Inhibition of tubulin polymerization with ribose-modified analogs of GDP and GTP reduced inhibition with microtubule-associated proteins and magnesium
- 24 January 1984
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - General Subjects
- Vol. 797 (1) , 117-127
- https://doi.org/10.1016/0304-4165(84)90390-8
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Stoichiometry and role of GTP hydrolysis in bovine neurotubule assemblyJournal of Biological Chemistry, 1978
- Kinetic analysis of cooperativity in tubulin polymerization in the presence of guanosine di- or triphosphate nucleotidesBiochemistry, 1978
- Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.Proceedings of the National Academy of Sciences, 1977
- Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulinJournal of Molecular Biology, 1977
- Nucleotide binding and phosphorylation in microtubule assembly in vitroJournal of Molecular Biology, 1977
- Role of GTP in the Assembly of MicrotubulesThe Journal of Biochemistry, 1977
- Microtubule Assembly in vitro. Purification of Assembly-Promoting FactorsEuropean Journal of Biochemistry, 1977
- Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.Journal of Biological Chemistry, 1977
- In vitro assembly of pure tubulin into microtubules in the absence of microtubule-associated proteins and glycerol.Proceedings of the National Academy of Sciences, 1977
- Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubulesBiochemistry, 1976