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Updated: May 12, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
Published on: August 6, 2020
Tripartin, a histone demethylase inhibitor from a bacterium associated with a dung beetle larva
Seong-Hwan Kim1, So Hee Kwon, Seon-Hui Park
1Natural Products Research Institute, College of Pharmacy, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-742, Republic of Korea.
Abstract:
Tripartin (1), a new dichlorinated indanone, was isolated from the culture broth of the Streptomyces sp. associated with a larva of the dung beetle Copris tripartitus Waterhouse. The planar structure of tripartin (1) was identified by the spectroscopic analyses of NMR, mass, UV, and IR data. The structure was confirmed, and the absolute configuration of 1 was determined by X-ray crystallography. Tripartin displayed specific activity as an inhibitor of the histone H3 lysine 9 demethylase KDM4 in HeLa cells.
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