Evidence map›Paper›PMID 33479245›Full record

SynthesisScientific data2021

The human O-GlcNAcome database and meta-analysis.

Eugenia Wulff-Fuentes, Rex R Berendt, Logan Massman, Laura Danner, Florian Malard, Jeet Vora, Robel Kahsay, Stephanie Olivier-Van Stichelen

Abstract readMeta-Analysis
In one paragraph

Synthesis in Scientific data, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
155citing 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

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

  1. Pooled it
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  6. Review
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  8. Article
  9. PerturbingCells · 2026
    Article
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  15. Review
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  20. Review

95 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

8 authors.

Eugenia Wulff-Fuentes *Department of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.ORCID http://orcid.org/0000-0002-9995-7130
Rex R Berendt *Department of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.
Logan MassmanDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.ORCID http://orcid.org/0000-0002-5579-4798
Laura DannerDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.
Florian MalardDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, USA.
Jeet VoraDepartment of Biochemistry & Molecular Medicine, The George Washington School of Medicine and Health Sciences, Washington, DC, 20052, USA.
Robel KahsayDepartment of Biochemistry & Molecular Medicine, The George Washington School of Medicine and Health Sciences, Washington, DC, 20052, USA.
Stephanie Olivier-Van StichelenDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, USA. solivier@mcw.edu.

Funding

GlyGen Supplement: Develop automatic literature mining tool for extracting context specific glycan-protein data that will enhance the extent and quality of data in GlyGenU01GM125267 · NIGMS · UNIVERSITY OF GEORGIA · PI MAZUMDER, RAJA, TIEMEYER, MICHAEL · 2017 to 2021
$10.2M
Placental Hormones and O-GlcNAcylation in Gestational DiabetesR01HD104808 · NICHD · MEDICAL COLLEGE OF WISCONSIN · PI Stephanie Olivier-Van Stichelen · 2022 to 2026
$1.8M
Nutrient sensing O-GlcNAcylation in pituitary developmentR00HD087430 · NICHD · MEDICAL COLLEGE OF WISCONSIN · PI OLIVIER-VAN STICHELEN, STEPHANIE · 2019 to 2021
$737k
NICHD NIH HHS R00 HD087430NICHD NIH HHS R01 HD104808U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) 1U01GM125267
6 · The paper itself

Abstract

Over the past 35 years, ~1700 articles have characterized protein O-GlcNAcylation. Found in almost all living organisms, this post-translational modification of serine and threonine residues is highly conserved and key to biological processes. With half of the primary research articles using human models, the O-GlcNAcome recently reached a milestone of 5000 human proteins identified. Herein, we provide an extensive inventory of human O-GlcNAcylated proteins, their O-GlcNAc sites, identification methods, and corresponding references ( www.oglcnac.mcw.edu ). In the absence of a comprehensive online resource for O-GlcNAcylated proteins, this list serves as the only database of O-GlcNAcylated proteins. Based on the thorough analysis of the amino acid sequence surrounding 7002 O-GlcNAc sites, we progress toward a more robust semi-consensus sequence for O-GlcNAcylation. Moreover, we offer a comprehensive meta-analysis of human O-GlcNAcylated proteins for protein domains, cellular and tissue distribution, and pathways in health and diseases, reinforcing that O-GlcNAcylation is a master regulator of cell signaling, equal to the widely studied phosphorylation.

Indexed as

Databases, ProteinGlycoproteinsGlycosylationHumansProtein Processing, Post-TranslationalGlycoproteins

Identifiers

PMID33479245
PMCPMC7820439

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.