Band 4.1 causes spectrin-actin gels to become thixiotropic
Authors:
- Carl M. CohenCCCarl M. Cohen
- Catherine KorsgrenCKCatherine Korsgren
- 1 December 1980
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 97 (4) , 1429-1435
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
- Spectrin-actin associations studied by electron microscopy of shadowed preparationsCell, 1980
- Spectrin-dependent and -independent association of F-actin with the erythrocyte membrane.Journal of Cell Biology, 1980
- Structural comparison of several actin-binding macromolecules.Journal of Cell Biology, 1980
- Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.Journal of Cell Biology, 1980
- Spectrin plus band 4.1 cross-link actin. Regulation by micromolar calcium.Journal of Cell Biology, 1980
- 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
- In vitro formation of a complex between cytoskeletal proteins of the human erythrocyteNature, 1979
- The role of spectrin in erythrocyte membrane-stimulated actin polymerisationNature, 1979
- The gelation of actin by actin-binding protein.Journal of Biological Chemistry, 1978
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951