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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

María Isabel Niemeyer

Centro de Estudios Científicos

Valdivia 5110566



Name/email consistency: high



  • Centro de Estudios Científicos, Valdivia 5110566, Chile. 2001 - 2010
  • Centro de Estudios Cientificos, Av. Arturo Prat 514, Casilla 1469, Valdivia, Chile. 2001 - 2007


  1. Separate gating mechanisms mediate the regulation of K2P potassium channel TASK-2 by intra- and extracellular pH. Niemeyer, M.I., Cid, L.P., Peña-Münzenmayer, G., Sepúlveda, F.V. J. Biol. Chem. (2010) [Pubmed]
  2. Neutralization of a single arginine residue gates open a two-pore domain, alkali-activated K+ channel. Niemeyer, M.I., González-Nilo, F.D., Zúñiga, L., González, W., Cid, L.P., Sepúlveda, F.V. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  3. Gating of two-pore domain K+ channels by extracellular pH. Niemeyer, M.I., González-Nilo, F.D., Zúñiga, L., González, W., Cid, L.P., Sepúlveda, F.V. Biochem. Soc. Trans. (2006) [Pubmed]
  4. Extracellular conserved cysteine forms an intersubunit disulphide bridge in the KCNK5 (TASK-2) K+ channel without having an essential effect upon activity. Niemeyer, M.I., Cid, L.P., Valenzuela, X., Paeile, V., Sepúlveda, F.V. Mol. Membr. Biol. (2003) [Pubmed]
  5. A voltage-independent K+ conductance activated by cell swelling in Ehrlich cells is modulated by a G-protein-mediated process. Niemeyer, M.I., Stutzin, A., Sepúlveda, F.V. Biochim. Biophys. Acta (2002) [Pubmed]
  6. Modulation of the two-pore domain acid-sensitive K+ channel TASK-2 (KCNK5) by changes in cell volume. Niemeyer, M.I., Cid, L.P., Barros, L.F., Sepúlveda, F.V. J. Biol. Chem. (2001) [Pubmed]
  7. K+ conductance activated during regulatory volume decrease. The channels in Ehrlich cells and their possible molecular counterpart. Niemeyer, M.I., Cid, L.P., Sepúlveda, F.V. Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. (2001) [Pubmed]
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