Evidence map›Paper›PMID 22645316›Full record

ArticleMolecular & cellular proteomics : MCP2012

Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse.

Jonathan C Trinidad, David T Barkan, Brittany F Gulledge, Agnes Thalhammer, Andrej Sali, Ralf Schoepfer, Alma L Burlingame

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers.

0numbers the graph read from it
0cells of the map it votes in
253citing papers in PubMed
12.9field-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

253 citing papers in PubMed, 419 citations in OpenAlex.

  1. Article
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  10. A Scalable Design for Proximity-Inducing Molecules.bioRxiv : the preprint server for biology · 2026
    Article
  11. Review
  12. Article
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  20. International journal of molecular sciences · 2025
    Review

193 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

7 authors at 2 institutions in 2 countries.

Jonathan C TrinidadDepartment of Pharmaceutical Chemistry, UCSF, San Francisco, California 94158, USA.
David T Barkan
Brittany F Gulledge
Agnes Thalhammer
Andrej Sali
Ralf Schoepfer
Alma L Burlingame
University of California, San Francisco · USUniversity College London · GB

Funding

The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ALMO, STEVEN C. · 2010 to 2014
$32.6M
Rewiring Therapeutic Cells: User-Controlled T Cells and Stem CellsP50GM081879 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI LIM, WENDELL A · 2010 to 2017
$19.0M
Unbiased Functional Characterization of Enterovirus-Host InteractionsP01AI091575 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANDINO, RAUL · 2011 to 2015
$10.5M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
Howard Hughes Medical InstituteNIAID NIH HHS P01 AI091575NIGMS NIH HHS 8P41GM103481NIGMS NIH HHS P41 GM103481NIGMS NIH HHS P50 GM081879NIGMS NIH HHS R01 GM083960NIGMS NIH HHS U54 GM094662
6 · The paper itself

Abstract

O-linked N-acetylglucosamine (O-GlcNAc) is a dynamic, reversible monosaccharide modifier of serine and threonine residues on intracellular protein domains. Crosstalk between O-GlcNAcylation and phosphorylation has been hypothesized. Here, we identified over 1750 and 16,500 sites of O-GlcNAcylation and phosphorylation from murine synaptosomes, respectively. In total, 135 (7%) of all O-GlcNAcylation sites were also found to be sites of phosphorylation. Although many proteins were extensively phosphorylated and minimally O-GlcNAcylated, proteins found to be extensively O-GlcNAcylated were almost always phosphorylated to a similar or greater extent, indicating the O-GlcNAcylation system is specifically targeting a subset of the proteome that is also phosphorylated. Both PTMs usually occur on disordered regions of protein structure, within which, the location of O-GlcNAcylation and phosphorylation is virtually random with respect to each other, suggesting that negative crosstalk at the structural level is not a common phenomenon. As a class, protein kinases are found to be more extensively O-GlcNAcylated than proteins in general, indicating the potential for crosstalk of phosphorylation with O-GlcNAcylation via regulation of enzymatic activity.

Indexed as

AcetylglucosamineAmino Acid SequenceAnimalsBinding SitesBrainChromatography, Reverse-PhaseGlycosylationMass SpectrometryMiceMice, Inbred C57BLN-AcetylglucosaminyltransferasesPeptidesPhosphorylationProtein Processing, Post-TranslationalProteinsProteomicsAcetylglucosamineN-AcetylglucosaminyltransferasesPeptidesProteins

Identifiers

PMID22645316
PMCPMC3412957
OpenAlexW2168386087

What OpenQuestion holds

Textmetadata
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.