Results 21 to 30 of about 43,522 (228)
Discovery of a Potent and Selective Naphthyridine-Based Chemical Probe for Casein Kinase 2. [PDF]
ACS Med Chem Lett, 2023 Naphthyridine-based inhibitors were synthesized to yield a potent and cell-active inhibitor of casein kinase 2 (CK2). Compound 2 selectively inhibits CK2α and CK2α′ when profiled broadly, thereby making it an exquisitely selective chemical probe for CK2.
Davis-Gilbert ZW +12 more
europepmc +2 more sources
Casein kinase 2 dependent phosphorylation of neprilysin regulates receptor tyrosine kinase signaling to Akt. [PDF]
PLoS ONE, 2010 Neprilysin (NEP) is a type II membrane metalloproteinase that cleaves physiologically active peptides at the cell surface thus regulating the local concentration of these peptides available for receptor binding and signal transduction.
Martin Siepmann +3 more
doaj +1 more source
Casein kinase 2 is essential for mitophagy [PDF]
The EMBO Reports, 2013 Mitophagy is a process that selectively degrades mitochondria. When mitophagy is induced in yeast, the mitochondrial outer membrane protein Atg32 is phosphorylated, interacts with the adaptor protein Atg11 and is recruited into the vacuole with mitochondria.
Tomotake, Kanki +10 more
openaire +2 more sources
Phosphorylation of fibrinogen by casein kinase 2 [PDF]
Biochemical Journal, 1986 Casein kinase 2 from rat liver cytosol phosphorylated human fibrinogen in a reaction that was not stimulated by Ca2+ or cyclic AMP, but was markedly inhibited by heparin, and proceeded at a similar rate when either ATP or GTP was used as phosphate donor.
M D, Guasch +3 more
openaire +2 more sources
Ribofuranosyl‐benzimidazole derivatives as inhibitors of casein kinase‐2 and casein kinase‐1 [PDF]
European Journal of Biochemistry, 1990 5,6‐Dichloro‐1‐(β‐d‐ribofuranosyl)benzimidazole (DiCl‐RB) is a powerful inhibitor of casein kinase‐2 (CK‐2) [Zandomeni, R. et al. (1986) J. Biol. Chem. 261, 3414–3420]. Here a series of 17 analogues of DiCl‐RB has been employed for studying the specificity and the mode of action of this family of CK‐2 inhibitors.
MEGGIO, FLAVIO, Shugar D, PINNA, LORENZO
openaire +3 more sources
Effect of all-trans retinoic acid on casein and fatty acid synthesis in MAC-T cells [PDF]
Asian-Australasian Journal of Animal Sciences, 2020 Objective Caseins and fatty acids of milk are synthesized and secreted by the epithelial cells of the mammary gland. All-trans retinoic acid (ATRA), an active metabolite of vitamin A, has been shown to promote mammary development.
Xian-Dong Liao +6 more
doaj +1 more source
Contribution of the CK2 Catalytic Isoforms α and α’ to the Glycolytic Phenotype of Tumor Cells
Cells, 2021 CK2 is a Ser/Thr protein kinase overexpressed in many cancers. It is usually present in cells as a tetrameric enzyme, composed of two catalytic (α or α’) and two regulatory (β) subunits, but it is active also in its monomeric form, and the specific role ...
Francesca Zonta +7 more
doaj +1 more source
Casein kinase 2 associates with and phosphorylates Dishevelled [PDF]
The EMBO Journal, 1997 The dishevelled (dsh) gene of Drosophila melanogaster encodes a phosphoprotein whose phosphorylation state is elevated by Wingless stimulation, suggesting that the phosphorylation of Dsh and the kinase(s) responsible for this phosphorylation are integral parts of the Wg signaling pathway.
K, Willert +4 more
openaire +2 more sources
The Physical Association of Casein Kinase 2 with Nucleolin [PDF]
Journal of Biological Chemistry, 1996 CK2 (formerly called casein kinase 2) is a ubiquitous messenger-independent serine/threonine protein kinase implicated in cell growth and proliferation. To investigate the regulation and functions of this enzyme, experiments were carried out to search for CK2-interacting proteins.
D, Li, G, Dobrowolska, E G, Krebs
openaire +2 more sources
CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site
Nature Communications, 2022 Here the authors identify SUZ12 as a cellular substate of casein kinase 2 (CK2), and show this phosphorylation changes the active site structure of Polycomb repressive complex 2 (PRC2) and promotes PRC2 function in cell identity maintenance during stem ...
Lihu Gong +5 more
doaj +1 more source