Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins

Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing cond...

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Autores principales:	Caroline E. Weller, Abhinav Dhall, Feizhi Ding, Edlaine Linares, Samuel D. Whedon, Nicholas A. Senger, Elizabeth L. Tyson, John D. Bagert, Xiaosong Li, Ohara Augusto, Champak Chatterjee
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b48cef68f3dc4e9fa4b70b0add885ae3
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spelling	oai:doaj.org-article:b48cef68f3dc4e9fa4b70b0add885ae32021-12-02T14:39:15ZAromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins10.1038/ncomms129792041-1723https://doaj.org/article/b48cef68f3dc4e9fa4b70b0add885ae32016-09-01T00:00:00Zhttps://doi.org/10.1038/ncomms12979https://doaj.org/toc/2041-1723Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing conditions.Caroline E. WellerAbhinav DhallFeizhi DingEdlaine LinaresSamuel D. WhedonNicholas A. SengerElizabeth L. TysonJohn D. BagertXiaosong LiOhara AugustoChampak ChatterjeeNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Caroline E. Weller Abhinav Dhall Feizhi Ding Edlaine Linares Samuel D. Whedon Nicholas A. Senger Elizabeth L. Tyson John D. Bagert Xiaosong Li Ohara Augusto Champak Chatterjee Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
description	Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing conditions.
format	article
author	Caroline E. Weller Abhinav Dhall Feizhi Ding Edlaine Linares Samuel D. Whedon Nicholas A. Senger Elizabeth L. Tyson John D. Bagert Xiaosong Li Ohara Augusto Champak Chatterjee
author_facet	Caroline E. Weller Abhinav Dhall Feizhi Ding Edlaine Linares Samuel D. Whedon Nicholas A. Senger Elizabeth L. Tyson John D. Bagert Xiaosong Li Ohara Augusto Champak Chatterjee
author_sort	Caroline E. Weller
title	Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
title_short	Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
title_full	Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
title_fullStr	Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
title_full_unstemmed	Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
title_sort	aromatic thiol-mediated cleavage of n–o bonds enables chemical ubiquitylation of folded proteins
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/b48cef68f3dc4e9fa4b70b0add885ae3
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Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins

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