在谷氨酸受体1（GluR1）亚基中，谷氨酰胺到组氨酸的点突变可抑制内向整流，但不影响钙通透性。
In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeability.
作者信息
Curutchet P, Bochet P, Prado de Carvalho L, Lambolez B, Stinnakre J, Rossier J
机构信息
Laboratoire de Physiologie Nerveuse, Centre National de la Recherche Scientifique, Gif sur Yvette, France.
出版信息
Biochem Biophys Res Commun. 1992 Feb 14;182(3):1089-93. doi: 10.1016/0006-291x(92)91843-f.
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.
近期的论文描述了克隆的AMPA/海人酸受体亚基中谷氨酰胺到精氨酸的点突变，这些突变改变了电流-电压关系并抑制了Ca2+通透性，从而将这两个特性联系起来。我们描述了在同一位置发生的谷氨酰胺到组氨酸的突变，该突变改变了电流-电压关系，但保留了Ca2+通透性，从而使这两个特性分离。
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