Evidence map›Paper›PMID 27695962›Full record

ArticleAnalytical and bioanalytical chemistry2017

Isotope-targeted glycoproteomics (IsoTaG) analysis of sialylated N- and O-glycopeptides on an Orbitrap Fusion Tribrid using azido and alkynyl sugars.

Christina M Woo, Alejandra Felix, Lichao Zhang, Joshua E Elias, Carolyn R Bertozzi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Analytical and bioanalytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

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0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Article
  2. Minimalist TetrazineJournal of the American Chemical Society · 2024
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Christina M WooDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Alejandra FelixDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA.
Lichao ZhangChemical and Systems Biology, Stanford University, Stanford, CA, 94305, USA.
Joshua E EliasChemical and Systems Biology, Stanford University, Stanford, CA, 94305, USA.
Carolyn R BertozziDepartment of Chemistry, Stanford University, Stanford, CA, 94305, USA. bertozzi@stanford.edu.

Funding

Investigating the Surface GlycoproteomeR01CA200423 · NCI · STANFORD UNIVERSITY · PI Carolyn Bertozzi · 2015 to 2026
$3.8M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA200423
6 · The paper itself

Abstract

Protein glycosylation is a post-translational modification (PTM) responsible for many aspects of proteomic diversity and biological regulation. Assignment of intact glycan structures to specific protein attachment sites is a critical step towards elucidating the function encoded in the glycome. Previously, we developed isotope-targeted glycoproteomics (IsoTaG) as a mass-independent mass spectrometry method to characterize azide-labeled intact glycopeptides from complex proteomes. Here, we extend the IsoTaG approach with the use of alkynyl sugars as metabolic labels and employ new probes in analysis of the sialylated glycoproteome from PC-3 cells. Using an Orbitrap Fusion Tribrid mass spectrometer, we identified 699 intact glycopeptides from 192 glycoproteins. These intact glycopeptides represent a total of eight sialylated glycan structures across 126 N- and 576 O-glycopeptides. IsoTaG is therefore an effective platform for identification of intact glycopeptides labeled by alkynyl or azido sugars and will facilitate further studies of the glycoproteome.

Indexed as

ProteomicsAzidesGlycopeptidesIsotopesOligopeptidesarginyl-glycyl-aspartic acidAzidesGlycopeptidesIsotopesOligopeptidesChemical proteomicsGlycoproteomicsLC-MS/MSMetabolic labelingSialic acid

Identifiers

PMID27695962
PMCPMC5342897

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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.