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- W2092860293 abstract "Argiotoxin636, a component of the spider venom of argiope species, was chemically synthesized together with a number of derivatives in order to analyse their blocking activity on mammalian glutamate receptors. Xenopus laevis oocytes injected with rat brain mRNA served as assay system. The results showed that argiotoxin636 had a higher affinity for N-methyl-D-aspartate (NMDA) than for kainate receptors, blocking the corresponding ion channels in a voltage-dependent manner. Modifications of the polyamine tail or the terminal arginine residue strongly reduced the blocking potency. The iodinated monohydroxyl phenylderivatives, however, retained their NMDA-selective binding and could serve as non-competitive antagonists for radioligand binding assays aiding in the biochemical isolation of glutamate receptors." @default.
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- W2092860293 date "1991-11-01" @default.
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- W2092860293 title "Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes" @default.
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- W2092860293 doi "https://doi.org/10.1016/0304-3940(91)90298-8" @default.
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