%0 Journal Article %1 franz2015parasitespecific %A Franz, E. %A Kim, J. %A Schneider, O. %A Bertinetti, D. %A Kim, C. %A Herberg, F.W. %D 2015 %J BMC Pharmacology and Toxicology %K herberg myown %N Suppl 1 %P A51 %R 10.1186/2050-6511-16-S1-A51 %T The role of a parasite-specific D-site in activation of Plasmodium falciparum cGMP-dependent protein kinase %U http://www.biomedcentral.com/2050-6511/16/S1/A51 %V 16 %X Malaria is one of the most dangerous tropical diseases worldwide, resulting in approximately 1.5-2.7 million deaths per year. Furthermore, malaria belongs to the four major infectious diseases also including HIV, tuberculosis and hepatitis. In humans, malaria is transmitted by four species of the genus Plasmodium. However, most malaria deaths are caused by Plasmodium falciparum. The Plasmodium falciparum cGMP-dependent protein kinase (PfPKG) is one of the key regulators of the malaria parasite life cycle in both sexual and asexual blood-stages. Inhibition of PfPKG stops differentiation and transmission of the parasites, indicating that this kinase is a promising drug target for malaria. However, despite its physiological importance, the activation mechanism of PfPKG is not fully understood. Recently, our group discovered that disrupting cGMP binding at the C-terminal cyclic nucleotide-binding (CNB-D) domain almost completely abolishes the kinase activation. Therefore, we investigate the functional role of the PfCNB-D in PfPKG activation.

@article{franz2015parasitespecific, abstract = {Malaria is one of the most dangerous tropical diseases worldwide, resulting in approximately 1.5-2.7 million deaths per year. Furthermore, malaria belongs to the four major infectious diseases also including HIV, tuberculosis and hepatitis. In humans, malaria is transmitted by four species of the genus Plasmodium. However, most malaria deaths are caused by Plasmodium falciparum. The Plasmodium falciparum cGMP-dependent protein kinase (PfPKG) is one of the key regulators of the malaria parasite life cycle in both sexual and asexual blood-stages. Inhibition of PfPKG stops differentiation and transmission of the parasites, indicating that this kinase is a promising drug target for malaria. However, despite its physiological importance, the activation mechanism of PfPKG is not fully understood. Recently, our group discovered that disrupting cGMP binding at the C-terminal cyclic nucleotide-binding (CNB-D) domain almost completely abolishes the kinase activation. Therefore, we investigate the functional role of the PfCNB-D in PfPKG activation.}, added-at = {2015-10-22T15:12:34.000+0200}, author = {Franz, E. and Kim, J. and Schneider, O. and Bertinetti, D. and Kim, C. and Herberg, F.W.}, biburl = {https://www.bibsonomy.org/bibtex/298d2bb8972b6cfaaa68fe503e5154646/biochemie}, description = {BMC Pharmacology and Toxicology | Full text | The role of a parasite-specific D-site in activation of Plasmodium falciparum cGMP-dependent protein kinase}, doi = {10.1186/2050-6511-16-S1-A51}, interhash = {2657d9c7e1ee9040441078f2b68ae2b0}, intrahash = {98d2bb8972b6cfaaa68fe503e5154646}, issn = {2050-6511}, journal = {BMC Pharmacology and Toxicology}, keywords = {herberg myown}, number = {Suppl 1}, pages = {A51}, timestamp = {2016-11-04T11:17:38.000+0100}, title = {The role of a parasite-specific D-site in activation of Plasmodium falciparum cGMP-dependent protein kinase}, url = {http://www.biomedcentral.com/2050-6511/16/S1/A51}, volume = 16, year = 2015 }