1,721,115 research outputs found
Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosol.
No full textRandom tyrosine and glutamic acid-containing polymers are very powerful inhibitors of casein kinase-2.
No full textPhosphorylation of phosvitin by casein kinase-2 provides the evidence that phosphoserines can replace carboxylic amino acids as specificity determinants.
No full textPhosphorylation of threonine and serine residues of native and partially dephosphorylated caseins by a rat liver cyclic AMP-insensitive protein kinase.
No full textDual role of calsequestrin as substrate and inhibitor of casein kinase-1 and casein kinase-2
No full textCalsequestrin from different muscle tissues and species has been phosphorylated by casein kinase-1 and casein kinase-2, in the conditions previously reported by Cala and Jones (J. Biol. Chem. 266, 391-398, 1991). Results indicates that rabbit cardiac and skeletal calsequestrin and frog skeletal calsequestrin are phosphorylated by both casein kinase-1 and casein kinase-2, at variance with chicken skeletal calsequestrin which is a poor substrate for both enzymes. We also observed that chicken calsequestrin is able to inhibit phosphorylation of cardiac calsequestrin, as well as other specific substrates, when added together to the assay medium
Casein kinases and their protein substrates in rat liver cytosol: evidence for their participation in multimolecular systems.
No full textAutophosphorylation of type 2 casein kinase TS at both its alpha- and beta-subunits. Influence of different effectors.
No full textA new procedure for the measurement of the protein-kinase-catalyzed incorporation of the gamma-32P-phosphoryl group of ATP into phospho-proteins and phosphopeptides.
No full textA study with model substrates of the structure of the sites phosphorylated by rat liver casein kinase TS.
No full textStructural features determining the site specificity of a rat liver cAMP-independent protein kinase.
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