Evidence map›Paper›PMID 25902539›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Unraveling functional significance of natural variations of a human galectin by glycodendrimersomes with programmable glycan surface.

Shaodong Zhang, Ralph-Olivier Moussodia, Sabine Vértesy, Sabine André, Michael L Klein, Hans-Joachim Gabius, Virgil Percec

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.8field-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

37 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  8. Selective synthesis ofFrontiers in chemistry · 2022
    Article
  9. Role of Globotriaosylceramide in Physiology and Pathology.Frontiers in molecular biosciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. How galectins have become multifunctional proteins.Histology and histopathology · 2020
    Review
  16. Article
  17. Article
  18. Encoding biological recognition in a bicomponent cell-membrane mimic.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

7 authors at 3 institutions in 2 countries.

Shaodong ZhangRoy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323;
Ralph-Olivier MoussodiaRoy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323;
Sabine VértesyInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany; and.
Sabine AndréInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany; and.
Michael L KleinInstitute of Computational Molecular Science, Temple University, Philadelphia, PA 19122 mlklein@temple.edu percec@sas.upenn.edu.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539 Munich, Germany; and.
Virgil PercecRoy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323; mlklein@temple.edu percec@sas.upenn.edu.
Ludwig-Maximilians-Universität München · DEUniversity of Pennsylvania · USTemple University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Surface-presented glycans (complex carbohydrates) are docking sites for adhesion/growth-regulatory galectins within cell-cell/matrix interactions. Alteration of the linker length in human galectin-8 and single-site mutation (F19Y) are used herein to illustrate the potential of glycodendrimersomes with programmable glycan displays as a model system to reveal the functional impact of natural sequence variations in trans recognition. Extension of the linker length slightly reduces lectin capacity as agglutinin and slows down aggregate formation at low ligand surface density. The mutant protein is considerably less active as agglutinin and less sensitive to low-level ligand presentation. The present results suggest that mimicking glycan complexity and microdomain occurrence on the glycodendrimersome surface can provide key insights into mechanisms to accomplish natural selectivity and specificity of lectins in structural and topological terms.

Indexed as

Alternative SplicingAmino Acid SequenceAutoimmune DiseasesCell CommunicationCell MembraneGalectinsHumansLectinsLigandsMagnetic Resonance SpectroscopyMolecular Sequence DataMutationPolymorphism, Single NucleotidePolysaccharidesProtein BindingProtein ConformationGalectinsLectinsLGALS8 protein, humanLigandsPolysaccharidesadhesionagglutinationglycobiologymembrane mimicself-assembly

Identifiers

PMID25902539
PMCPMC4426414
OpenAlexW2079055720

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.