EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction

Epigallocatechin gallate (EGCG) is a catechin flavonoid which induces apoptosis in cancerous cells, but the underlying molecular mechanisms remain poorly understood. Here authors use an interdisciplinary approach to show a direct interaction between EGCG and the tumor suppressor p53 and demonstrate...

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Autores principales:	Jing Zhao, Alan Blayney, Xiaorong Liu, Lauren Gandy, Weihua Jin, Lufeng Yan, Jeung-Hoi Ha, Ashley J. Canning, Michael Connelly, Chao Yang, Xinyue Liu, Yuanyuan Xiao, Michael S. Cosgrove, Sozanne R. Solmaz, Yingkai Zhang, David Ban, Jianhan Chen, Stewart N. Loh, Chunyu Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/bfe12496e2674532a1bf41a125983054
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spelling	oai:doaj.org-article:bfe12496e2674532a1bf41a1259830542021-12-02T12:14:49ZEGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction10.1038/s41467-021-21258-52041-1723https://doaj.org/article/bfe12496e2674532a1bf41a1259830542021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21258-5https://doaj.org/toc/2041-1723Epigallocatechin gallate (EGCG) is a catechin flavonoid which induces apoptosis in cancerous cells, but the underlying molecular mechanisms remain poorly understood. Here authors use an interdisciplinary approach to show a direct interaction between EGCG and the tumor suppressor p53 and demonstrate that EGCG inhibits ubiquitination of p53 by MDM2.Jing ZhaoAlan BlayneyXiaorong LiuLauren GandyWeihua JinLufeng YanJeung-Hoi HaAshley J. CanningMichael ConnellyChao YangXinyue LiuYuanyuan XiaoMichael S. CosgroveSozanne R. SolmazYingkai ZhangDavid BanJianhan ChenStewart N. LohChunyu WangNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jing Zhao Alan Blayney Xiaorong Liu Lauren Gandy Weihua Jin Lufeng Yan Jeung-Hoi Ha Ashley J. Canning Michael Connelly Chao Yang Xinyue Liu Yuanyuan Xiao Michael S. Cosgrove Sozanne R. Solmaz Yingkai Zhang David Ban Jianhan Chen Stewart N. Loh Chunyu Wang EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
description	Epigallocatechin gallate (EGCG) is a catechin flavonoid which induces apoptosis in cancerous cells, but the underlying molecular mechanisms remain poorly understood. Here authors use an interdisciplinary approach to show a direct interaction between EGCG and the tumor suppressor p53 and demonstrate that EGCG inhibits ubiquitination of p53 by MDM2.
format	article
author	Jing Zhao Alan Blayney Xiaorong Liu Lauren Gandy Weihua Jin Lufeng Yan Jeung-Hoi Ha Ashley J. Canning Michael Connelly Chao Yang Xinyue Liu Yuanyuan Xiao Michael S. Cosgrove Sozanne R. Solmaz Yingkai Zhang David Ban Jianhan Chen Stewart N. Loh Chunyu Wang
author_facet	Jing Zhao Alan Blayney Xiaorong Liu Lauren Gandy Weihua Jin Lufeng Yan Jeung-Hoi Ha Ashley J. Canning Michael Connelly Chao Yang Xinyue Liu Yuanyuan Xiao Michael S. Cosgrove Sozanne R. Solmaz Yingkai Zhang David Ban Jianhan Chen Stewart N. Loh Chunyu Wang
author_sort	Jing Zhao
title	EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
title_short	EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
title_full	EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
title_fullStr	EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
title_full_unstemmed	EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction
title_sort	egcg binds intrinsically disordered n-terminal domain of p53 and disrupts p53-mdm2 interaction
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/bfe12496e2674532a1bf41a125983054
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EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction

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