Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions |
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Authors: | Singh S B Zink D L Liesch J M Dombrowski A W Darkin-Rattray S J Schmatz D M Goetz M A |
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Institution: | Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. sheo_singh@merck.com |
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Abstract: | structure: see text]. Isolation and structure elucidation of two novel cyclic tetrapeptides that show a variety of potent antiprotozoal activities by reversibly inhibiting HDAC have been reported. These are the new members of a unique family of cyclic tetrapeptides that do not require the electrophilic alpha-epoxyketone moiety of HC-toxin, trapoxin A, or chlamydocin for their potent activities against HDAC and the malarial parasite. |
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