Phosphorylation of αs2-casein by two rat liver ‘casein kinases’
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(78)81176-4/fullpdf
Reference15 articles.
1. Phosphorylation of casein fractions by rat liver ‘phosvitin kinase’
2. Casein phosphatase dependent dephosphorylation of 32P-casein fractions labelled by two protein kinases
3. Different susceptibility of whole casein components to enzymatic phosphorylation by two forms of rat liver ‘casein kinase’
4. Premiers elements de structure primaire des caseines αs2 bovines
5. Complete amino acid sequence of bovine αS2 -casein
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1. “Genuine” Casein Kinase (Fam20C): The Mother of the Phosphosecretome;Kinomics;2015-09-25
2. Substrate Specificity of the Nuclear Protein Kinase NII from Porcine Liver;European Journal of Biochemistry;2005-03-03
3. Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity;Critical Reviews in Oral Biology & Medicine;1997-10
4. In vitro Phosphorylation of Mouse Osteopontin Expressed in E. coli;Biochemical and Biophysical Research Communications;1993-02
5. Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1;Biochemistry;1992-06-30
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