The gating mechanism in cyclic nucleotide-gated ion channels
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-18499-0.pdf
Reference48 articles.
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2. Berkefeld, H., Fakler, B. & Schulte, U. Ca2+-activated K+ channels: from protein complexes to function. Physiol. Rev. 90, 1437–1459 (2010).
3. Garneau, L. et al. Aromatic-aromatic interactions between residues in KCa3.1 pore helix and S5 transmembrane segment control the channel gating process. J. Gen. Physiol. 143, 289–307 (2014).
4. Suzuki, T., Hansen, A. & Sanguinetti, M. C. Hydrophobic interactions between the S5 segment and the pore helix stabilizes the closed state of Slo2.1 potassium channels. Biochim. Biophys. Acta 1858, 783–792 (2016).
5. Matulef, K. & Zagotta, W. N. Cyclic nucleotide-gated ion channels. Annu. Rev. Cell Dev. Biol. 19, 23–44 (2003).
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