@article{oai:niigata-u.repo.nii.ac.jp:00014657,
 author = {池野, 観寿},
 issue = {10},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Oct},
 note = {The physiological function of the GluRδ subfamily which is one of the glutamate receptor channel subunits has not yet been clarified, because no GluR channel activity was detected in heterologous expression systems. The Lurcher mutation, a point mutation of the GluRδ 2 subunit, converts it into a functional channel. We introduced this mutation into GluRδ, AMPA-and NMDA-type GluR channel subunits, and characterized their channel properties. It was shown that the Lurcher mutation exerts effects only on the AMPA-and NMDA-type channel gating, but not on their ionic channel permeabilities. These findings support the idea that the Lurcher mutant GluRδ 1 and GluRδ 2 channels are permeable to Ca^2+, reflecting their original channel properties. It was also found that the ionic permeability of the mutant GluRδ 1 channels was modulated by TPA.},
 pages = {506--517},
 title = {Lurcher型変異を用いたグルタミン酸受容体 δサブユニットのチャネル特性解析},
 volume = {115},
 year = {2001}
}