Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique

Reversible cysteine modifications play important roles in cellular redox signaling. Here, the authors develop a chemical proteomics strategy that enables the quantitative analysis of endogenous cysteine nitrosylation sites and their dynamic regulation under nitrosative stress conditions.

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Autores principales:	Ruzanna Mnatsakanyan, Stavroula Markoutsa, Kim Walbrunn, Andreas Roos, Steven H. L. Verhelst, René P. Zahedi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a46b2f4d4dac4cac9faa09918943bfac
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spelling	oai:doaj.org-article:a46b2f4d4dac4cac9faa09918943bfac2021-12-02T17:01:47ZProteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique10.1038/s41467-019-10182-42041-1723https://doaj.org/article/a46b2f4d4dac4cac9faa09918943bfac2019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10182-4https://doaj.org/toc/2041-1723Reversible cysteine modifications play important roles in cellular redox signaling. Here, the authors develop a chemical proteomics strategy that enables the quantitative analysis of endogenous cysteine nitrosylation sites and their dynamic regulation under nitrosative stress conditions.Ruzanna MnatsakanyanStavroula MarkoutsaKim WalbrunnAndreas RoosSteven H. L. VerhelstRené P. ZahediNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ruzanna Mnatsakanyan Stavroula Markoutsa Kim Walbrunn Andreas Roos Steven H. L. Verhelst René P. Zahedi Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
description	Reversible cysteine modifications play important roles in cellular redox signaling. Here, the authors develop a chemical proteomics strategy that enables the quantitative analysis of endogenous cysteine nitrosylation sites and their dynamic regulation under nitrosative stress conditions.
format	article
author	Ruzanna Mnatsakanyan Stavroula Markoutsa Kim Walbrunn Andreas Roos Steven H. L. Verhelst René P. Zahedi
author_facet	Ruzanna Mnatsakanyan Stavroula Markoutsa Kim Walbrunn Andreas Roos Steven H. L. Verhelst René P. Zahedi
author_sort	Ruzanna Mnatsakanyan
title	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
title_short	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
title_full	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
title_fullStr	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
title_full_unstemmed	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
title_sort	proteome-wide detection of s-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/a46b2f4d4dac4cac9faa09918943bfac
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Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique

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