Properties of Tubulin treated with alkaline phosphatase to remove guanine nucleotides from the exchangeable binding site
- 1 December 1978
- journal article
- Published by Wiley in FEBS Letters
- Vol. 96 (1) , 83-86
- https://doi.org/10.1016/0014-5793(78)81067-9
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Opposite end assembly and disassembly of microtubules at steady state in vitroCell, 1978
- Nucleotide binding and phosphorylation in microtubule assembly in vitroJournal of Molecular Biology, 1977
- Microtubule-associated proteins and the stimulation of tubulin assembly in vitroBiochemistry, 1976
- Role of nucleotide hydrolysis in microtubule assemblyNature, 1976
- Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubulesBiochemistry, 1976
- Effect of guanine nucleotides on the assembly of brain microtubules: Ability of 5′-guanylyl imidodiphosphate to replace GTP in promoting the polymerization of microtubules in vitroBiochemical and Biophysical Research Communications, 1976
- Purification of Tubulin from Bovine Brain and Its Interaction with Guanine NucleotidesThe Journal of Biochemistry, 1975
- Interactions of tubulin with vinblastine and guanosine triphosphateJournal of Molecular Biology, 1972
- Colchicine-binding protein of mammalian brain and its relation to microtubulesBiochemistry, 1968
- Studies on calf-intestinal alkaline phosphatase I. Chromatographic purification, microheterogeneity and some other properties of the purified enzymeBiochimica et Biophysica Acta, 1961