Characterization of the hypertonically induced tyrosine phosphorylation of erythrocyte band 3.
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Summary
It is hypothesized that shrinkage-induced tyrosine phosphorylation results from an excluded-volume effect, stemming from an increase in intracellular crowding, or from changes in membrane curvature that accompany the decrease in cell volume.
- Type
- article
- Published
- 1998-10-15
- Cited by
- 48
- References
- 1
- Access
- Open access
- OpenAlex
- https://openalex.org/W1874922015
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:7859913
Keywords
Phosphorylation, Tyrosine phosphorylation, Tyrosine, Band 3, Protein tyrosine phosphatase
References
Cited by
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- Differential sorting of tyrosine kinases and phosphotyrosine phosphatases acting on band 3 during vesiculation of human erythrocytes.
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- Regulation of K-Cl cotransport by Syk and Src protein tyrosine kinases in deoxygenated sickle cells
- A Transport Metabolon
- Protein kinases activities in erythrocyte membranes of asphyxiated newborns.
- Erythrocytes anion transport and oxidative change in β‐thalassaemias
- Blood or spores? A cautionary note on interpreting cellular debris on human skeletal remains
- Antibiotic effects on SO 42− uptake in human erythrocytes
- Human red blood cells alterations in primary aldosteronism.
- Sulphate and Chloride-Dependent Potassium Transport in Human Erythrocytes are Affected by Crude Venom from Nematocysts of the Jellyfish Pelagia noctiluca
- Human kidney anion exchanger 1 localisation in MDCK cells is controlled by the phosphorylation status of two critical tyrosines
- Phosphotyrosine phosphatases acting on band 3 in human erythrocytes of different age: PTP1B processing during cell ageing.
- Effect of glycyrrhetinic acid on membrane band 3 in human erythrocytes.
- Deoxygenation of sickle cells stimulates Syk tyrosine kinase and inhibits a membrane tyrosine phosphatase.
- Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3.
- Band 3 tyr-phosphorylation in human erythrocytes from non-pregnant and pregnant women.
- Chemical and Pathological Oxidative Influences on Band 3 Protein Anion-exchanger
- Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes.
- Anion permeability and erythrocyte swelling.
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