Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin.
Open Access
- 1 February 1980
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (3) , 835-838
- https://doi.org/10.1016/s0021-9258(19)86105-7
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.The Journal of cell biology, 1980
- Actin polymerization induced by a motility-related high-affinity cytochalasin binding complex from human erythrocyte membraneProceedings of the National Academy of Sciences, 1979
- High affinity binding of [3H]dihydrocytochalasin B to peripheral membrane proteins related to the control of cell shape in the human red cell.Journal of Biological Chemistry, 1978
- Comparative biochemistry of non-muscle actins.Journal of Biological Chemistry, 1977
- High affinity cytochalasin B binding to red cell membrane proteins which are unrelated to sugar transport.Journal of Biological Chemistry, 1977
- Characterization of cytoplasmic actin isolated from Acanthamoeba castellanii by a new method.Journal of Biological Chemistry, 1976
- Determination of protein: A modification of the lowry method that gives a linear photometric responseAnalytical Biochemistry, 1972
- Electron Microscopic Particle Length of F-Actin Polymerized in VitroThe Journal of Biochemistry, 1970
- The cooperative nature of G-F transformation of actinBiochimica et Biophysica Acta, 1962
- The G - F equilibrium in actin solutions under various conditionsBiochimica et Biophysica Acta, 1962