Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule

Microtubule assembly and disassembly is the target of many anticancer therapies, with β-tubulin the most-frequent target. Here, the authors used biochemical and biophysical techniques to demonstrate pironetin binds to α-tubulin and thereby inhibits microtubule polymerization providing a basis for th...

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Autores principales:	Jianhong Yang, Yuxi Wang, Taijing Wang, Jian Jiang, Catherine H. Botting, Huanting Liu, Qiang Chen, Jinliang Yang, James H. Naismith, Xiaofeng Zhu, Lijuan Chen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/706d09f37b2b4e7daab3ae36d7438e61
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spelling	oai:doaj.org-article:706d09f37b2b4e7daab3ae36d7438e612021-12-02T15:35:46ZPironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule10.1038/ncomms121032041-1723https://doaj.org/article/706d09f37b2b4e7daab3ae36d7438e612016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms12103https://doaj.org/toc/2041-1723Microtubule assembly and disassembly is the target of many anticancer therapies, with β-tubulin the most-frequent target. Here, the authors used biochemical and biophysical techniques to demonstrate pironetin binds to α-tubulin and thereby inhibits microtubule polymerization providing a basis for the rational design of novel anticancer drugs.Jianhong YangYuxi WangTaijing WangJian JiangCatherine H. BottingHuanting LiuQiang ChenJinliang YangJames H. NaismithXiaofeng ZhuLijuan ChenNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jianhong Yang Yuxi Wang Taijing Wang Jian Jiang Catherine H. Botting Huanting Liu Qiang Chen Jinliang Yang James H. Naismith Xiaofeng Zhu Lijuan Chen Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
description	Microtubule assembly and disassembly is the target of many anticancer therapies, with β-tubulin the most-frequent target. Here, the authors used biochemical and biophysical techniques to demonstrate pironetin binds to α-tubulin and thereby inhibits microtubule polymerization providing a basis for the rational design of novel anticancer drugs.
format	article
author	Jianhong Yang Yuxi Wang Taijing Wang Jian Jiang Catherine H. Botting Huanting Liu Qiang Chen Jinliang Yang James H. Naismith Xiaofeng Zhu Lijuan Chen
author_facet	Jianhong Yang Yuxi Wang Taijing Wang Jian Jiang Catherine H. Botting Huanting Liu Qiang Chen Jinliang Yang James H. Naismith Xiaofeng Zhu Lijuan Chen
author_sort	Jianhong Yang
title	Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
title_short	Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
title_full	Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
title_fullStr	Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
title_full_unstemmed	Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
title_sort	pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/706d09f37b2b4e7daab3ae36d7438e61
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Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule

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