IN THE GLUR1 GLUTAMATE RECEPTOR SUBUNIT A GLUTAMINE TO HISTIDINE POINT MUTATION SUPPRESSES INWARD RECTIFICATION BUT NOT CALCIUM PERMEABILITY

被引：24

作者：

CURUTCHET, P

BOCHET, P

DECARVALHO, LP

LAMBOLEZ, B

STINNAKRE, J

ROSSIER, J

机构：

[1] LAB PHYSIOL NERVEUSE,CNRS,F-91198 GIF SUR YVETTE,FRANCE

[2] LAB NEUROBIOL CELLULAIRE & MOLEC,CNRS,F-91198 GIF SUR YVETTE,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 182卷 / 03期

关键词：

D O I：

10.1016/0006-291X(92)91843-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1992.

引用

页码：1089 / 1093

页数：5

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