Evidence map›Paper›PMID 28518125›Full record

ArticleJournal of visualized experiments : JoVE2017

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry.

Javier Barallobre-Barreiro, Ferheen Baig, Marika Fava, Xiaoke Yin, Manuel Mayr

Open access · greenAbstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Mass spectrometry reveals age-dependent collagen decline in murine atria.Annals of the New York Academy of Sciences · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Decellularized Splenic Matrix as a Scaffold for Spleen Bioengineering.Frontiers in bioengineering and biotechnology · 2020
    Article
  12. Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules.Molecular & cellular proteomics : MCP · 2019
    Review
  13. Article
  14. Article
  15. Glycoproteomic Analysis of the Aortic Extracellular Matrix in Marfan Patients.Arteriosclerosis, thrombosis, and vascular biology · 2019
    Article
  16. Article
  17. Review
  18. Review
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 at 3 institutions in 2 countries.

Javier Barallobre-BarreiroKing's British Heart Foundation Centre, King's College London.
Ferheen BaigKing's British Heart Foundation Centre, King's College London.
Marika FavaKing's British Heart Foundation Centre, King's College London.
Xiaoke YinKing's British Heart Foundation Centre, King's College London.
Manuel MayrKing's British Heart Foundation Centre, King's College London; manuel.mayr@kcl.ac.uk.
British Heart Foundation · GBKing's College London · GBHeart Foundation · US

Funding

British Heart Foundation CH/16/3/32406British Heart Foundation FS/13/2/29892British Heart Foundation PG/17/48/32956British Heart Foundation RG/16/14/32397
6 · The paper itself

Abstract

Fibrosis is a hallmark of many cardiovascular diseases and is associated with the exacerbated secretion and deposition of the extracellular matrix (ECM). Using proteomics, we have previously identified more than 150 ECM and ECM-associated proteins in cardiovascular tissues. Notably, many ECM proteins are glycosylated. This post-translational modification affects protein folding, solubility, binding, and degradation. We have developed a sequential extraction and enrichment method for ECM proteins that is compatible with the subsequent liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis of intact glycopeptides. The strategy is based on sequential incubations with NaCl, SDS for tissue decellularization, and guanidine hydrochloride for the solubilization of ECM proteins. Recent advances in LC-MS/MS include fragmentation methods, such as combinations of higher-energy collision dissociation (HCD) and electron transfer dissociation (ETD), which allow for the direct compositional analysis of glycopeptides of ECM proteins. In the present paper, we describe a method to prepare the ECM from tissue samples. The method not only allows for protein profiling but also the assessment and characterization of glycosylation by MS analysis.

Indexed as

Cardiovascular DiseasesChromatography, LiquidExtracellular MatrixExtracellular Matrix ProteinsFibrosisGlycopeptidesGlycosylationProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryExtracellular Matrix ProteinsGlycopeptides

Identifiers

PMID28518125
PMCPMC5565024
OpenAlexW2606531290

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.