Pharmacological inhibition of protein kinases in intact cells: antagonism of beta adrenergic receptor ligand binding by H-89 reveals limitations of usefulness.

@article{Penn1999PharmacologicalIO,
  title={Pharmacological inhibition of protein kinases in intact cells: antagonism of beta adrenergic receptor ligand binding by H-89 reveals limitations of usefulness.},
  author={Raymond B. Penn and J L Parent and Alexey N. Pronin and Reynold A Panettieri and Jeffrey L. Benovic},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1999},
  volume={288 2},
  pages={428-37}
}
The use of pharmacological inhibitors of protein kinases represents a potentially powerful tool in dissecting the regulatory features of intracellular signaling pathways. However, although the in vitro potency, selectivity, and efficacy of numerous kinase inhibitors have been characterized, little is known regarding the usefulness of these compounds as inhibitors in intact cells. In attempting to characterize the role of protein kinase A (PKA) in regulating the beta-2 adrenergic receptor (AR… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 33 extracted citations

A-kinase anchoring proteins regulate compartmentalized cAMP signaling in airway smooth muscle.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology • 2012
View 1 Excerpt

pH-dependent regulation of the α-subunit of H+-K+-ATPase (HKα2).

American journal of physiology. Renal physiology • 2011
View 1 Excerpt

References

Publications referenced by this paper.
Showing 1-10 of 25 references

Inhibitors of protein kinases and phosphatases.

Trends in biochemical sciences • 1994
View 8 Excerpts
Highly Influenced

endothelial thromboxane A2 receptor

KJ Romstedt, LA Lust, MT Clark, DD Miller, DR Feller
J Biol Chem 269:19256–19261 • 1997

Similar Papers

Loading similar papers…