ArticleCurrent protocols in chemical biology2016
Isotope Targeted Glycoproteomics (IsoTaG) to Characterize Intact, Metabolically Labeled Glycopeptides from Complex Proteomes.
Article in Current protocols in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Biochemical Applications of Microbial Rare Glycan Biosynthesis, Recognition, and Sequencing.Biochemistry · 2025Review
- Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice.Plant biotechnology journal · 2023Article
- Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.ACS chemical biology · 2022Article
- Synthesis and Application of Rare Deoxy Amino l-Sugar Analogues to Probe Glycans in Pathogenic Bacteria.ACS infectious diseases · 2022Article
- Dismantling the bacterial glycocalyx: Chemical tools to probe, perturb, and image bacterial glycans.Bioorganic & medicinal chemistry · 2021Review
- Target protein deglycosylation in living cells by a nanobody-fused split O-GlcNAcase.Nature chemical biology · 2021Article
- Isotope-targeted glycoproteomics (IsoTaG) analysis of sialylated N- and O-glycopeptides on an Orbitrap Fusion Tribrid using azido and alkynyl sugars.Analytical and bioanalytical chemistry · 2017Article
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- Proteomic dataset for altered glycoprotein expression upon GALNT3 knockdown in ovarian cancer cells.Data in brief · 2016Article
- A metabolic labeling approach for glycoproteomic analysis reveals altered glycoprotein expression upon GALNT3 knockdown in ovarian cancer cells.Journal of proteomics · 2016Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Protein glycosylation plays many critical roles in biological function and creates the most diversity of all post-translational modifications (PTMs). Glycan structural diversity is directly correlated with difficulty in characterizing the intact glycoproteome by mass spectrometry (MS). In this protocol, we describe a novel mass-independent chemical glycoproteomics platform for characterizing intact, metabolically labeled glycopeptides from complex proteomes, termed Isotope Targeted Glycoproteomics (IsoTaG). To use IsoTaG, cell culture samples are metabolically labeled with an azido- or alkynyl-sugar. Metabolically labeled glycoproteins are then tagged using Click chemistry and enriched with an isotopic recoding biotin probe. Intact glycopeptides are recovered by cleavage of the probe, analyzed with directed MS, and assigned by targeted mass-independent data analysis. The outlined procedure is well defined in cell culture and has been executed with over 15 cell lines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.