Evidence map›Paper›PMID 30899004›Full record

ArticleNature communications2019

Capturing site-specific heterogeneity with large-scale N-glycoproteome analysis.

Nicholas M Riley, Alexander S Hebert, Michael S Westphall, Joshua J Coon

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

140 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  10. UnderstandingJournal of the American Society for Mass Spectrometry · 2026
    Article
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  14. Journal of proteome research · 2025
    Article
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80 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

4 authors.

Nicholas M RileyGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-1536-2966
Alexander S HebertGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Michael S WestphallGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Joshua J CoonGenome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, 53706, USA. jcoon@chem.wisc.edu.

Funding

TR&D 2 Metabolic Labels for Ultraplexed Protein Quantification p. 453P41GM108538 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$13.1M
Structure, Function and Regulation of the ProteomeR35GM118110 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$9.1M
Uniting Mass Spectrometry and Glycoscience to Investigate Cancer BiologyK00CA212454 · NCI · STANFORD UNIVERSITY · PI RILEY, NICHOLAS M · 2018 to 2021
$331k
Uniting Mass Spectrometry and Glycoscience to Investigate Cancer BiologyF99CA212454 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI RILEY, NICHOLAS M · 2016 to 2017
$65k
NCI NIH HHS F99 CA212454NCI NIH HHS K00 CA212454NIGMS NIH HHS P41 GM108538NIGMS NIH HHS R35 GM118110NIH HHS F99 CA212454NIH HHS P41 GM108538NIH HHS R35 GM118110
6 · The paper itself

Abstract

Protein glycosylation is a highly important, yet poorly understood protein post-translational modification. Thousands of possible glycan structures and compositions create potential for tremendous site heterogeneity. A lack of suitable analytical methods for large-scale analyses of intact glycopeptides has limited our abilities both to address the degree of heterogeneity across the glycoproteome and to understand how this contributes biologically to complex systems. Here we show that N-glycoproteome site-specific microheterogeneity can be captured via large-scale glycopeptide profiling methods enabled by activated ion electron transfer dissociation (AI-ETD), ultimately characterizing 1,545 N-glycosites (>5,600 unique N-glycopeptides) from mouse brain tissue. Our data reveal that N-glycosylation profiles can differ between subcellular regions and structural domains and that N-glycosite heterogeneity manifests in several different forms, including dramatic differences in glycosites on the same protein. Moreover, we use this large-scale glycoproteomic dataset to develop several visualizations that will prove useful for analyzing intact glycopeptides in future studies.

Indexed as

Protein Processing, Post-TranslationalAnimalsBrainBrain ChemistryDatasets as TopicFemaleGene ExpressionGlycopeptidesGlycosylationMiceMice, Inbred C57BLNerve Tissue ProteinsPolysaccharidesProteomeTandem Mass SpectrometryGlycopeptidesNerve Tissue ProteinsPolysaccharidesProteome

Identifiers

PMID30899004
PMCPMC6428843

What OpenQuestion holds

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LicenceCC BY
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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.