@article{oai:tsukuba.repo.nii.ac.jp:00039948, author = {臼井, 健郎 and 木越, 英夫 and Hayakawa, Ichiro and Shioda, Shuya and Chinen, Takumi and Hatanaka, Taisei and Ebisu, Haruna and Sakakura, Akira and Usui, Takeo and 木越, 英夫}, issue = {21}, journal = {Bioorganic & Medicinal Chemistry}, month = {Nov}, note = {We have discovered O6-benzyl glaziovianin A, which showed stronger inhibition of microtubule polymerization (IC50 = 2.1 μM) than known α,β-tubulin inhibitors, such as colchicine and glaziovianin A. Also, we performed competition binding experiments of O6-benzyl glaziovianin A and revealed that O6-benzyl glaziovianin A binds to the colchicine binding site with high affinity. It is interesting that glaziovianin A derivatives change their mode of action in benzylation at the O6 (α,β-tubulin inhibitor) or O7 (γ-tubulin-specific inhibitor) position.}, pages = {5639--5645}, title = {Discovery of O6-benzyl glaziovianin A, a potent cytotoxic substance and a potent inhibitor of α,β-tubulin polymerization}, volume = {24}, year = {2016}, yomi = {キゴシ, ヒデオ} }