1-3 of 3
Keywords: protein kinase Cα (PKCα)
Close
Save search
Follow your search
Access your saved searches in your account
Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Articles

PI3Kγ controls oxidative bursts in neutrophils via interactions with PKCα and p47phox

Katja Lehmann, Jörg P. Müller, Bernhard Schlott, Philipp Skroblin, Dagmar Barz, Johannes Norgauer, Reinhard Wetzker
Journal: Biochemical Journal
Biochem J (2009) 419 (3): 603–610.
https://doi.org/10.1042/BJ20081268
Published: 14 April 2009
... the association of PI3Kγ with protein kinase Cα (PKCα). Specific inhibition of PI3Kγ suppresses fMLP-mediated activation of PKCα activity and ROS production, suggesting that the protein kinase activity of PI3Kγ is involved. Our data suggest that the direct interaction of PI3Kγ with PKCα forms a discrete...
View articletitled, PI3Kγ controls oxidative bursts in neutrophils via interactions with PKCα and p47phox
Open the PDF for PI3Kγ controls oxidative bursts in neutrophils via interactions with PKCα and p47phox in another window
Includes: Supplementary data
Articles

Phosphorylation of CK1δ: identification of Ser 370 as the major phosphorylation site targeted by PKA in vitro and in vivo

Georgios Giamas, Heidrun Hirner, Levani Shoshiashvili, Arnhild Grothey, Susanne Gessert, Michael Kühl, Doris Henne-Bruns, Constantinos E. Vorgias, Uwe Knippschild
Journal: Biochemical Journal
Biochem J (2007) 406 (3): 389–398.
https://doi.org/10.1042/BJ20070091
Published: 29 August 2007
... 6 2007 © The Authors Journal compilation © 2007 Biochemical Society 2007 A-kinase-anchoring protein (AKAP) cAMP-dependent protein kinase (PKA) casein kinase 1 δ (CK1δ) CDC-like kinase 2 (CLK2) protein kinase B (Akt) protein kinase Cα (PKCα) The CK1 (casein kinase 1) group...
View articletitled, Phosphorylation of CK1δ: identification of Ser 370 as the major phosphorylation site targeted by PKA in vitro and in vivo
Open the PDF for Phosphorylation of CK1δ: identification of Ser 370 as the major phosphorylation site targeted by PKA in vitro and in vivo in another window
Includes: Supplementary data
Articles

Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Cα and calpain proteolytic cleavage

Sandrine DULONG, Sebastien GOUDENEGE, Karine VUILLIER-DEVILLERS, Stéphane MANENTI, Sylvie POUSSARD, Patrick COTTIN
Journal: Biochemical Journal
Biochem J (2004) 382 (3): 1015–1023.
https://doi.org/10.1042/BJ20040347
Published: 07 September 2004
... should be addressed (email [email protected] ). 4 3 2004 7 7 2004 7 7 2004 7 7 2004 The Biochemical Society, London 2004 actin cytoskeleton Ca 2+ calpain myristoylated alanine-rich C kinase substrate (MARCKS) myogenesis protein kinase Cα (PKCα...
View articletitled, Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Cα and calpain proteolytic cleavage
Open the PDF for Myristoylated alanine-rich C kinase substrate (MARCKS) is involved in myoblast fusion through its regulation by protein kinase Cα and calpain proteolytic cleavage in another window