Evidence map›Paper›PMID 25894945›Full record

ArticleNature methods2015

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

Christina M Woo, Anthony T Iavarone, David R Spiciarich, Krishnan K Palaniappan, Carolyn R Bertozzi

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed, 1 pooled it
13.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

125 citing papers in PubMed, 1 synthesis or guideline pooled it, 263 citations in OpenAlex.

  1. Pooled it
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  15. ACS central science · 2024
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  16. Integrating the analysis of human biopsies using post-translational modifications proteomics.Protein science : a publication of the Protein Society · 2024
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65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Christina M WooDepartment of Chemistry, University of California, Berkeley, California, USA.
Anthony T IavaroneQB3/Chemistry Mass Spectrometry Facility, University of California, Berkeley, California, USA.
David R SpiciarichDepartment of Chemistry, University of California, Berkeley, California, USA.
Krishnan K PalaniappanDepartment of Chemistry, University of California, Berkeley, California, USA.
Carolyn R Bertozzi1] Department of Chemistry, University of California, Berkeley, California, USA. [2] Department of Molecular and Cell Biology, University of California, Berkeley, California, USA. [3] Howard Hughes Medical Institute, Berkeley, California, USA.
University of California, Berkeley · US

Funding

Investigating the Surface GlycoproteomeR01CA200423 · NCI · STANFORD UNIVERSITY · PI Carolyn Bertozzi · 2015 to 2026
$3.8M
Howard Hughes Medical InstituteNCI NIH HHS CA200423NCI NIH HHS R01 CA200423
6 · The paper itself

Abstract

Protein glycosylation is a heterogeneous post-translational modification (PTM) that plays an essential role in biological regulation. However, the diversity found in glycoproteins has undermined efforts to describe the intact glycoproteome via mass spectrometry (MS). We present IsoTaG, a mass-independent chemical glycoproteomics platform for characterization of intact, metabolically labeled glycopeptides at the whole-proteome scale. In IsoTaG, metabolic labeling of the glycoproteome is combined with (i) chemical enrichment and isotopic recoding of glycopeptides to select peptides for targeted glycoproteomics using directed MS and (ii) mass-independent assignment of intact glycopeptides. We structurally assigned 32 N-glycopeptides and over 500 intact and fully elaborated O-glycopeptides from 250 proteins across three human cancer cell lines and also discovered unexpected peptide sequence polymorphisms (pSPs). The IsoTaG platform is broadly applicable to the discovery of PTM sites that are amenable to chemical labeling, as well as previously unknown protein isoforms including pSPs.

Indexed as

Isotope LabelingCell Line, TumorGlycoproteinsGlycosylationHumansMolecular StructureProteomeProteomicsTandem Mass SpectrometryGlycoproteinsProteome

Identifiers

PMID25894945
PMCPMC4599779
OpenAlexW1982936666

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.