Evidence map›Paper›PMID 23816992›Full record

ArticleMolecular & cellular proteomics : MCP2013

N- and O-glycosylation in the murine synaptosome.

Jonathan C Trinidad, Ralf Schoepfer, Alma L Burlingame, Katalin F Medzihradszky

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
9.3field-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

88 citing papers in PubMed, 173 citations in OpenAlex.

  1. Review
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  15. Uncovering the Role ofJournal of the American Chemical Society · 2023
    Article
  16. Article
  17. Review
  18. Review
  19. The dynamic brain N-glycome.Glycoconjugate journal · 2022
    Review
  20. Article

28 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 at 2 institutions in 2 countries.

Jonathan C TrinidadDepartment of Pharmaceutical Chemistry, Mass Spectrometry Facility, School of Pharmacy, University of California San Francisco, San Francisco, California 94158-2517;
Ralf Schoepfer
Alma L Burlingame
Katalin F Medzihradszky
University of California, San Francisco · USUniversity College London · GB

Funding

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
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103481NIGMS NIH HHS P50 GM081879PHS HHS NIH NIGMS 8P41GM103481
6 · The paper itself

Abstract

We present the first large scale study characterizing both N- and O-linked glycosylation in a site-specific manner on hundreds of proteins. We demonstrate that a lectin-affinity fractionation step using wheat germ agglutinin enriches not only peptides carrying intracellular O-GlcNAc, but also those bearing ER/Golgi-derived N- and O-linked carbohydrate structures. Liquid chromatography-MS (LC/MS) analysis with high accuracy precursor mass measurements and high sensitivity ion trap electron-transfer dissociation (ETD) were utilized for structural characterization of glycopeptides. Our results reveal both the identity of the precise sites of glycosylation and information on the oligosaccharide structures possible on these proteins. We report a novel iterative approach that allowed us to interpret the ETD data set directly without making prior assumptions about the nature and distribution of oligosaccharides present in our glycopeptide mixture. Over 2500 unique N- and O-linked glycopeptides were identified on 453 proteins. The extent of microheterogeneity varied extensively, and up to 19 different oligosaccharides were attached at a given site. We describe the presence of the well-known mucin-type structures for O-glycosylation, an EGF-domain-specific fucosylation and a rare O-mannosylation on the transmembrane phosphatase Ptprz1. Finally, we identified three examples of O-glycosylation on tyrosine residues.

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAnimalsCarbohydrate SequenceChemical FractionationChromatography, LiquidFucoseGlycopeptidesGlycosylationMannoseMiceMolecular Sequence AnnotationMolecular Sequence DataMucinsProteomicsSynaptosomesFucoseGlycopeptidesMannoseMucinsWheat Germ Agglutinins

Identifiers

PMID23816992
PMCPMC3861701
OpenAlexW2109830799

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.