Evidence map›Paper›PMID 8785483›Full record

ReviewGlycoconjugate journal1996

O-linked protein glycosylation structure and function.

E F Hounsell, M J Davies, D V Renouf

Abstract readReview
PubMed Publisher
In one paragraph

Review in Glycoconjugate journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 225 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. A Coarse-Grained MARTINI Model for Mucins.Journal of chemical theory and computation · 2026
    Article
  6. GalNAc-Transferases in Cancer.Biomedicines · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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  18. Article
  19. Article
  20. Targeting Glycoproteins as a therapeutic strategy for diabetes mellitus and its complications.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2020
    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

3 authors at 1 institution in 1 country.

E F HounsellDepartment of Biochemistry and Molecular Biology, University College London, UK.
M J Davies
D V Renouf
University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There has been a recent resurgence of interest in the post-translational modification of serine and threonine hydroxyl groups by glycosylation, because the resulting O-linked oligosaccharide chains tend to be clustered over short stretches of peptide and hence they can present multivalent carbohydrate antigenic or functional determinants for antibody recognition, mammalian cell adhesion and microorganism binding. Co-operativity can greatly increase the affinity of interactions with antibodies or carbohydrate binding proteins. Thus, in addition to their known importance in bearing tumour associated antigens in the gastrointestinal and respiratory tracts, glycoproteins with O-linked chains have been implicated as ligands or co-receptors for selectins (mammalian carbohydrate binding proteins). Microorganisms may have adopted similar mechanisms for interactions with mammalian cells in infection, by having relatively low affinity ligands (adhesins) for carbohydrate binding, which may bind with higher affinity due to the multivalency of the host ligand and which are complemented by other virulence factors such as interactions with integrin-type molecules. In addition to specific adhesion signals from O-linked carbohydrate chains, multivalent O-glycosylation is involved in determining protein conformation and forming conjugate oligosaccharide-protein antigenic, and possible functional determinants.

Indexed as

Amino Acid SequenceAnimalsCarbohydrate ConformationCarbohydrate SequenceGlycoconjugatesGlycoproteinsGlycosylationHumansMagnetic Resonance SpectroscopyMolecular Sequence DataMolecular StructureProtein ConformationProtein Processing, Post-TranslationalThermodynamicsGlycoconjugatesGlycoproteins

Identifiers

PMID8785483
OpenAlexW1992042749

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.