Journal ArticleDOI
The structure and synthesis of dolastatin 3
George R. Pettit,Yoshiaki Kamano,Cedric W. Holzapfel,Cedric W. Holzapfel,Wynand J. Van Zyl,Wynand J. Van Zyl,Albert A. Tuinman,Albert A. Tuinman,Cherry L. Herald,L. Baczynskyj,L. Baczynskyj,Jean M. Schmidt +11 more
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This article is published in Journal of the American Chemical Society.The article was published on 1987-11-01. It has received 56 citations till now.read more
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Dolastatin 10, a powerful cytostatic peptide derived from a marine animal: Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain
TL;DR: Pettit et al. as mentioned in this paper showed that dolastatin 10 inhibited tubulin polymerization and the binding of radiolabeled vinblastine to tubulin.
Journal ArticleDOI
Cyclic peptides and depsipeptides from cyanobacteria: a review.
TL;DR: An elaborate array of structurally-novel and biologically-active cyclic peptides and depsipeptides are found in blue-green algae (cyanobacteria) as mentioned in this paper.
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MICROALGAL METABOLITES: A New Perspective
TL;DR: Occurrence of secondary metabolites in microalgae (protoctista) is discussed with respect to the phylogenic or taxonomic relationships of organisms.
Journal ArticleDOI
Natural products which interact with tubulin in the vinca domain: Maytansine, rhizoxin, phomopsin a, dolastatins 10 and 15 and halichondrin B
TL;DR: This paper summarizes published data on the interactions of tubulin with antimitotic compounds that inhibit the binding of vinca alkaloids to the protein to highlight effects on tubulin polymerization, ligand binding interactions and structure-activity relationships.
Journal ArticleDOI
Isolation of dolastatins 10–15 from the marine mollusc dolabella auricularia☆☆☆
George R. Pettit,Yoshiaki Kamano,Cherry L. Herald,Youichi Fujii,Haruhisa Kizu,Michael R. Boyd,Fred E. Boettner,Dennis L. Doubek,Jean M. Schmidt,Jean-Charles Chapuis,Claude Michel +10 more
TL;DR: Intensive Study of the cell growth inhibition and antineoplastic constituents of the sea hare Dolabella auricularia provided the structurally unique peptides designated dolastatins 1-15, which represents the largest scale separation ofSea hare components.