Evidence map›Paper›PMID 30459171›Full record

ArticleMolecular systems biology2018

Mapping the O-glycoproteome using site-specific extraction of O-linked glycopeptides (EXoO).

Weiming Yang, Minghui Ao, Yingwei Hu, Qing Kay Li, Hui Zhang

Abstract read
In one paragraph

Article in Molecular systems biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing 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

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

  1. Pooled it
  2. CD97/Cells · 2026
    Review
  3. Review
  4. Review
  5. Deep Learning Prediction of O-Glycopeptide Tandem Mass Spectra Enhances O-Glycoproteomics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Foods (Basel, Switzerland) · 2025
    Article
  14. Sialylated CD43 is a glyco-immune checkpoint for macrophage phagocytosis.bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

27 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.

Weiming YangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-5023-2155
Minghui AoDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Yingwei HuDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Qing Kay LiDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Hui ZhangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD, USA huizhang@jhu.edu.

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
The Comprehensive Proteome Characterization Center at Johns Hopkins: High Precision Discovery and Confirmation of Genoproteomic TargetsU24CA210985 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2016 to 2020
$5.3M
Targeting Latently Infected Primary Cells using Integrated GlycoproteomicsR21AI122382 · NIAID · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2016 to 2017
$446k
NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA210985NHLBI NIH HHS P01 HL107153NIAID NIH HHS R21 AI122382
6 · The paper itself

Abstract

Protein glycosylation is one of the most abundant post-translational modifications. However, detailed analysis of O-linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of suitable methodologies. Here, a chemoenzymatic method is introduced for the site-specific extraction of O-linked glycopeptides (EXoO), which enabled the mapping of over 3,000 O-linked glycosylation sites and definition of their glycans on over 1,000 proteins in human kidney tissues, T cells, and serum. This large-scale localization of O-linked glycosylation sites demonstrated that EXoO is an effective method for defining the site-specific O-linked glycoproteome in different types of sample. Detailed structural analysis of the sites identified revealed conserved motifs and topological orientations facing extracellular space, the cell surface, the lumen of the Golgi, and the endoplasmic reticulum (ER). EXoO was also able to reveal significant differences in the O-linked glycoproteome of tumor and normal kidney tissues pointing to its broader use in clinical diagnostics and therapeutics.

Indexed as

Cells, CulturedChromatography, LiquidGlycoproteinsGlycosylationHumansKidneyProtein Processing, Post-TranslationalProteomicsSerumSolid Phase ExtractionTandem Mass SpectrometryT-LymphocytesGlycoproteinsglycoproteomicsglycosylationO‐GalNAcO‐linkedsite‐specific

Identifiers

PMID30459171
PMCPMC6243375

What OpenQuestion holds

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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.