Two Galpha(i1) rate-modifying mutations act in concert to allow receptor-independent, steady-state measurements of RGS protein activity.

@article{Zielinski2009TwoGR,
  title={Two Galpha(i1) rate-modifying mutations act in concert to allow receptor-independent, steady-state measurements of RGS protein activity.},
  author={Thomas P. Zielinski and Adam J. Kimple and Stephanie Q. Hutsell and Mark D Koeff and David P. Siderovski and Robert G. Lowery},
  journal={Journal of biomolecular screening},
  year={2009},
  volume={14 10},
  pages={1195-206}
}
RGS proteins are critical modulators of G-protein-coupled receptor (GPCR) signaling given their ability to deactivate Galpha subunits via GTPase-accelerating protein (GAP) activity. Their selectivity for specific GPCRs makes them attractive therapeutic targets. However, measuring GAP activity is complicated by slow guanosine diphosphate (GDP) release from Galpha and lack of solution phase assays for detecting free GDP in the presence of excess guanosine triphosphate (GTP). To overcome these… CONTINUE READING

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