Band 3, the major transmembrane multifunctional protein of human erythrocytes, has been found to be phosphorylated-dephosphorylated on both Ser/Thr- and Tyr-residues by specific protein kinases and protein phosphatases. The results reported here would indicate that the ghosts prepared from human erythrocytes pretreated with DIDS, well known inhibitor of band 3-mediated anion transport, exhibit a markedly reduced Ser/Thr-phosphorylation of spectrin and band 3, when incubated with [gamma-32P]ATP in the presence of Mg2+. On the other hand, Tyr-phosphorylation of this latter protein is practically unchanged or even slightly enhanced. This suggests that Ser/Thr- and Tyr-phosphorylation of band 3 display a different functional role
Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogeno...
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...
Band 3, the major transmembrane multifunctional protein of human erythrocytes, has been found to be ...
The response of serine/threonine-phosphorylation of the major transmembrane protein (band 3) in huma...
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a ...
The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constit...
The Tyr-phosphorylation of the cytoplasmic domain of the major membrane-spanning band 3, rather than...
One of the most intensively studied post-translational modifications of erythrocyte proteins is the ...
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a ...
AbstractOxidative stress-induced tyrosine phosphorylation has been ascribed to activation of phospho...
Abstract: SHP-1 is a SH2-domain containing protein Tyr-phosphatase expressed in hematopoietic cell l...
Band 3, the most abundant erythrocyte membrane protein, mediates one-for-one· exchange of cr and ...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
Previous studies demonstrated that the in vitro tyrosine phosphorylation of the human erythrocyte an...
Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogeno...
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...
Band 3, the major transmembrane multifunctional protein of human erythrocytes, has been found to be ...
The response of serine/threonine-phosphorylation of the major transmembrane protein (band 3) in huma...
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a ...
The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constit...
The Tyr-phosphorylation of the cytoplasmic domain of the major membrane-spanning band 3, rather than...
One of the most intensively studied post-translational modifications of erythrocyte proteins is the ...
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a ...
AbstractOxidative stress-induced tyrosine phosphorylation has been ascribed to activation of phospho...
Abstract: SHP-1 is a SH2-domain containing protein Tyr-phosphatase expressed in hematopoietic cell l...
Band 3, the most abundant erythrocyte membrane protein, mediates one-for-one· exchange of cr and ...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
Previous studies demonstrated that the in vitro tyrosine phosphorylation of the human erythrocyte an...
Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogeno...
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...