Evidence map›Paper›PMID 36701102›Full record

ReviewGlycoconjugate journal2023

Gangliosides as Siglec ligands.

Ronald L Schnaar

Open access · greenAbstract readReview
In one paragraph

Review in Glycoconjugate journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Gangliosides in molecular interactions and cell regulation.The Journal of biological chemistry · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Methods for Investigating Siglec-Ganglioside Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Glycosylation in Cancer.Handbook of experimental pharmacology · 2025
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  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

1 author at 1 institution in 1 country.

Ronald L SchnaarDepartment of Pharmacology and Molecular Sciences, Department of Neuroscience, Johns Hopkins University School of Medicine, 725 N Wolfe St, Baltimore, MD, 21205, USA. schnaar@jhu.edu.ORCID 0000-0002-7701-5484
Johns Hopkins University · US

Funding

Using siglecs and their ligands to treat allergic diseases SALTADU19AI136443 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SCHNAAR, RONALD L · 2018 to 2022
$7.6M
Ganglioside interactome toolkitU01CA241953 · NCI · JOHNS HOPKINS UNIVERSITY · PI SCHNAAR, RONALD L · 2019 to 2021
$1.5M
NCI NIH HHS U01 CA241953NIAID NIH HHS U19 AI136443
6 · The paper itself

Abstract

The structure of a sialoglycan can be translated into to a biological response when it binds to a specific endogenous lectin. Among endogenous sialic acid-binding lectins in humans are those comprising the 15-member Siglec family, most of which are expressed on overlapping sets of immune cells. Endogenous Siglec ligands are sialoglycolipids (gangliosides) and/or sialoglycoproteins, on cell surfaces or in the extracellular milieu, that bind to and initiate signaling by cell surface Siglecs. In the nervous system, where gangliosides are the predominant sialoglycans, Siglec-4 (myelin-associated glycoprotein) on myelinating cells binds to gangliosides GD1a and GT1b on nerve cell axons to ensure stable and productive axon-myelin interactions. In the immune system, Siglec-7 on natural killer cells binds to gangliosides GD3 and GD2 to inhibit immune signaling. Expression of GD3 and GD2 on cancer cells can lead to tumor immune evasion. Siglec-1 (sialoadhesin, CD169) on macrophages binds to gangliosides on tumors and enveloped viruses. This may enhance antigen presentation in some cases, or increase viral distribution in others. Several other Siglecs bind to gangliosides in vitro, the biological significance of which has yet to be fully established. Gangliosides, which are found on all human cells and tissues in cell-specific distributions, are functional Siglec ligands with varied roles driving Siglec-mediated signaling.

Indexed as

GangliosidesSialic Acid Binding Immunoglobulin-like LectinsHumansLigandsNeuronsGangliosidesLigandsSialic Acid Binding Immunoglobulin-like LectinsCD33MacrophagesMyelin-associated glycoproteinNatural killer cellsSialic acidSialoadhesin

Identifiers

PMID36701102
PMCPMC11000168
OpenAlexW4318054885

What OpenQuestion holds

Textmetadata
LicenceTDM
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.