Evidence map›Paper›PMID 20807768›Full record

ArticleThe Journal of biological chemistry2010

Mutational tuning of galectin-3 specificity and biological function.

Emma Salomonsson, Michael C Carlsson, Veronica Osla, Ruth Hendus-Altenburger, Barbro Kahl-Knutson, Christopher T Oberg, Anders Sundin, Rickard Nilsson, Eva Nordberg-Karlsson, Ulf J Nilsson and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

54 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025
    Review
  3. Binding free energy analysis of galectin-3 natural ligands and synthetic inhibitors.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
  5. Article
  6. Gal-3 blocks the binding between PD-1 and pembrolizumab.Journal for immunotherapy of cancer · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Anchoring immunosuppression to inflamed tissue.Nature biomedical engineering · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
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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

13 authors at 3 institutions in 2 countries.

Emma SalomonssonSection MIG, Department of Laboratory Medicine, Lund University, 223 62 Lund, Sweden.
Michael C Carlsson
Veronica Osla
Ruth Hendus-Altenburger
Barbro Kahl-Knutson
Christopher T Oberg
Anders Sundin
Rickard Nilsson
Eva Nordberg-Karlsson
Ulf J Nilsson
Anna Karlsson
James M Rini
Hakon Leffler
Lund University · SEUniversity of Gothenburg · SEUniversity of Toronto · CA

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Galectins are defined by a conserved β-galactoside binding site that has been linked to many of their important functions in e.g. cell adhesion, signaling, and intracellular trafficking. Weak adjacent sites may enhance or decrease affinity for natural β-galactoside-containing glycoconjugates, but little is known about the biological role of this modulation of affinity (fine specificity). We have now produced 10 mutants of human galectin-3, with changes in these adjacent sites that have altered carbohydrate-binding fine specificity but that retain the basic β-galactoside binding activity as shown by glycan-array binding and a solution-based fluorescence anisotropy assay. Each mutant was also tested in two biological assays to provide a correlation between fine specificity and function. Galectin-3 R186S, which has selectively lost affinity for LacNAc, a disaccharide moiety commonly found on glycoprotein glycans, has lost the ability to activate neutrophil leukocytes and intracellular targeting into vesicles. K176L has increased affinity for β-galactosides substituted with GlcNAcβ1-3, as found in poly-N-acetyllactosaminoglycans, and increased potency to activate neutrophil leukocytes even though it has lost other aspects of galectin-3 fine specificity. G182A has altered carbohydrate-binding fine specificity and altered intracellular targeting into vesicles, a possible link to the intracellular galectin-3-mediated anti-apoptotic effect known to be lost by this mutant. Finally, the mutants have helped to define the differences in fine specificity shown by Xenopus, mouse, and human galectin-3 and, as such, the evidence for adaptive change during evolution.

Indexed as

Mutation, MissenseAmino Acid SubstitutionAnimalsGalactosidesGalectin 3HumansMiceNeutrophil ActivationNeutrophilsSubstrate SpecificityXenopus laevisGalactosidesGalectin 3Lgals3 protein, mouse

Identifiers

PMID20807768
PMCPMC2966122
OpenAlexW2090602226

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.