Evidence map›Paper›PMID 31326232›Full record

ReviewCurrent opinion in structural biology2019

Relating glycoprotein structural heterogeneity to function - insights from native mass spectrometry.

Weston B Struwe, Carol V Robinson

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Review
  2. Article
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  9. Review
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  11. Article
  12. Review
  13. Uncovering the Role ofJournal of the American Chemical Society · 2023
    Article
  14. Special Issue: New Insights into Protein Glycosylation.Molecules (Basel, Switzerland) · 2023
    Article
  15. Article
  16. Article
  17. Systems-Wide Site-Specific Analysis of Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  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

2 authors.

Weston B StruweDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK. Electronic address: weston.struwe@chem.ox.ac.uk.
Carol V RobinsonDepartment of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK. Electronic address: carol.robinson@chem.ox.ac.uk.

Funding

Wellcome Trust 104633Wellcome Trust 104633/Z/14/Z
6 · The paper itself

Abstract

Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological states. Most biotherapeutic proteins are glycosylated, which influences drug safety and efficacy. Therefore, the ability to characterize glycoproteins is important in all areas of biomolecular and medicinal research. Here we discuss recent advances in native mass spectrometry that have significantly improved our ability to characterize heterogeneous glycoproteins and to relate glycan structure to protein function.

Indexed as

GlycoproteinsMass SpectrometryPolysaccharidesGlycoproteinsPolysaccharides

Identifiers

PMID31326232
PMCPMC7104348

What OpenQuestion holds

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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.