Dani_1995_Curr.Opin.Neurobiol_5_310

Reference

Title : Structure and function of glutamate and nicotinic acetylcholine receptors - Dani_1995_Curr.Opin.Neurobiol_5_310
Author(s) : Dani JA , Mayer ML
Ref : Current Opinion in Neurobiology , 5 :310 , 1995
Abstract :

The past year has seen remarkable progress in defining the structure of various ligand-gated ion channels. Images of opened and closed nicotinic acetylcholine receptors at 9 A resolution have now made it easier to identify the conformational changes underlying gating. In addition, recent studies on glutamate receptors have led to a radical revision of their postulated transmembrane topology: models for agonist-binding and allosteric domains now use sites previously thought to lie in cytoplasmic loops. Other areas that are being actively pursued include identification of the amino acids lining the ion channels, accurate measurements of Ca2+ fluxes, and tests of transmembrane topology in kainate receptor subunits.

PubMedSearch : Dani_1995_Curr.Opin.Neurobiol_5_310
PubMedID: 7580153

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Citations formats

Dani JA, Mayer ML (1995)
Structure and function of glutamate and nicotinic acetylcholine receptors
Current Opinion in Neurobiology 5 :310

Dani JA, Mayer ML (1995)
Current Opinion in Neurobiology 5 :310