国家自然科学基金(81171164)

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Cysteine residues 87 and 320 in the amino terminal domain of NMDA receptor GluN2A govern its homodimerization but do not influence GluN2A/GluN1 heteromeric assembly被引量：2
《Neuroscience Bulletin》2013年第6期671-684,共14页Xiao-Min Zhang Xin-You Lv Yang Tang Li-Jun Zhu Jian-Hong Luo 
supported by grants from the National Basic Research Development Program of China(2010CB912002);the National Natural Science Foundation of China(30730038 and 81171164)
N-Methyl-D-aspartate receptors（NMDARs） play a central role in various physiological and pathological processes in the central nervous system.And they are commonly composed of four subunits,two GluN1 subunits and two...
关键词：N-methyl-D-aspartate receptor amino terminal domain HOMODIMERIZATION heteromeric assembly 
GluN2A versus GluN2B:twins,but quite different被引量：5
《Neuroscience Bulletin》2013年第6期761-772,共12页Xiao-Min Zhang Jian-Hong Luo 
supported by grants from the National Basic Research Development Program of China(2010CB912002);the National Natural Science Foundation of China(30730038 and 81171164)
N-Methyl-D-aspartate receptors（NMDARs） play vital roles in the central nervous system,as they are primary mediators of Ca2＋influx during synaptic activity.The subunits that compose NMDARs share similar topological ...
关键词：N-methyl-D-aspartate receptors GluN2A GluN2B developmental expression brain distribution FUNCTION TRAFFICKING 
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