Ligand binding to porcine ionotropic glutamate receptors with chemically modified arginyl residues

1997 ◽  
Vol 234 (2-3) ◽  
pp. 83-86
Author(s):  
Zsolt Jenei ◽  
Vince Varga ◽  
Réka Janáky ◽  
Pirjo Saransaari ◽  
Simo S Oja
2014 ◽  
Vol 106 (2) ◽  
pp. 152a
Author(s):  
Benoite Bargeton ◽  
Matteo Dal Peraro ◽  
Richard Benton

2010 ◽  
Vol 98 (3) ◽  
pp. 526a
Author(s):  
Margaret W. Thompson ◽  
Kathryn A. McMenimen ◽  
Henry A. Lester ◽  
Dennis A. Dougherty

2011 ◽  
Vol 57 ◽  
pp. 3-16
Author(s):  
Zorica Serafimoska ◽  
Tommy N. Johansen ◽  
Karla Frydenvang ◽  
Ljubica Suturkova

Ionotropic glutamate receptors (iGluRs) constitute a family of ligand gated ion channels subdivided in three classes, NMDA, AMPA (iGluA1-4) and KA (1-5) according to the agonists that selectively activate them. iGluRs are tetrameric assemblies of highly homologous receptor subunits. They are critically important for normal brain function and are considered to be involved on neurological disorders and degenerative diseases such as schizophrenia, Alzheimer’s disease, brain damage following stroke and epilepsy. Since the first publication of the structure of recombinant soluble protein of ligand binding domain of GluA2 extensive studies on this group of receptors were performed and many crystal structures as complexes of GluA2-LBD with agonists, partial agonists and antagonists were obtained. The structural information in combination with functional data makes good platform for consecutive investigation and design of new selective drugs which will be used in treatment of neurodegerative diseases.


2006 ◽  
Vol 4 (6) ◽  
pp. 1058 ◽  
Author(s):  
Ulla Pentikäinen ◽  
Luca Settimo ◽  
Mark S. Johnson ◽  
Olli T. Pentikäinen

2021 ◽  
pp. 108631
Author(s):  
David Stroebel ◽  
Laetitia Mony ◽  
Pierre Paoletti

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