An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules

Ubiquitination and ubiquitin-like modifications of proteins regulate multiple cellular processes but identifying substrates of specific E2 and E3 enzymes remains challenging. Here, the authors conjugate E2 enzymes with enrichable ubiquitin derivatives to identify substrates of specific E2/E3 pairs b...

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Autores principales:	Gábor Bakos, Lu Yu, Igor A. Gak, Theodoros I. Roumeliotis, Dimitris Liakopoulos, Jyoti S. Choudhary, Jörg Mansfeld
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2f933e1692cc471fbb02a4f43cc71f65
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spelling	oai:doaj.org-article:2f933e1692cc471fbb02a4f43cc71f652021-12-02T14:39:07ZAn E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules10.1038/s41467-018-07251-52041-1723https://doaj.org/article/2f933e1692cc471fbb02a4f43cc71f652018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07251-5https://doaj.org/toc/2041-1723Ubiquitination and ubiquitin-like modifications of proteins regulate multiple cellular processes but identifying substrates of specific E2 and E3 enzymes remains challenging. Here, the authors conjugate E2 enzymes with enrichable ubiquitin derivatives to identify substrates of specific E2/E3 pairs by mass spectrometry.Gábor BakosLu YuIgor A. GakTheodoros I. RoumeliotisDimitris LiakopoulosJyoti S. ChoudharyJörg MansfeldNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Gábor Bakos Lu Yu Igor A. Gak Theodoros I. Roumeliotis Dimitris Liakopoulos Jyoti S. Choudhary Jörg Mansfeld An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
description	Ubiquitination and ubiquitin-like modifications of proteins regulate multiple cellular processes but identifying substrates of specific E2 and E3 enzymes remains challenging. Here, the authors conjugate E2 enzymes with enrichable ubiquitin derivatives to identify substrates of specific E2/E3 pairs by mass spectrometry.
format	article
author	Gábor Bakos Lu Yu Igor A. Gak Theodoros I. Roumeliotis Dimitris Liakopoulos Jyoti S. Choudhary Jörg Mansfeld
author_facet	Gábor Bakos Lu Yu Igor A. Gak Theodoros I. Roumeliotis Dimitris Liakopoulos Jyoti S. Choudhary Jörg Mansfeld
author_sort	Gábor Bakos
title	An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
title_short	An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
title_full	An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
title_fullStr	An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
title_full_unstemmed	An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
title_sort	e2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/2f933e1692cc471fbb02a4f43cc71f65
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An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules

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