Mutagenesis of ?-tubulin cysteine residues inSaccharomyces cerevisiae: Mutation of cysteine 354 results in cold-stable microtubules
Author:
Publisher
Wiley
Subject
Cell Biology,Structural Biology
Reference40 articles.
1. Identification of the cysteine residue of .beta.-tubulin alkylated by the antimitotic agent 2,4-dichlorobenzyl thiocyanate, facilitated by separatio of the protein subunits of tubulin by hydrophobic column chromatography
2. Identification of Cysteine 354 of β-Tubulin as Part of the Binding Site for the A Ring of Colchicine
3. Direct Photoaffinity Labeling of Cysteine 211 or a Nearby Amino Acid Residue of β-Tubulin by Guanosine 5′-Diphosphate Bound in the Exchangeable Site
4. The Colchicine-Binding and Pyrene-Excimer-Formation Activities of Tubulin Involve a Common Cysteine Residue in the beta Subunit
5. Chapter 3 Isolation of Yeast DNA
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