Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change
- 1 September 1981
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 293 (5830) , 302-305
- https://doi.org/10.1038/293302a0
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cellsNature, 1980
- Identification of membrane proteins mediating the interaction of human plateletsThe Journal of cell biology, 1980
- Mechanism of action of cytochalasin B on actinCell, 1980
- Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay.Proceedings of the National Academy of Sciences, 1979
- Cytochalasin inhibits the rate of elongation of actin filament fragmentsThe Journal of cell biology, 1979
- Actin polymerization induced by a motility-related high-affinity cytochalasin binding complex from human erythrocyte membraneProceedings of the National Academy of Sciences, 1979
- Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease ICell, 1978
- Effects of Cytochalasin B on Actin FilamentsPublished by Cold Spring Harbor Laboratory ,1973
- Microfilaments in Cellular and Developmental ProcessesScience, 1971
- Microfibrils of blood platelets: their relationship to microtubules and the contractile proteinJournal of Clinical Investigation, 1969