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  Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes

Draguhn, A., Jahn, W., & Witzemann, V. (1991). Argiotoxin636 inhibits NMDA-activated ion channels expressed in Xenopus oocytes. Neuroscience Letters, 132(2), 187-190. doi:10.1016/0304-3940(91)90298-8 Get.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AC75-A Version Permalink: http://hdl.handle.net/21.11116/0000-0000-64E7-B
Genre: Journal Article

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NeurosciLett_132_1991_187.pdf (Any fulltext), 343KB
 
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 Creators:
Draguhn, Andreas1, Author              
Jahn, Werner2, 3, Author              
Witzemann, Veit1, 4, 5, 6, Author              
Affiliations:
1Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
3Muscle Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497731              
4Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
5Working Group Witzemann / Koenen, Max Planck Institute for Medical Research, Max Planck Society, ou_1497748              
6Molecular anatomy of the neuromuscular junction, Max Planck Institute for Medical Research, Max Planck Society, ou_1497727              

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 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.

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Language(s): eng - English
 Dates: 1991-07-301991-06-241991-07-312003-03-191991-11-11
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Neuroscience Letters
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 132 (2) Sequence Number: - Start / End Page: 187 - 190 Identifier: ISSN: 0304-3940
CoNE: https://pure.mpg.de/cone/journals/resource/954925512448