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The heteromeric mouse ε2/ζ1 N-methyl-d-aspartate (NMDA) receptor was expressed in Xenopus oocytes, and its channel properties were studied using both the outside-out-patch-clamp and two-microelectrode voltage-clamp techniques. In the cloned receptor channel, permeation properties of monovalent and divalent cations, and voltage-dependent block by Mg 2+ were similar to those reported previously...
The primary structure of a novel subunit of the mouse NMDA (N-methyl-d-aspartate) receptor channel, designated 4, has been revealed by cloning and sequencing the cDNA. The 4 subunit shares high amino acid sequence identity with the 1, 2 and 3 subunits of the mouse NMDA. receptor channel, thus constituting the subfamily of the glutamate receptor channel. Expression from cloned cDNAs of...
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