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Cited by 233

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Kinase Inhibitors from Polygonum cuspidatum

Open access
Jayatilake, Gamini S., Jayasuriya, Hiranthi, Lee, Eung-Seok, Koonchanok, Nuphavan M., Geahlen, Robert L., Ashendel, Curtis L., McLaughlin, Jerry L., Chang, Ching-Jer·1993·Journal of Natural Products

Abstract

Bioassay-directed fractionation of a medicinal plant, Polygonum cuspidatum (Polygonaceae), has led to the discovery of a hydroxystilbene, resveratrol [1], as an inhibitor of a protein-tyrosine kinase (p56lck) partially purified from bovine thymus. Both trans and cis isomers of resveratrol possess comparable protein-tyrosine kinase inhibitory activity. Comparison of the IC50 values of resveratrol for protein-tyrosine kinase inhibitory activity with those of piceid (resveratrol-O3-beta-glucoside) [2] and resveratrol-O4'-beta-glucoside [3] shows the requirement of free hydroxyl groups on both phenyl rings for the protein-tyrosine kinase inhibition. Protein kinase C inhibitory analysis suggests the requirements of two free hydroxyl groups on one phenyl ring only.

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Authors
Jayatilake, G. S., Jayasuriya, H., Lee, E.-S., Koonchanok, N. M., Geahlen, R. L., Ashendel, C. L., McLaughlin, J. L., & Chang, C.-J.
Venue
Journal of Natural Products
Published
1993-10
Volume
56
Issue
10
Pages
1805-1810
ISSN
  • 0163-3864 (ISSN-L)
  • 1520-6025
OpenAlex
W1987062124
Cited by
233
References
0
FWCI
5.80
Type
journal article
Language
en
Open access
hybrid

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