These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Ustiloxins, new antimitotic cyclic peptides: interaction with porcine brain tubulin.
    Author: Li Y, Koiso Y, Kobayashi H, Hashimoto Y, Iwasaki S.
    Journal: Biochem Pharmacol; 1995 May 17; 49(10):1367-72. PubMed ID: 7763278.
    Abstract:
    Biochemical and electron microscopic studies demonstrated that ustiloxins A-D, which are antimitotic 13-membered cyclic peptides produced by the rice plant pathogen Ustilaginoidea virens, strongly inhibited the polymerization of porcine brain tubulin in vitro and depolymerized pre-formed microtubules. The IC50 values of polymerization inhibited by ustiloxins A-D were determined to be 0.7, 2.8, 4.4 and 6.6 microM, respectively, under the experimental conditions used, indicating that ustiloxin A is the most potent inhibitor of tubulin polymerization currently known. Ustiloxins A-C were found to inhibit the binding of radiolabelled rhizoxin to tubulin with inhibition constants (Ki) of 0.08, 0.13 and 0.23 microM, respectively, and also inhibited the binding of radiolabelled phomopsin A as strongly as rhizoxin. These results suggest that the binding site of ustiloxins is identical with that of rhizoxin.
    [Abstract] [Full Text] [Related] [New Search]