Related Experiment Video
Updated: Aug 21, 2026

Identifying Inhibitors of the HBx-DDB1 Interaction Using a Split Luciferase Assay System
Published on: December 21, 2019
Unprecedented olefin-dependent histidine-kinase inhibitory of zerumbone ring-opening material
Takashi Kitayama1, Risa Iwabuchi, Shu Minagawa
1Advanced Life Science, Graduate School of Agriculture, Kinki University, Nara 631-8505, Japan.
Abstract:
Zerumbone ring-opening derivative, 4 (10E/10Z=3/2), inhibited autophosphorylation of the essential histidine-kinase YycG existing in Bacillus subtilis constituting a two-component system (TCS). Generation of 4E-form could be regulated chemically using the difference from the ring-opening reactivity of the precursor forming of 4 and pure 4E was isolated. The stereoisomer, 4E, showed main inhibition activity of autophosphorylation of YycG (IC(50)=63.5 microM).
Related Concept Videos
Base-Catalyzed Ring-Opening of Epoxides
Inhibitors of Bacterial DNA Synthesis
Radical Chain-Growth Polymerization: Overview
ortho–para-Directing Deactivators: Halogens
Ziegler–Natta Chain-Growth Polymerization: Overview
ortho–para-Directing Activators: –CH3, –OH, –⁠NH2, –OCH3
