Results 21 to 30 of about 115,342,253 (257)

Malaria protein kinase CK2 (PfCK2) shows novel mechanisms of regulation [PDF]

, 2014
Casein kinase 2 (protein kinase CK2) is a conserved eukaryotic serine/theronine kinase with multiple substrates and roles in the regulation of cellular processes such as cellular stress, cell proliferation and apoptosis.
Schmid, Ralf, Solyakov, Lev, Doerig, Christian, Graciotti, Michele, Burley, Glenn, Tobin, Andrew B, Cullis, Paul, Alam, Mahmood, Bottrill, Andrew R   +8 more
core   +3 more sources

New Aspects for the Treatment of Cardiac Diseases Based on the Diversity of Functional Controls on Cardiac Muscles: Mitochondrial Ion Channels and Cardioprotection

Journal of Pharmacological Sciences, 2009
Mitochondrial ATP-sensitive K+ (mitoKATP) and Ca2+-activated K+ (mitoKCa) channels exist in cardiac myocytes, and they play key roles in cardioprotection.
Hirofumi Nishida, Toshiaki Sato, Takehiko Ogura, Haruaki Nakaya   +3 more
doaj   +1 more source

Evolution of the cAMP-dependent protein kinase (PKA) catalytic subunit isoforms. [PDF]

PLoS ONE, 2017
The 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase, or protein kinase A (PKA), pathway is one of the most versatile and best studied signaling pathways in eukaryotic cells.
Kristoffer Søberg, Line Victoria Moen, Bjørn Steen Skålhegg, Jon Kristen Laerdahl   +3 more
doaj   +1 more source

Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D [PDF]

, 2007
Phosphoinoisitide dependent kinase l (PDK1) is proposed to phosphorylate a key threonine residue within the catalytic domain of the protein kinase C (PKC) superfamily that controls the stability and catalytic competence of these kinases.
Kelly, April P., Cantrell, Doreen A., Wood, C. David, Matthews, Sharon A.   +3 more
core   +1 more source

Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A

eLife, 2020
In the nucleus, the spatiotemporal regulation of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) is orchestrated by an intrinsically disordered protein kinase inhibitor, PKI, which recruits the CRM1/RanGTP nuclear exporting complex.
Cristina Olivieri, Yingjie Wang, Geoffrey C Li, Manu V S, Jonggul Kim, Benjamin R Stultz, Matthew Neibergall, Fernando Porcelli, Joseph M Muretta, David DT Thomas, Jiali Gao, Donald K Blumenthal, Susan S Taylor, Gianluigi Veglia   +13 more
doaj   +1 more source

Cyclic AMP increases COX-2 expression via mitogen-activated kinase in human myometrial cells [PDF]

, 2011
Cyclic AMP (cAMP) is the archetypal smooth muscle relaxant, mediating the effects of many hormones and drugs. However, recently PGI2, acting via cAMP/PKA, was found to increase contraction-associated protein expression in myometrial cells and to promote ...
Mandeep Kandola, Mark R. Johnson, Kandola, Mandeep, Zhiqing Liang, Johnson, Mark R., Chen, Li, Lei, Kaiyu, Sooranna, Suren R, Phillip R. Bennett, Dimitri Grammatopoulos, Grammatopoulos, Dimitris, Bennett, Phillip, Johnson, Mark R, Suren R. Sooranna, Chen, Li I., Li Chen, Kaiyu Lei, Sooranna, Suren R., Grammatopoulos, Dimitri, Liang, Zhiqing, Bennett, Phillip R   +20 more
core   +1 more source

Control of PKA stability and signalling by RING ligase praja2 [PDF]

, 2010
Ligand-mediated activation of G-Protein Coupled Receptors (GPCRs) mobilises compartmentalised pulses of second messengers like cAMP. The main cellular effector of cAMP is Protein Kinase A (PKA) which is assembled as inactive holoenzyme consisting of two ...
Lignitto, Luca
core   +1 more source

Comprehensive Analysis of Aspergillus nidulans PKA Phosphorylome Identifies a Novel Mode of CreA Regulation

mBio, 2019
In filamentous fungi, an important kinase responsible for adaptation to changes in available nutrients is cyclic AMP (cAMP)-dependent protein kinase (protein kinase A [PKA]).
Liliane F. C. Ribeiro, Cynthia Chelius, Karthik R. Boppidi, Nisha S. Naik, Simin Hossain, Jessica J. J. Ramsey, Jyothi Kumar, Lucas F. Ribeiro, Marc Ostermeier, Bao Tran, Young Ah Goo, Leandro J. de Assis, Mevlut Ulas, Ozgur Bayram, Gustavo H. Goldman, Stephen Lincoln, Ranjan Srivastava, Steven D. Harris, Mark R. Marten   +18 more
doaj   +1 more source

Deep evolutionary conservation of an intramolecular protein kinase activation mechanism [PDF]

, 2012
DYRK-family kinases employ an intramolecular mechanism to autophosphorylate a critical tyrosine residue in the activation loop. Once phosphorylated, DYRKs lose tyrosine kinase activity and function as serine/threonine kinases.
Cleghon Vaughn, Aman Singh (191216), Cleghon, V., Nathan Luebbering (191210), Sibbet Gary, Jingfen Han, Luebbering Nathan, Nathan Luebbering, Michael A J Ferguson, Singh, A., Aman Singh, Ferguson, M.A.J., Ferguson Michael A. J., Hong, W., Diego Miranda-Saavedra (36622), Michael A. J. Ferguson (166662), Jingfen Han, Han, J., Gary Sibbet (191221), Vaughn Cleghon (191224), Miranda-Saavedra Diego, Sibbet, G., Ferguson, M.A.J.; id_orcid, Han Jingfen, Miranda-Saavedra, D., Gary Sibbet, Luebbering, N., Diego Miranda-Saavedra, Michael A. J. Ferguson, Vaughn Cleghon, Singh Aman, Jingfen Han (191204)   +31 more
core   +1 more source

MAGI1 Mediates eNOS Activation and NO Production in Endothelial Cells in Response to Fluid Shear Stress

Cells, 2019
Fluid shear stress stimulates endothelial nitric oxide synthase (eNOS) activation and nitric oxide (NO) production through multiple kinases, including protein kinase A (PKA), AMP-activated protein kinase (AMPK), AKT and Ca2+/calmodulin-dependent protein ...
Kedar Ghimire, Jelena Zaric, Begoña Alday-Parejo, Jochen Seebach, Mélanie Bousquenaud, Jimmy Stalin, Grégory Bieler, Hans-Joachim Schnittler, Curzio Rüegg   +8 more
doaj   +1 more source