A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation

Cullins are central components of the ubiquitin-proteosome system and are activated via a neddylation process mediated by the DCN1–UBC12 complex. Here, the authors develop a small molecule inhibitor of the DCN1–UBC12 interaction that specifically blocks cullin 3 neddylation and can be used to probe...

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Autores principales: Haibin Zhou, Jianfeng Lu, Liu Liu, Denzil Bernard, Chao-Yie Yang, Ester Fernandez-Salas, Krishnapriya Chinnaswamy, Stephanie Layton, Jeanne Stuckey, Qing Yu, Weihua Zhou, Zhenqiang Pan, Yi Sun, Shaomeng Wang
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/a1e0427493d44f3fa81a56f36c37a6f4
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spelling oai:doaj.org-article:a1e0427493d44f3fa81a56f36c37a6f42021-12-02T15:38:54ZA potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation10.1038/s41467-017-01243-72041-1723https://doaj.org/article/a1e0427493d44f3fa81a56f36c37a6f42017-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01243-7https://doaj.org/toc/2041-1723Cullins are central components of the ubiquitin-proteosome system and are activated via a neddylation process mediated by the DCN1–UBC12 complex. Here, the authors develop a small molecule inhibitor of the DCN1–UBC12 interaction that specifically blocks cullin 3 neddylation and can be used to probe the cellular function of cullin 3.Haibin ZhouJianfeng LuLiu LiuDenzil BernardChao-Yie YangEster Fernandez-SalasKrishnapriya ChinnaswamyStephanie LaytonJeanne StuckeyQing YuWeihua ZhouZhenqiang PanYi SunShaomeng WangNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Haibin Zhou
Jianfeng Lu
Liu Liu
Denzil Bernard
Chao-Yie Yang
Ester Fernandez-Salas
Krishnapriya Chinnaswamy
Stephanie Layton
Jeanne Stuckey
Qing Yu
Weihua Zhou
Zhenqiang Pan
Yi Sun
Shaomeng Wang
A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
description Cullins are central components of the ubiquitin-proteosome system and are activated via a neddylation process mediated by the DCN1–UBC12 complex. Here, the authors develop a small molecule inhibitor of the DCN1–UBC12 interaction that specifically blocks cullin 3 neddylation and can be used to probe the cellular function of cullin 3.
format article
author Haibin Zhou
Jianfeng Lu
Liu Liu
Denzil Bernard
Chao-Yie Yang
Ester Fernandez-Salas
Krishnapriya Chinnaswamy
Stephanie Layton
Jeanne Stuckey
Qing Yu
Weihua Zhou
Zhenqiang Pan
Yi Sun
Shaomeng Wang
author_facet Haibin Zhou
Jianfeng Lu
Liu Liu
Denzil Bernard
Chao-Yie Yang
Ester Fernandez-Salas
Krishnapriya Chinnaswamy
Stephanie Layton
Jeanne Stuckey
Qing Yu
Weihua Zhou
Zhenqiang Pan
Yi Sun
Shaomeng Wang
author_sort Haibin Zhou
title A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
title_short A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
title_full A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
title_fullStr A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
title_full_unstemmed A potent small-molecule inhibitor of the DCN1-UBC12 interaction that selectively blocks cullin 3 neddylation
title_sort potent small-molecule inhibitor of the dcn1-ubc12 interaction that selectively blocks cullin 3 neddylation
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/a1e0427493d44f3fa81a56f36c37a6f4
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