Title : Splice variants of the N-methyl-D-aspartate receptor NR1 identify domains involved in regulation by polyamines and protein kinase C.

Pub. Date : 1993 Jul 15

PMID : 8341692






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 NR1 receptors that lacked the N-terminal exon (NR1(000), NR1(010), and NR1(011)) exhibited a relatively high affinity for NMDA (EC50 approximately 13 microM) and marked potentiation by spermine. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
2 NR1 receptors that lacked the N-terminal exon (NR1(000), NR1(010), and NR1(011)) exhibited a relatively high affinity for NMDA (EC50 approximately 13 microM) and marked potentiation by spermine. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
3 NR1 receptors that lacked the N-terminal exon (NR1(000), NR1(010), and NR1(011)) exhibited a relatively high affinity for NMDA (EC50 approximately 13 microM) and marked potentiation by spermine. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis
4 NR1 receptors that lacked the N-terminal exon (NR1(000), NR1(010), and NR1(011)) exhibited a relatively high affinity for NMDA (EC50 approximately 13 microM) and marked potentiation by spermine. N-Methylaspartate glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis