular Physiology and Biochemistry},
  pages        = {250 -- 269},
  publisher    = {S. Karger AG},
  title        = {{Properties of Shaker-homologous potassium channels expressed in the mammalian brain.}},
  doi          = {10.1159/000154691},
  volume       = {3},
  year         = {1993},
}