Steady-state head-to-tail polymerization of actin or microtubules. II. Two-state and three-state kinetic cycles
- 1 March 1981
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 33 (3), 353-371
- https://doi.org/10.1016/s0006-3495(81)84900-4
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Bioenergetic aspects and polymer length distribution in steady-state head-to-tail polymerization of actin or microtubules.Proceedings of the National Academy of Sciences, 1980
- Implications of treadmilling for the stability and polarity of actin and tubulin polymers in vivo.The Journal of cell biology, 1980
- The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization.Journal of Biological Chemistry, 1980
- Head-to-tail polymerization of microtubules in vitro. Electron microscope analysis of seeded assembly.The Journal of cell biology, 1980
- Cytochalasin B and the structure of actin gelsJournal of Molecular Biology, 1979
- Exchange of ADP, ATP and 1:N6‐Ethenoadenosine 5′‐Triphosphate at G‐ActinEuropean Journal of Biochemistry, 1979
- "Viral" expansion of enzyme flux and use of quasi-chemical approximation for two-state enzymes with enzyme-enzyme interactions.Proceedings of the National Academy of Sciences, 1977
- Further study of the effect of enzyme-enzyme interactions on steady-state enzyme kinetics.Proceedings of the National Academy of Sciences, 1977
- Theoretical study of the effect of enzyme-enzyme interactions on steady-state enzyme kinetics.Proceedings of the National Academy of Sciences, 1977
- Head to tail polymerization of actinJournal of Molecular Biology, 1976