期刊
ASSAY AND DRUG DEVELOPMENT TECHNOLOGIES
卷 1, 期 2, 页码 261-273出版社
MARY ANN LIEBERT INC PUBL
DOI: 10.1089/15406580360545071
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The diversity of physiological functions mediated by the GPCR superfamily provides a rich source of molecular targets for drug discovery programs. Consequently, a variety of assays have been designed to identify lead molecules based on ligand binding or receptor function. In one of these, the binding of [S-35]GTPgammaS, a nonhydrolyzable analogue of GTP, to receptor-activated G-protein alpha subunits represents a unique functional assay for GPCRs and is well suited for use with automated HTS. Here we compare [S-35]GTPgammaS scintillation proximity binding assays for two different G(i)-coupled GPCRs, and describe their implementation with automated high-throughput systems.
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