Synthetic peptide substrates for casein kinase 2. Assessment of minimum structural requirements for phosphorylation
- 1 October 1988
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 971 (3), 332-338
- https://doi.org/10.1016/0167-4889(88)90149-8
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Structure and phosphorylation of eukaryotic initiation factor 2. Casein kinase 2 and protein kinase C phosphorylate distinct but adjacent sites in the β-subunitBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1988
- Phosphorylation of nucleolin by a nucleolar type NII protein kinaseBiochemistry, 1987
- Phosphorylation in vitro of human fibrinogen with casein kinase TS and characterization of phosphorylated sitesArchives of Biochemistry and Biophysics, 1987
- Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactionsBiochemical Journal, 1985
- Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type-2).Journal of Biological Chemistry, 1984
- Subunit structure and autophosphorylation mechanism of casein kinase-TS (type-2) from rat liver cytosolEuropean Journal of Biochemistry, 1984
- Polyamines and heparin do not appreciably influence phosphorylation of chromatin proteins HMG 14 and HMG 17 by nuclear protein kinase IIBiochimica et Biophysica Acta (BBA) - General Subjects, 1984
- Casein Kinases—Multipotential Protein KinasesCurrent Topics in Cellular Regulation, 1982
- Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinasesBiochimie, 1981
- Cyclic Nucleotide‐Independent Protein Kinases from Rabbit ReticulocytesEuropean Journal of Biochemistry, 1979