Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein

Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.

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Autores principales:	Tiantian Fang, Wanbiao Chen, Yaping Sheng, Siming Yuan, Qiaowei Tang, Gongyu Li, Guangming Huang, Jihu Su, Xuan Zhang, Jianye Zang, Yangzhong Liu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/eb788873ae41467b98ebc2094c4d5779
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

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spelling	oai:doaj.org-article:eb788873ae41467b98ebc2094c4d57792021-12-02T16:50:58ZTetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein10.1038/s41467-018-08102-z2041-1723https://doaj.org/article/eb788873ae41467b98ebc2094c4d57792019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-08102-zhttps://doaj.org/toc/2041-1723Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.Tiantian FangWanbiao ChenYaping ShengSiming YuanQiaowei TangGongyu LiGuangming HuangJihu SuXuan ZhangJianye ZangYangzhong LiuNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tiantian Fang Wanbiao Chen Yaping Sheng Siming Yuan Qiaowei Tang Gongyu Li Guangming Huang Jihu Su Xuan Zhang Jianye Zang Yangzhong Liu Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
description	Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.
format	article
author	Tiantian Fang Wanbiao Chen Yaping Sheng Siming Yuan Qiaowei Tang Gongyu Li Guangming Huang Jihu Su Xuan Zhang Jianye Zang Yangzhong Liu
author_facet	Tiantian Fang Wanbiao Chen Yaping Sheng Siming Yuan Qiaowei Tang Gongyu Li Guangming Huang Jihu Su Xuan Zhang Jianye Zang Yangzhong Liu
author_sort	Tiantian Fang
title	Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
title_short	Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
title_full	Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
title_fullStr	Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
title_full_unstemmed	Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
title_sort	tetrathiomolybdate induces dimerization of the metal-binding domain of atpase and inhibits platination of the protein
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/eb788873ae41467b98ebc2094c4d5779
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Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein

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