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The rapid development of different aspects of glutamate and GABA receptor research makes it difficult to establish a general view of the field. Studies of the receptors are a multi-disciplinary task employing many specialised techniques. Glutamate and GABA Receptors and Transporters: Structure, Function and Pharmacology conveys recent discoveries in a framework of the basic concepts in the field of glutamate and GABA receptor research. Suitable for postgraduate students, it is also beneficial for industrial and academic research scientists in both the glutamate and GABA field, as well as universities offering programs in neuroscience, molecular pharmacology or medicinal chemistry.
Sommario
Ionotropic Glutamate Receptors: Functional and Pharmacological Properties in Relation to Constituent Subunits. Molecular Structure of Ionotropic Glutamate Receptors. Glutamate Receptor Trafficking. Pharmacology of NMDA Receptors. Pharmacology of AMPA/kainate Receptors. Metabotropic Glutamate Receptors (mGluRs): Structure and Functions. Pharmacology of Metabotropic Receptors. Insights into GABAA Receptor Complexity From the Study of Cerebellar Granule Cells: Synaptic and Extrasynaptic Receptors. GABAA Receptor Complex: Structure and Function. GABAA Receptor Complex: Structural Requirements for Ligand Interactions. Molecular Structure of the GABAB Receptors. Phamacology of GABAB Receptors. Structure, Function and Regulation of Glutamate Transporters. GABA Transporters: Functional and Pharmacological Properties. Transgenic Models for Glutamate Receptor Function. Transgenic Models for GABAA Receptor Function. Glutamatergic transmission: Therapeutic Prospects for Schizophrenia and Alzheimer's Disease. GABA-ergic Transmission: Therapeutic Prospects.
Info autore
Jan Egebjerg, Arne Schousboe, Povl Krogsgaard-Larsen
Riassunto
Describes the structural and functional diversity of the ionotropic and metabotropic classes of receptor that have been identified for glutamate and GABA. This book also describes the analysis of crystallized complexes of recombinant binding domains of these receptors with specific ligands.
