Purified tyrosine kinases, the EGF receptor kinase and the src kinase, can catalyze the phosphorylation of the band 3 protein from human erythrocytes
- 1 March 1986
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 135 (3) , 720-727
- https://doi.org/10.1016/0006-291x(86)90988-5
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Primary structure and transmembrane orientation of the murine anion exchange proteinNature, 1985
- Stimulation of tyrosine-specific phosphorylation in vitro by insulin-like growth factor INature, 1983
- High tyrosine kinase activity in normal nonproliferating cellsNature, 1983
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free systemNature, 1982
- Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factorNature, 1982
- The Molecular Basis for Membrane – Cytoskeleton Association in Human ErythrocytesJournal of Cellular Biochemistry, 1982
- The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranesNature, 1979
- Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membraneBiochemistry, 1976
- THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANEThe Journal of cell biology, 1974
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971