Diversity in protein associations of the spectrin-based membrane skeleton of nonerythroid cells
- 1 June 1988
- journal article
- Published by Springer Nature in Protoplasma
- Vol. 145 (2-3) , 89-94
- https://doi.org/10.1007/bf01349343
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors.The Journal of cell biology, 1987
- The neural cell spectrin skeleton: a reviewAmerican Journal of Physiology-Cell Physiology, 1986
- Colocalization of Band 3 with Ankyrin and Spectrin at the Basal Membrane of Intercalated Cells in the Rat KidneyScience, 1985
- Visualization of the protein associations in the erythrocyte membrane skeleton.Proceedings of the National Academy of Sciences, 1985
- THE MEMBRANE SKELETON OF HUMAN ERYTHROCYTES AND ITS IMPLICATIONS FOR MORE COMPLEX CELLSAnnual Review of Biochemistry, 1985
- Anion transporter: highly cell-type-specific expression of distinct polypeptides and transcripts in erythroid and nonerythroid cells.The Journal of cell biology, 1985
- Fodrin is the general spectrin-like protein found in most cells whereas spectrin and the TW protein have a restricted distributionCell, 1983
- Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrinNature, 1982
- Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.Proceedings of the National Academy of Sciences, 1982
- Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissuesNature, 1979