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Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-b...

Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-b...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a46b2f4d4dac4cac9faa09918943bfac

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2019-05, Vol.10 (1), p.2195-2195, Article 2195

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Cysteine modifications emerge as important players in cellular signaling and homeostasis. Here, we present a chemical proteomics strategy for quantitative analysis of reversibly modified Cysteines using bioorthogonal cleavable-linker and switch technique (Cys-BOOST). Compared to iodoTMT for total Cysteine analysis, Cys-BOOST shows a threefold highe...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_a46b2f4d4dac4cac9faa09918943bfac

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_a46b2f4d4dac4cac9faa09918943bfac

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-019-10182-4

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