Spectrin-actin associations studied by electron microscopy of shadowed preparations
- 1 October 1980
- Vol. 21 (3) , 875-883
- https://doi.org/10.1016/0092-8674(80)90451-1
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erythrocyte cytoskeleton.Journal of Biological Chemistry, 1980
- Spectrin-actin interaction. Phosphorylated and dephosphorylated spectrin tetramer cross-link F-actin.Journal of Biological Chemistry, 1979
- Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1.Proceedings of the National Academy of Sciences, 1979
- In vitro formation of a complex between cytoskeletal proteins of the human erythrocyteNature, 1979
- The molecular structure of human erythrocyte spectrinJournal of Molecular Biology, 1979
- Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.Proceedings of the National Academy of Sciences, 1979
- Identification by peptide analysis of the spectrin-binding protein in human erythrocytesJournal of Biological Chemistry, 1979
- Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrinJournal of Biological Chemistry, 1979
- Triton shells of intact erythrocytesJournal of Supramolecular Structure, 1978
- Interaction of filamin with f-actin in solution.Proceedings of the National Academy of Sciences, 1977