The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Phomopsin A     (E)-2-[[(E)-2-[[(2S)-1- [[(3R,4S,7S,10S...

Synonyms: CHEMBL446991, SureCN1096541, AC1O5PXJ, LS-105926, C19955, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Phomopsin A

  • Monoclonal antibody (mAb) C3C11, which recognizes the antimicrotubule phomopsin mycotoxins, was used to isolate peptide mimics of phomopsin A from a random 15-mer phage display peptide library [1].
  • It was shown that the different toxic preparations containing similar amounts of phomopsin A varied substantially in toxicity [2].
  • Phomopsin, a hexapeptide mycotoxin contaminant of lupin plant and seed materials, was administered subcutaneously to adult rats at a daily dose rate of 30 micrograms/kg body weight (approximately 0.005 median lethal dose) for 2, 6 or 17 wks and the development of liver damage was observed during treatment and for up to 2 yr after [3].

High impact information on Phomopsin A


Biological context of Phomopsin A


Associations of Phomopsin A with other chemical compounds


Gene context of Phomopsin A

  • Like vinblastine, phomopsin A stabilizes colchicine binding to tubulin [11].

Analytical, diagnostic and therapeutic context of Phomopsin A


  1. Peptide mimotopes of phomopsins: identification, characterization and application in an immunoassay. Yu, M., Than, K., Colegate, S., Shiell, B., Michalski, W.P., Prowse, S., Wang, L.F. Mol. Divers. (2005) [Pubmed]
  2. Evidence that phomopsins A and B are not the only toxic metabolites produced by Phomopsis leptostromiformis. Allen, J.G., Hancock, G.R. Journal of applied toxicology : JAT. (1989) [Pubmed]
  3. Biliary hyperplasia and carcinogenesis in chronic liver damage induced in rats by phomopsin. Peterson, J.E. Pathology. (1990) [Pubmed]
  4. Natural products which interact with tubulin in the vinca domain: maytansine, rhizoxin, phomopsin A, dolastatins 10 and 15 and halichondrin B. Hamel, E. Pharmacol. Ther. (1992) [Pubmed]
  5. Tubulin sulfhydryl groups as probes and targets for antimitotic and antimicrotubule agents. Luduena, R.F., Roach, M.C. Pharmacol. Ther. (1991) [Pubmed]
  6. Effects of antimitotic agents on tubulin-nucleotide interactions. Correia, J.J. Pharmacol. Ther. (1991) [Pubmed]
  7. Localization of the antimitotic peptide and depsipeptide binding site on beta-tubulin. Mitra, A., Sept, D. Biochemistry (2004) [Pubmed]
  8. Interaction of phomopsin A with porcine brain tubulin. Inhibition of tubulin polymerization and binding at a rhizoxin binding site. Li, Y., Kobayashi, H., Tokiwa, Y., Hashimoto, Y., Iwasaki, S. Biochem. Pharmacol. (1992) [Pubmed]
  9. Dolastatin 10, a powerful cytostatic peptide derived from a marine animal. Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain. Bai, R., Pettit, G.R., Hamel, E. Biochem. Pharmacol. (1990) [Pubmed]
  10. Comparison of cellular effects of phomopsin and colcemid in Chinese hamster cells in vitro. Brown, J.K., Bick, Y.A. Cytobios (1986) [Pubmed]
  11. Effect of phomopsin A on the alkylation of tubulin. Ludueña, R.F., Roach, M.C., Prasad, V., Lacey, E. Biochem. Pharmacol. (1990) [Pubmed]
WikiGenes - Universities