Evidence map›Paper›PMID 32872358›Full record

ReviewCells2020

Protein Glycosylation Investigated by Mass Spectrometry: An Overview.

Anna Illiano, Gabriella Pinto, Chiara Melchiorre, Andrea Carpentieri, Vincenza Faraco, Angela Amoresano

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Glycomics Meets Oncology: The Role of Mass Spectrometry in Cancer Research.Advances in experimental medicine and biology · 2026
    Review
  3. Article
  4. Article
  5. Quantitative Modeling of IgG N-Glycosylation Profiles from Population Data.International journal of molecular sciences · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Autism-Linked Mutations in αPharmaceuticals (Basel, Switzerland) · 2024
    Article
  16. Review
  17. Proteomic Investigation of Immune Checkpoints and Some of Their Inhibitors.International journal of molecular sciences · 2024
    Review
  18. Review
  19. Review
  20. 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

6 authors at 3 institutions in 1 country.

Anna IllianoDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
Gabriella PintoDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
Chiara MelchiorreDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
Andrea CarpentieriDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
Vincenza FaracoDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
Angela AmoresanoDepartment of Chemical Sciences, University of Naples Federico II, Via Cinthia 26, 80126 Naples, Italy.
University of Naples Federico II · ITCeinge Biotecnologie Avanzate (Italy) · ITIstituto Nazionale Biostrutture e Biosistemi · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein glycosylation is a post-translational modification of crucial importance for its involvement in molecular recognition, protein trafficking, regulation, and inflammation. Indeed, abnormalities in protein glycosylation are correlated with several disease states such as cancer, inflammatory diseases, and congenial disorders. The understanding of cellular mechanisms through the elucidation of glycan composition encourages researchers to find analytical solutions for their detection. Actually, the multiplicity and diversity of glycan structures bond to the proteins, the variations in polarity of the individual saccharide residues, and the poor ionization efficiencies make their detection much trickier than other kinds of biopolymers. An overview of the most prominent techniques based on mass spectrometry (MS) for protein glycosylation (glycoproteomics) studies is here presented. The tricks and pre-treatments of samples are discussed as a crucial step prodromal to the MS analysis to improve the glycan ionization efficiency. Therefore, the different instrumental MS mode is also explored for the qualitative and quantitative analysis of glycopeptides and the glycans structural composition, thus contributing to the elucidation of biological mechanisms.

Indexed as

GlycosylationHumansMass SpectrometryProtein Processing, Post-TranslationalProteomicsglycosylationglycosylation and diseases correlationpost-translational modifications (PTM), mass spectrometryquantitative analysis

Identifiers

PMID32872358
PMCPMC7564411
OpenAlexW3082670149

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.