Phosphorylation by Akt within the ST loop of AMPK-α1 down-regulates its activation in tumour cells [PDF]
, 2014 The insulin/IGF-1 (insulin-like growth factor 1)-activated protein kinase Akt (also known as protein kinase B) phosphorylates Ser(487) in the ‘ST loop’ (serine/threonine-rich loop) within the C-terminal domain of AMPK-α1 (AMP-activated protein kinase-α1),
Chen +53 more
core +3 more sources
Diacylglycerol kinase control of protein kinase C
Biochemical Journal, 2019 Abstract The diacylglycerol kinases (DGK) are lipid kinases that transform diacylglycerol (DAG) into phosphatidic acid (PA) in a reaction that terminates DAG-based signals. DGK provide negative regulation to conventional and novel protein kinase C (PKC) enzymes, limiting local DAG availability in a tissue- and subcellular-restricted ...
Isabel Mérida +3 more
openaire +4 more sources
Protein Kinases as Drug Development Targets for Heart Disease Therapy
Pharmaceuticals, 2010 Protein kinases are intimately integrated in different signal transduction pathways for the regulation of cardiac function in both health and disease.
Alison L. Müller, Naranjan S. Dhalla
doaj +1 more source
Activation of tyrosine kinases by mutation of the gatekeeper threonine. [PDF]
, 2008 Protein kinases targeted by small-molecule inhibitors develop resistance through mutation of the gatekeeper threonine residue of the active site. Here we show that the gatekeeper mutation in the cellular forms of c-ABL, c-SRC, platelet-derived growth ...
Azam, Mohammad +4 more
core +1 more source
Phosphorylation by protein kinase C and the responsiveness of Mg2+-ATPase to Ca2+ of myofibrils isolated from stunned and non-stunned porcine myocardinm [PDF]
, 1997 Previously we showed in an in situ porcine model that the thiadiazinone derivative [+]EMD 60263, a Ca2+ sensitizer without phosphodiesterase III inhibitory properties, increased contractility more profoundly in stunned than in non-stunned myocardium ...
Bezstarosti, K. (Karel) +3 more
core +2 more sources
Protein kinase C and cancer: what we know and what we do not
Oncogene, 2014 Since their discovery in the late 1970s, protein kinase C (PKC) isozymes represent one of the most extensively studied signaling kinases. PKCs signal through multiple pathways and control the expression of genes relevant for cell cycle progression ...
Rachana Garg +5 more
semanticscholar +1 more source
Phosphorylation of protein kinase C by casein kinase‐1 [PDF]
FEBS Letters, 1989 Because phosphorylation of protein kinase C (PKC) may provide a mechanism for regulation of this enzyme, we have examined the ability of two other kinases to phosphorylate PKC. Our results show that casein kinase 1 (CK‐1), but not casein kinase 2 (CK‐2), can phosphorylate PKC in the absence of Ca2+ and phospholipids.
Michael J. Weber +4 more
openaire +3 more sources
Do anionic phospholipids serve as cofactors or second messengers for the regulation of activity of cloned ATP-sensitive K+ channels? [PDF]
, 2003 The regulation of ion channels by anionic phospholipids is currently very topical. An outstanding issue is whether phosphatidylinositol 4,5-diphosphate and related species act as true second messengers in signaling or behave in a manner analogous to an ...
Clapp, LH +4 more
core +1 more source
Insights into Activation Mechanisms of Store-Operated TRPC1 Channels in Vascular Smooth Muscle. [PDF]
, 2020 In vascular smooth muscle cells (VMSCs), the stimulation of store-operated channels (SOCs) mediate Ca2+ influx pathways which regulate important cellular functions including contraction, proliferation, migration, and growth that are associated with the ...
Albert, AP +3 more
core +1 more source
Journal of Biological Chemistry, 2002 Nrf2, a basic leucine zipper transcription factor, is an essential activator of the coordinated transcription of genes encoding antioxidant enzymes and phase II detoxifying enzymes through the regulatory sequence termed antioxidant response element (ARE).
H.‐C. Huang +2 more
semanticscholar +1 more source