María Isabel Niemeyer
Centro de Estudios Científicos
Valdivia 5110566
Chile
Name/email consistency: high
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)