Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition

Arginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus i...

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Autores principales: Evgenia Shishkova, Hao Zeng, Fabao Liu, Nicholas W. Kwiecien, Alexander S. Hebert, Joshua J. Coon, Wei Xu
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/222565a41f79486c861ca88378e98eac
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spelling oai:doaj.org-article:222565a41f79486c861ca88378e98eac2021-12-02T14:42:21ZGlobal mapping of CARM1 substrates defines enzyme specificity and substrate recognition10.1038/ncomms155712041-1723https://doaj.org/article/222565a41f79486c861ca88378e98eac2017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15571https://doaj.org/toc/2041-1723Arginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus in substrate recognition.Evgenia ShishkovaHao ZengFabao LiuNicholas W. KwiecienAlexander S. HebertJoshua J. CoonWei XuNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Evgenia Shishkova
Hao Zeng
Fabao Liu
Nicholas W. Kwiecien
Alexander S. Hebert
Joshua J. Coon
Wei Xu
Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
description Arginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus in substrate recognition.
format article
author Evgenia Shishkova
Hao Zeng
Fabao Liu
Nicholas W. Kwiecien
Alexander S. Hebert
Joshua J. Coon
Wei Xu
author_facet Evgenia Shishkova
Hao Zeng
Fabao Liu
Nicholas W. Kwiecien
Alexander S. Hebert
Joshua J. Coon
Wei Xu
author_sort Evgenia Shishkova
title Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
title_short Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
title_full Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
title_fullStr Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
title_full_unstemmed Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
title_sort global mapping of carm1 substrates defines enzyme specificity and substrate recognition
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/222565a41f79486c861ca88378e98eac
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