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  Molecular biology of glutamate receptors

Schöpfer, R., Monyer, H., Sommer, B., Wisden, W., Sprengel, R., Kuner, T., et al. (1994). Molecular biology of glutamate receptors. Progress in Neurobiology, 42(2), 353-357. doi:10.1016/0301-0082(94)90076-0.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A996-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-B304-E
Genre: Journal Article

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ProgNeurobiol_42_1994_353.pdf (Any fulltext), 1016KB
 
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Schöpfer, Ralf1, Author              
Monyer, Hannah1, Author              
Sommer, Bernd, Author
Wisden, William, Author
Sprengel, Rolf1, 2, 3, Author              
Kuner, Thomas1, 4, 5, 6, 7, Author              
Lomeli, Hilda, Author
Herb, Anne1, Author              
Köhler, Martin1, Author              
Burnashev, Nail7, Author              
Günther, Willy, Author
Ruppersberg, J. Peter7, Author              
Seeburg, Peter H.1, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Rolf Sprengel Group, Max Planck Institute for Medical Research, Max Planck Society, ou_1497741              
3Olfaction Web, Max Planck Institute for Medical Research, Max Planck Society, ou_1497733              
4Interdisciplinary WIN-Research Group on Olfactory Dynamics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497717              
5Synaptic Transmission MNTB, Max Planck Institute for Medical Research, Max Planck Society, ou_1497745              
6Synaptic Transmission, Max Planck Institute for Medical Research, Max Planck Society, ou_1497744              
7Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 Abstract: The ligand-gated receptors for L-glutamate play a central role in acute neuronal degeneration. Recently cDNAs have been isolated for subunits of several glutamate receptor subtypes. By sequence homology all these subunits clearly belong to one large gene family. Several subfamilies exist and match roughly previously pharmacologically and electrophysiologically defined subtypes of glutamate receptors. Currently four genes (GluR A, B, C and D) are known that code for the AMPA subtypes of glutamate receptors. Recombinant expression of wild type and mutated sequences identified a critical residue in the putative TM2 channel-lining segment that controls Ca2+ ion permeability. The arginine (R) found in GluR B subunits at that position renders AMPA channels impermeable for Ca2+ ions, whereas glutamine (Q) containing GluR A, C and D subunits give rise to Ca2+ permeable channels. RNA editing converts the genomically encoded glutamine codon into the arginine codon found in GluR B cDNAs for the Q/R site. NMDA subtypes of glutamate receptors are formed after coexpression of the NR1 cDNA with a cDNA of the NR2 family. Depending on the member of the NR2 family used, NMDA receptors with different kinetical and pharmacological properties are generated. Common to all channels of these NMDA receptors is a high permeability for Ca2+ ions and a voltage dependent block by Mg2+ ions. All currently known NMDA receptor subunits have an asparagine at the Q/R homologous position. We found that this residue is critical for Mg2+ block and Ca2+ permeability of NMDA receptor channels.

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Language(s): eng - English
 Dates: 2003-03-071994-02
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666749
DOI: 10.1016/0301-0082(94)90076-0
URI: https://www.ncbi.nlm.nih.gov/pubmed/8008835
Other: 4105
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Title: Progress in Neurobiology
Source Genre: Journal
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Publ. Info: Oxford, Eng. : Pergamon
Pages: - Volume / Issue: 42 (2) Sequence Number: - Start / End Page: 353 - 357 Identifier: ISSN: 0301-0082
CoNE: https://pure.mpg.de/cone/journals/resource/954925509370