Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer

The hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling.

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Autores principales: Giada Zurlo, Xijuan Liu, Mamoru Takada, Cheng Fan, Jeremy M. Simon, Travis S. Ptacek, Javier Rodriguez, Alex von Kriegsheim, Juan Liu, Jason W. Locasale, Adam Robinson, Jing Zhang, Jessica M. Holler, Baek Kim, Marie Zikánová, Jörgen Bierau, Ling Xie, Xian Chen, Mingjie Li, Charles M. Perou, Qing Zhang
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/4f3b6b5738bf4496a2ce34dde8289124
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spelling oai:doaj.org-article:4f3b6b5738bf4496a2ce34dde82891242021-12-02T17:01:52ZProlyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer10.1038/s41467-019-13168-42041-1723https://doaj.org/article/4f3b6b5738bf4496a2ce34dde82891242019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13168-4https://doaj.org/toc/2041-1723The hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling.Giada ZurloXijuan LiuMamoru TakadaCheng FanJeremy M. SimonTravis S. PtacekJavier RodriguezAlex von KriegsheimJuan LiuJason W. LocasaleAdam RobinsonJing ZhangJessica M. HollerBaek KimMarie ZikánováJörgen BierauLing XieXian ChenMingjie LiCharles M. PerouQing ZhangNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Giada Zurlo
Xijuan Liu
Mamoru Takada
Cheng Fan
Jeremy M. Simon
Travis S. Ptacek
Javier Rodriguez
Alex von Kriegsheim
Juan Liu
Jason W. Locasale
Adam Robinson
Jing Zhang
Jessica M. Holler
Baek Kim
Marie Zikánová
Jörgen Bierau
Ling Xie
Xian Chen
Mingjie Li
Charles M. Perou
Qing Zhang
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
description The hydroxylase EgIN2 contributes to triple negative breast cancers. Here, using an enzyme-substrate trapping strategy, the authors identify ASDL as a bona fide substrate of EgIN2 promoting aggressive properties of TNBC via the activation of cMYC signaling.
format article
author Giada Zurlo
Xijuan Liu
Mamoru Takada
Cheng Fan
Jeremy M. Simon
Travis S. Ptacek
Javier Rodriguez
Alex von Kriegsheim
Juan Liu
Jason W. Locasale
Adam Robinson
Jing Zhang
Jessica M. Holler
Baek Kim
Marie Zikánová
Jörgen Bierau
Ling Xie
Xian Chen
Mingjie Li
Charles M. Perou
Qing Zhang
author_facet Giada Zurlo
Xijuan Liu
Mamoru Takada
Cheng Fan
Jeremy M. Simon
Travis S. Ptacek
Javier Rodriguez
Alex von Kriegsheim
Juan Liu
Jason W. Locasale
Adam Robinson
Jing Zhang
Jessica M. Holler
Baek Kim
Marie Zikánová
Jörgen Bierau
Ling Xie
Xian Chen
Mingjie Li
Charles M. Perou
Qing Zhang
author_sort Giada Zurlo
title Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
title_short Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
title_full Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
title_fullStr Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
title_full_unstemmed Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
title_sort prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/4f3b6b5738bf4496a2ce34dde8289124
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