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XB-ART-24003
Biochem Biophys Res Commun 1992 Feb 14;1823:1089-93.
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In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeability.

Curutchet P, Bochet P, Prado de Carvalho L, Lambolez B, Stinnakre J, Rossier J.


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Recent papers have described glutamine to arginine point mutations of the cloned AMPA/Kainate receptor subunits that alter current-voltage relationship and suppress Ca2+ permeability, thus linking these two characteristics. We describe a glutamine to histidine mutation at the same position, which alters current-voltage relationship but retains Ca2+ permeability, thus dissociating the two properties.

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Species referenced: Xenopus laevis
Genes referenced: gria1