Adenosine 3':5'-monophosphate-regulated phosphorylation of erythrocyte membrane proteins. Separation of membrane-associated cyclic adenosine 3':5'-monophosphate-dependent protein kinase from its endogenous substrates
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. Subcellular Distribution of Adenosine 3',5'-Monophosphate-dependent Protein Kinase in Rat Brain
2. Cyclic Adenosine 3′,5′-Monophosphate-dependent Protein Kinase of Human Erythrocyte Membranes
3. Phosphorylation of an Endogenous Membrane Protein by an Endogenous, Membrane-associated Cyclic Adenosine 3′,5′-Monophosphate-dependent Protein Kinase in Human Erythrocyte Ghosts
4. The role of cyclic AMP in the phosphorylation of proteins in human erythrocyte membranes
5. Erythrocyte Protein Phosphorylation
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1. Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1990-10
2. Purification of Erythrocyte Dematin (protein 4.9) Reveals an Endogenous Protein Kinase That Modulates Actin-bundling Activity;Journal of Biological Chemistry;1989-05
3. Volume-dependent regulation of ion transport and membrane phosphorylation in human and rat erythrocytes;The Journal of Membrane Biology;1989-02
4. Erythrocyte membrane skeleton phosphoproteins: identification of two unrelated phosphoproteins in band 4.9;Biochimica et Biophysica Acta (BBA) - Biomembranes;1988-10
5. The role of calpain in the selective increased phosphorylation of the anion-transport protein in red cell of hypertensive subjects;Biochemical and Biophysical Research Communications;1988-02
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