scholarly journals Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2).

1984 ◽  
Vol 259 (23) ◽  
pp. 14576-14579 ◽  
Author(s):  
F Meggio ◽  
F Marchiori ◽  
G Borin ◽  
G Chessa ◽  
L A Pinna
Keyword(s):  
Rat Liver ◽  
Synthetic Peptides ◽  
Casein Kinase

scholarly journals Detection of type-2 casein kinase and its endogenous substrates in the components of the microsomal fraction of rat liver

1984 ◽  
Vol 138 (2) ◽  
pp. 379-385 ◽  
Author(s):  
Flavio MEGGIO ◽  
Anna Maria BRUNATI ◽  
Arianna DONELLA-DEANA ◽  
Lorenzo A. PINNA
Keyword(s):  
Rat Liver ◽  
Microsomal Fraction ◽  
Casein Kinase ◽  
Endogenous Substrates

Steady-State Cleavage Kinetics for Dengue Virus Type 2 Ns2b-Ns3(Pro) Serine Protease With Synthetic Peptides

2003 ◽  
Vol 10 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Rabuesak Khumthong ◽  
Pornwarat Niyomrattanakit ◽  
Santad Chanprapaph ◽  
Chanan Angsuthanasombat ◽  
Sakol Panyim ◽  
...  
Keyword(s):  
Steady State ◽  
Dengue Virus ◽  
Serine Protease ◽  
Virus Type ◽  
Synthetic Peptides ◽  
Dengue Virus Type 2

scholarly journals Effects of Casein Kinase 2 Alpha 1 Gene Expression on Mice Liver Susceptible to Type 2 Diabetes Mellitus and Obesity

2020 ◽  
Vol 17 (1) ◽  
pp. 13-20 ◽  
Author(s):  
Yu-Ching Lan ◽  
Yeh-Han Wang ◽  
Hsin-Han Chen ◽  
Sui-Foon Lo ◽  
Shih-Yin Chen ◽  
...  
Keyword(s):  
Gene Expression ◽  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Mice Liver

scholarly journals Phosphorylation of rat liver heterogeneous nuclear ribonucleoproteins A2 and C can be modulated by calmodulin.

1995 ◽  
Vol 15 (2) ◽  
pp. 661-670 ◽  
Author(s):  
R Bosser ◽  
M Faura ◽  
J Serratosa ◽  
J Renau-Piqueras ◽  
M Pruschy ◽  
...  
Keyword(s):  
Rat Liver ◽  
Peptide Mapping ◽  
Specific Protein ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Dependent Manner ◽  
Cell Nuclei ◽  
Ribonucleoprotein Particles ◽  
C Proteins

It was previously reported that the phosphorylation of three proteins of 36, 40 to 42, and 50 kDa by casein kinase 2 is inhibited by calmodulin in nuclear extracts from rat liver cells (R. Bosser, R. Aligué, D. Guerini, N. Agell, E. Carafoli, and O. Bachs, J. Biol. Chem. 268:15477-15483, 1993). By immunoblotting, peptide mapping, and endogenous phosphorylation experiments, the 36- and 40- to 42-kDa proteins have been identified as the A2 and C proteins, respectively, of the heterogeneous nuclear ribonucleoprotein particles. To better understand the mechanism by which calmodulin inhibits the phosphorylation of these proteins, they were purified by using single-stranded DNA chromatography, and the effect of calmodulin on their phosphorylation by casein kinase 2 was analyzed. Results revealed that whereas calmodulin inhibited the phosphorylation of purified A2 and C proteins in a Ca(2+)-dependent manner, it did not affect the casein kinase 2 phosphorylation of a different protein substrate, i.e., beta-casein. These results indicate that the effect of calmodulin was not on casein kinase 2 activity but on specific protein substrates. The finding that the A2 and C proteins can bind to a calmodulin-Sepharose column in a Ca(2+)-dependent manner suggests that this association could prevent the phosphorylation of the proteins by casein kinase 2. Immunoelectron microscopy studies have revealed that such interactions could also occur in vivo, since calmodulin and A2 and C proteins colocalize on the ribonucleoprotein particles in rat liver cell nuclei.

Spermine-mediated casein kinase II-uptake by rat liver mitochondria

1994 ◽  
Vol 1199 (3) ◽  
pp. 266-270 ◽  
Author(s):  
Luciana Bordin ◽  
Federica Cattapan ◽  
Giulio Clari ◽  
Antonio Toninello ◽  
Noris Siliprandi ◽  
...  
Keyword(s):  
Rat Liver ◽  
Casein Kinase Ii ◽  
Liver Mitochondria ◽  
Casein Kinase ◽  
Rat Liver Mitochondria
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