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Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopept...

Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopept...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4599779

Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis

About this item

Full title

Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis

Publisher

New York: Nature Publishing Group US

Journal title

Nature methods, 2015-06, Vol.12 (6), p.561-567

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Metabolically labeling proteins with glycans that enable attachment of an isotopically encoded tag allows for the identification of N- and O- glycopeptides and their glycan structures.
Protein glycosylation is a heterogeneous post-translational modification (PTM) that plays an essential role in biological regulation. However, the diversity found...

Alternative Titles

Full title

Isotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4599779

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4599779

Other Identifiers

ISSN

1548-7091

E-ISSN

1548-7105

DOI

10.1038/nmeth.3366

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