dolastatin-10 has been researched along with rhizoxin* in 2 studies
1 review(s) available for dolastatin-10 and rhizoxin
| Article | Year |
|---|---|
Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B.
This paper summarizes published data on the interactions of tubulin with antimitotic compounds that inhibit the binding of vinca alkaloids to the protein. These are all relatively complex natural products isolated from higher plants, fungi and marine invertebrate animals. These agents are maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B and their congeners. Effects on tubulin polymerization, ligand binding interactions and structure-activity relationships are emphasized. Topics: Animals; Antibiotics, Antineoplastic; Antineoplastic Agents; Depsipeptides; Ethers, Cyclic; Lactones; Macrolides; Maytansine; Mycotoxins; Oligopeptides; Tubulin; Vinca Alkaloids | 1992 |
1 other study(ies) available for dolastatin-10 and rhizoxin
| Article | Year |
|---|---|
Interaction of marine toxin dolastatin 10 with porcine brain tubulin: competitive inhibition of rhizoxin and phomopsin A binding.
Dolastatin 10, a cytostatic peptide containing several unique amino acid subunits, was isolated from the marine shell-less mollusk Dolabella auricularia. It inhibits microtubule assembly at concentrations below 5.0 microM (IC50, 3.0 microM) and causes formation of tubulin aggregates at higher (> 10 microM) concentrations in a somewhat different manner from that caused by vinblastine. Electron microscopical analysis showed irregular aggregates of microtubule proteins in the presence of 10 microM dolastatin 10. Dolastatin 10 inhibited the binding of both radiolabeled rhizoxin and phomopsin A to tubulin with inhibition constants (Ki) of 7 x 10(-8) M and 1 x 10(-7) M, respectively. The results suggest that at least one of the binding sites of dolastatin 10 on tubulin is the rhizoxin binding site. Topics: Animals; Antineoplastic Agents; Binding Sites; Binding, Competitive; Brain; Depsipeptides; Lactones; Macrolides; Microscopy, Electron; Microtubules; Mollusca; Mycotoxins; Oligopeptides; Polymers; Swine; Tubulin | 1994 |