All Outputs (7)

Generation of red blood cells from stem cells: Achievements, opportunities and perspectives for malaria research (2022)
Journal Article
Satchwell, T. J. (2022). Generation of red blood cells from stem cells: Achievements, opportunities and perspectives for malaria research. Frontiers in Cellular and Infection Microbiology, 12, Article 1039520. https://doi.org/10.3389/fcimb.2022.1039520

Parasites of the genus Plasmodium that cause malaria survive within humans by invasion of, and proliferation within, the most abundant cell type in the body, the red blood cell. As obligate, intracellular parasites, interactions between parasite and... Read More about Generation of red blood cells from stem cells: Achievements, opportunities and perspectives for malaria research.

Erythrocyte invasion receptors for Plasmodium falciparum: New and old (2016)
Journal Article
Satchwell, T. J. (2016). Erythrocyte invasion receptors for Plasmodium falciparum: New and old. Transfusion Medicine, 26(2), 77-88. https://doi.org/10.1111/tme.12280

Understanding the complex process by which the invasive form of the Plasmodium falciparum parasite, the merozoite, attaches to and invades erythrocytes as part of its blood stage life cycle represents a key area of research in the battle to combat ma... Read More about Erythrocyte invasion receptors for Plasmodium falciparum: New and old.

The sorting of blood group‐active proteins during enucleation (2015)
Journal Article
Satchwell, T. J., Bell, A. J., & Toye, A. M. (2015). The sorting of blood group‐active proteins during enucleation. ISBT Science Series, 10(S1), 163-168. https://doi.org/10.1111/voxs.12127

Enucleation represents the critical stage during red blood cell development when the nucleus is extruded from an orthochromatic erythroblast in order to generate a nascent immature reticulocyte. Extrusion of the nucleus results in loss of a proportio... Read More about The sorting of blood group‐active proteins during enucleation.

Refined views of multi-protein complexes in the erythrocyte membrane (2012)
Journal Article
Mankelow, T. J., Satchwell, T. J., & Burton, N. M. (2012). Refined views of multi-protein complexes in the erythrocyte membrane. Blood Cells, Molecules and Diseases, 49(1), 1-10. https://doi.org/10.1016/j.bcmd.2012.03.001

The erythrocyte membrane has been extensively studied, both as a model membrane system and to investigate its role in gas exchange and transport. Much is now known about the protein components of the membrane, how they are organised into large multi-... Read More about Refined views of multi-protein complexes in the erythrocyte membrane.

Anion exchanger 1 in red blood cells and kidney: Band 3's in a pod (2011)
Journal Article
Wu, F., Satchwell, T. J., & Toye, A. M. (2011). Anion exchanger 1 in red blood cells and kidney: Band 3's in a pod. Biochemistry and Cell Biology, 89(2), 106-114. https://doi.org/10.1139/O10-146

The bicarbonate/chloride exchanger 1 (AE1, Band 3) is abundantly expressed in the red blood cell membrane, where it is involved in gas exchange and functions as a major site of cytoskeletal attachment to the erythrocyte membrane. A truncated kidney i... Read More about Anion exchanger 1 in red blood cells and kidney: Band 3's in a pod.

Band 3 multiprotein complexes in the red cell membrane; of mice and men (2010)
Journal Article
van den Akker, E., Satchwell, T. J., Williamson, R. C., & Toye, A. M. (2010). Band 3 multiprotein complexes in the red cell membrane; of mice and men. Blood Cells, Molecules and Diseases, 45(1), 1-8. https://doi.org/10.1016/j.bcmd.2010.02.019

The bicarbonate/chloride exchanger band 3 (Anion Exchanger 1, AE1) is the most abundant protein in the erythrocyte membrane, it has an important role in gas exchange and functions as a point of attachment for the cytoskeletons maintaining the mechani... Read More about Band 3 multiprotein complexes in the red cell membrane; of mice and men.

Protein 4.2 : A complex linker (2009)
Journal Article
Satchwell, T. J., Shoemark, D. K., Sessions, R. B., & Toye, A. M. (2009). Protein 4.2 : A complex linker. Blood Cells, Molecules and Diseases, 42(3), 201-210. https://doi.org/10.1016/j.bcmd.2009.01.005

The peripheral membrane protein, protein 4.2, is one of the most abundant protein components of the erythrocyte membrane. Protein 4.2 has an important role in red cell membrane structure, its absence due to natural mutations in humans or gene knockou... Read More about Protein 4.2 : A complex linker.