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A fully automated s-35 gtp gamma s scintillation proximity assay for the high-throughput screening of g(i)-linked g protein-coupled receptors

Academic Article
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Overview

authors

  • Ferrer, M.
  • Kolodin, G. D.
  • Zuck, P.
  • Peltier, R.
  • Berry, K.
  • Mandala, S. M.
  • Rosen, Hugh
  • Ota, H.
  • Ozaki, S.
  • Inglese, J.
  • Strulovici, B.

publication date

  • April 2003

journal

  • Assay and Drug Development Technologies  Journal

abstract

  • 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 [(35)S]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 [(35)S]GTPgammaS scintillation proximity binding assays for two different G(i)-coupled GPCRs, and describe their implementation with automated high-throughput systems.

subject areas

  • Automation
  • Biological Assay
  • Combinatorial Chemistry Techniques
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • Radioligand Assay
  • Receptors, G-Protein-Coupled
  • Scintillation Counting
  • Sulfur Radioisotopes
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Identity

International Standard Serial Number (ISSN)

  • 1540-658X

Digital Object Identifier (DOI)

  • 10.1089/15406580360545071

PubMed ID

  • 15090191
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Additional Document Info

start page

  • 261

end page

  • 273

volume

  • 1

issue

  • 2

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