The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the okadaic acid (strong inhibitor of P-Ser/Thr-protein phosphatase(s)), is accompanied by a release of casein kinase from the membrane into cytosol. Such an intracellular translocation might provide a feedback mechanism for the regulation of the casein kinase catalyzed phosphorylation of membrane proteins in the human erythrocytes. (C) 1994 Academic Press, Inc
Indirect evidence has suggested that K-Cl cotransport in human and sheep erythrocytes is activated p...
The protein kinase activity located in the cytosol of hereditary spherocytosis erythrocytes is due t...
Protein phosphorylation is a nearly universal mechanism used by cells to regulate intracellular and ...
The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the ...
Membrane proteins of human erythrocytes can be phosphorylated not only by membrane casein kinase (MS...
The endogenous phosphorylation of human erythrocyte cytosolic proteins is markedly increased when th...
The endogenous phosphorylation of human erythrocyte cytosolic proteins is markedly increased when th...
Casein kinase and histone kinase(s) are solubilized from human erythrocyte membranes by buffered ion...
Casein kinase and histone kinase(s) are solubilized from human erythrocyte membranes by buffered ion...
AbstractThe relationship and substrate specificity of the human erythrocyte membrane kinase and case...
Both cytosol and membranes of human erythrocytes display protein kinase activity towards exogenous p...
The pH-dependence of the distribution of Tyr- and Ser/Thr-protein kinases between cytosol and membra...
Two cyclic AMP-independent casein kinases can be isolated from human erythrocyte hemolysate, one of ...
The pH-dependence of the distribution of Tyr- and Ser/Thr-protein kinases between cytosol and membra...
Okadaic acid, penetrating the human erythrocytes, almost completely inhibits P-Ser-protein phosphata...
Indirect evidence has suggested that K-Cl cotransport in human and sheep erythrocytes is activated p...
The protein kinase activity located in the cytosol of hereditary spherocytosis erythrocytes is due t...
Protein phosphorylation is a nearly universal mechanism used by cells to regulate intracellular and ...
The present paper shows that an increased phosphorylation of the membrane proteins, promoted by the ...
Membrane proteins of human erythrocytes can be phosphorylated not only by membrane casein kinase (MS...
The endogenous phosphorylation of human erythrocyte cytosolic proteins is markedly increased when th...
The endogenous phosphorylation of human erythrocyte cytosolic proteins is markedly increased when th...
Casein kinase and histone kinase(s) are solubilized from human erythrocyte membranes by buffered ion...
Casein kinase and histone kinase(s) are solubilized from human erythrocyte membranes by buffered ion...
AbstractThe relationship and substrate specificity of the human erythrocyte membrane kinase and case...
Both cytosol and membranes of human erythrocytes display protein kinase activity towards exogenous p...
The pH-dependence of the distribution of Tyr- and Ser/Thr-protein kinases between cytosol and membra...
Two cyclic AMP-independent casein kinases can be isolated from human erythrocyte hemolysate, one of ...
The pH-dependence of the distribution of Tyr- and Ser/Thr-protein kinases between cytosol and membra...
Okadaic acid, penetrating the human erythrocytes, almost completely inhibits P-Ser-protein phosphata...
Indirect evidence has suggested that K-Cl cotransport in human and sheep erythrocytes is activated p...
The protein kinase activity located in the cytosol of hereditary spherocytosis erythrocytes is due t...
Protein phosphorylation is a nearly universal mechanism used by cells to regulate intracellular and ...