Ca2+ control of actin filament length. Effects of macrophage gelsolin on actin polymerization.
Open Access
- 1 September 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (18), 9693-9697
- https://doi.org/10.1016/s0021-9258(19)68818-6
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Detection of actin assembly by fluorescence energy transfer.The Journal of cell biology, 1981
- A platelet inhibitor protein with cytochalasin-like activity against actin polymerization in vitroCell, 1980
- Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-associationBiochemical and Biophysical Research Communications, 1980
- Electron microscopy of thin filaments decorated with a Ca2+-regulated myosinJournal of Molecular Biology, 1980
- Cytochalasin B and the structure of actin gelsJournal of Molecular Biology, 1979
- Head to tail polymerization of actinJournal of Molecular Biology, 1976
- Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method.The Journal of cell biology, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Substructure of the myosin moleculeJournal of Molecular Biology, 1969
- Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscleJournal of Molecular Biology, 1963