The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Ion Channel Gating

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Ion Channel Gating

  • The mechanisms by which glycine acts on NMDA receptors are unknown, but single-channel recording experiments show an increase in opening frequency with no change in mean open time or conductance, suggesting that glycine could regulate transitions to states that are intermediate between binding of NMDA receptor agonists and ion-channel gating [1].
  • Simulations suggest that aniracetam either slows entry into a desensitized state or decreases the closing rate constant for ion channel gating [2].
  • The molecular events controlling glutamate receptor ion channel gating are complex [3].
  • We have identified a methionine residue (Met(823)) in the M4 domain of the NR2A subunit that regulates desensitization and ion channel gating [4].
  • Although ethanol is known to inhibit NMDA receptors by influencing ion-channel gating, its molecular site of action and the mechanism underlying this effect have not been established [5].

Biological context of Ion Channel Gating


Associations of Ion Channel Gating with chemical compounds


Gene context of Ion Channel Gating


  1. Regulation of NMDA receptor desensitization in mouse hippocampal neurons by glycine. Mayer, M.L., Vyklicky, L., Clements, J. Nature (1989) [Pubmed]
  2. Modulation of excitatory synaptic transmission by drugs that reduce desensitization at AMPA/kainate receptors. Vyklicky, L., Patneau, D.K., Mayer, M.L. Neuron (1991) [Pubmed]
  3. Conserved structural and functional control of N-methyl-D-aspartate receptor gating by transmembrane domain M3. Yuan, H., Erreger, K., Dravid, S.M., Traynelis, S.F. J. Biol. Chem. (2005) [Pubmed]
  4. A site in the fourth membrane-associated domain of the N-methyl-D-aspartate receptor regulates desensitization and ion channel gating. Ren, H., Honse, Y., Karp, B.J., Lipsky, R.H., Peoples, R.W. J. Biol. Chem. (2003) [Pubmed]
  5. A site of alcohol action in the fourth membrane-associated domain of the N-methyl-D-aspartate receptor. Ren, H., Honse, Y., Peoples, R.W. J. Biol. Chem. (2003) [Pubmed]
  6. An amino-acid substitution in the influenza-B NB protein affects ion-channel gating. Premkumar, A., Ewart, G.D., Cox, G.B., Gage, P.W. J. Membr. Biol. (2004) [Pubmed]
  7. Analysis of fractal ion channel gating kinetics: kinetic rates, energy levels, and activation energies. Liebovitch, L.S. Mathematical biosciences. (1989) [Pubmed]
  8. Statistical discrimination of fractal and Markov models of single-channel gating. Korn, S.J., Horn, R. Biophys. J. (1988) [Pubmed]
  9. Site-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating. Li, L., Lee, Y.H., Pappone, P., Palma, A., McNamee, M.G. Biophys. J. (1992) [Pubmed]
  10. Tryptophan substitutions reveal the role of nicotinic acetylcholine receptor alpha-TM3 domain in channel gating: differences between Torpedo and muscle-type AChR. Navedo, M., Nieves, M., Rojas, L., Lasalde-Dominicci, J.A. Biochemistry (2004) [Pubmed]
  11. The role of cystic fibrosis transmembrane conductance regulator phenylalanine 508 side chain in ion channel gating. Cui, L., Aleksandrov, L., Hou, Y.X., Gentzsch, M., Chen, J.H., Riordan, J.R., Aleksandrov, A.A. J. Physiol. (Lond.) (2006) [Pubmed]
  12. Sites in the fourth membrane-associated domain regulate alcohol sensitivity of the NMDA receptor. Honse, Y., Ren, H., Lipsky, R.H., Peoples, R.W. Neuropharmacology (2004) [Pubmed]
  13. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover. Aleksandrov, L., Aleksandrov, A.A., Chang, X.B., Riordan, J.R. J. Biol. Chem. (2002) [Pubmed]
  14. Ion-channel gating. Twist to open. Sansom, M.S. Curr. Biol. (1995) [Pubmed]
  15. A molecular envelope of the ligand-binding domain of a glutamate receptor in the presence and absence of agonist. Abele, R., Svergun, D., Keinänen, K., Koch, M.H., Madden, D.R. Biochemistry (1999) [Pubmed]
  16. Serotonin modulated Ca++ dependent K+ channels in alloimmune effector cell lytic function. Liepins, A., LeFever, A., Truitt, R.L. Immunopharmacology and immunotoxicology. (1989) [Pubmed]
WikiGenes - Universities