Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors.

@article{Hess1996CloningAF,
  title={Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors.},
  author={Stephen D. Hess and Lorrie P. Daggett and James H Crona and Cheri Deal and C. C. Lu and Arturo Urrutia and Laura E. Chavez-Noriega and Steven B. Ellis and E. Claire Johnson and G{\"o}n{\"u}l Veliçelebi},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1996},
  volume={278 2},
  pages={808-16}
}
Human cDNAs encoding N-methyl-D-aspartate receptor type (NMDAR)1A, NMDAR2A and NMDAR2B subunits were cloned and receptors encoded by these cDNAs were functionally expressed by injection of the respective mRNAs in Xenopus oocytes. The pharmacological properties of recombinant human N-methyl-D-aspartate (NMDA) receptors were characterized by profiling two agonists and four antagonists at both the NMDA and glycine sites in voltage-clamped oocytes. NMDA, glycine and D-serine were significantly more… CONTINUE READING

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