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Li Y, Kobayashi H, Hashimoto Y, et al. Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins. Biochem Biophys Res Commun. 1992;187(2):722-9doi: 10.1016/0006-291x(92)91255-o.
Li, Y., Kobayashi, H., Hashimoto, Y., & Iwasaki, S. (1992). Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins. Biochemical and biophysical research communications, 187(2), 722-9. https://doi.org/10.1016/0006-291x(92)91255-o
Li, Y, et al. "Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins." Biochemical and biophysical research communications vol. 187,2 (1992): 722-9. doi: https://doi.org/10.1016/0006-291x(92)91255-o
Li Y, Kobayashi H, Hashimoto Y, Iwasaki S. Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins. Biochem Biophys Res Commun. 1992 Sep 16;187(2):722-9. doi: 10.1016/0006-291x(92)91255-o. PMID: 1530630.
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Biochem Biophys Res Commun. 1992 Sep 16;187(2):722-9. doi: 10.1016/0006-291x(92)91255-o.

Binding selectivity of rhizoxin, phomopsin A, vinblastine, and ansamitocin P-3 to fungal tubulins: differential interactions of these antimitotic agents with brain and fungal tubulins.

Biochemical and biophysical research communications

Y Li, H Kobayashi, Y Hashimoto, S Iwasaki

Affiliations

  1. Institute of Applied Microbiology, University of Tokyo, Japan.

PMID: 1530630 DOI: 10.1016/0006-291x(92)91255-o

Abstract

The binding of four potent antimitotic agents, rhizoxin (RZX), phomopsin A (PMS-A), ansamitocin P-3 (ASMP-3), and vinblastine (VLB), to tubulins from RZX-sensitive and -resistant strains of Aspergillus nidulans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae was investigated. Mycelial extracts to which RZX could bind contained beta-tubulin with Asn as the 100th amino acid residue (Asn-100) in all cases, and those without affinity for RZX contained beta-tubulins with either Ile-100 or Val-100. Though PMS-A shares the same binding site as RZX and ASMP-3 on porcine brain tubulin (Asn-100), only ASMP-3 bound Asn-100 fungal tubulins in a competitive manner with respect to RZX. PMS-A and VLB, which strongly bind to porcine brain tubulin, did not bind to any of the fungal mycelial extracts examined. The results indicate differential interactions of these antimitotic agents with brain and fungal tubulins.

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