Evidence map›Paper›PMID 29162637›Full record

ReviewMolecular & cellular proteomics : MCP2018

Analysis of Mammalian O-Glycopeptides-We Have Made a Good Start, but There is a Long Way to Go.

Zsuzsanna Darula, Katalin F Medzihradszky

Abstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
–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

46 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Extension ofmBio · 2022
    Article
  15. DecipheringMolecular omics · 2022
    Article
  16. Review
  17. Revealing the human mucinome.Nature communications · 2022
    Article
  18. Article
  19. Article
  20. Article
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

2 authors.

Zsuzsanna DarulaFrom the ‡Laboratory of Proteomics Research, Biological Research Centre, Hungarian Academy of Sciences, H-6726, 62 Temesvari krt, Szeged, Hungary.
Katalin F MedzihradszkyFrom the ‡Laboratory of Proteomics Research, Biological Research Centre, Hungarian Academy of Sciences, H-6726, 62 Temesvari krt, Szeged, Hungary; medzihradszky.katalin@brc.mta.hu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is perhaps the most common post-translational modification. Recently there has been growing interest in cataloging the glycan structures, glycoproteins, and specific sites modified and deciphering the biological functions of glycosylation. Although the results are piling up for N-glycosylation, O-glycosylation is seriously trailing behind. In our review we reiterate the difficulties researchers have to overcome in order to characterize O-glycosylation. We describe how an ingenious cell engineering method delivered exciting results, and what could we gain from "wild-type" samples. Although we refer to the biological role(s) of O-glycosylation, we do not provide a complete inventory on this topic.

Indexed as

AnimalsGlycopeptidesGlycosylationHumansGlycopeptides

Identifiers

PMID29162637
PMCPMC5750848

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.