%0 Generic %1 huang2013structures %A Huang, G. %A Kim, J. %A Reger, A. %A Lorenz, R. %A Moon, E. %A Zhao, C. %A Casteel, D. %A Bertinetti, D. %A VanSchouwen, B. %A Selvaratnam, R. %A Pflugrath, J. %A Sankaran, B. %A Melacini, G. %A Herberg, F. W. %A Kim, C. %D 2013 %J BMC Pharmacology and Toxicology %K herberg ip myown %N Suppl 1 %P O16 %R 10.1186/2050-6511-14-S1-O16 %T Structures of human PKG reveal cGMP-selectived activation mechanisms %U http://www.biomedcentral.com/2050-6511/14/S1/O16 %V 14

@presentation{huang2013structures, added-at = {2013-09-16T15:29:19.000+0200}, author = {Huang, G. and Kim, J. and Reger, A. and Lorenz, R. and Moon, E. and Zhao, C. and Casteel, D. and Bertinetti, D. and VanSchouwen, B. and Selvaratnam, R. and Pflugrath, J. and Sankaran, B. and Melacini, G. and Herberg, F. W. and Kim, C.}, biburl = {https://www.bibsonomy.org/bibtex/2e800aebd727281a60da2464aae8526b4/biochemie}, description = {Cyclic guanosine monophosphate (cGMP) is a key secondary messenger that is produced in response to nitric oxide. One of the key mediators of cGMP signaling, cGMP-dependent protein kinase (PKG), is activated upon binding to cGMP and phosphorylates downstream substrates in a process required for important physiological processes such as vasodilation, nociception, and memory formation. PKGs are also known to mediate most effects of drugs that increase cellular cGMP levels, including nitric oxide-releasing agents and phosphodiesterase inhibitors, which are used for the treatment of angina pectoris and erectile dysfunction, respectively. It is known that PKG is preferentially activated by cGMP over cAMP roughly 60-100 fold – however, the molecular mechanism by which cGMP is distinguished from a structurally similar messenger, cAMP, is poorly defined. Using competition fluorescence polarization (FP), X-ray crystallography, and in vitro kinase assays, we sought to understand the molecular basis for cGMP selectivity in PKGI. }, doi = {10.1186/2050-6511-14-S1-O16}, interhash = {8044263bc9b0a6effd32b3af2dc8e625}, intrahash = {e800aebd727281a60da2464aae8526b4}, issn = {2050-6511}, journal = {BMC Pharmacology and Toxicology}, keywords = {herberg ip myown}, number = {Suppl 1}, pages = {O16}, timestamp = {2016-11-04T11:47:13.000+0100}, title = {Structures of human PKG reveal cGMP-selectived activation mechanisms}, url = {http://www.biomedcentral.com/2050-6511/14/S1/O16}, volume = 14, year = 2013 }