Evidence map›Paper›PMID 25621423›Full record

ReviewMolecules (Basel, Switzerland)2015

Lectins: getting familiar with translators of the sugar code.

Sabine André, Herbert Kaltner, Joachim C Manning, Paul V Murphy, Hans-Joachim Gabius

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.4field-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

28 citing papers in PubMed, 92 citations in OpenAlex.

  1. Characterization of a NovelInternational journal of molecular sciences · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.International journal of environmental research and public health · 2022
    Review
  8. Article
  9. Article
  10. 130 years of Plant Lectin Research.Glycoconjugate journal · 2020
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. 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

5 authors at 2 institutions in 2 countries.

Sabine AndréInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. Sabine.Andre@lmu.de.
Herbert KaltnerInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. kaltner@lmu.de.
Joachim C ManningInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. j.manning@lmu.de.
Paul V MurphySchool of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland. paul.v.murphy@nuigalway.ie.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University, Veterinärstr. 13, 80539 Munich, Germany. gabius@lectins.de.
Ludwig-Maximilians-Universität München · DEOllscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical properties endow carbohydrates to form oligomers with unsurpassed structural variability. Owing to their capacity to engage in hydrogen (and coordination) bonding and C-H/π-interactions these "code words" can be "read" (in Latin, legere) by specific receptors. A distinct class of carbohydrate-binding proteins are the lectins. More than a dozen protein folds have developed carbohydrate-binding capacity in vertebrates. Taking galectins as an example, distinct expression patterns are traced. The availability of labeled endogenous lectins facilitates monitoring of tissue reactivity, extending the scope of lectin histochemistry beyond that which traditionally involved plant lectins. Presentation of glycan and its cognate lectin can be orchestrated, making a glycan-based effector pathway in growth control of tumor and activated T cells possible. In order to unravel the structural basis of lectin specificity for particular glycoconjugates mimetics of branched glycans and programmable models of cell surfaces are being developed by strategic combination of lectin research with synthetic and supramolecular chemistry.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCarbohydrate SequenceGlycoproteinsHumansLectinsMolecular Sequence DataPolysaccharidesProtein BindingProtein ConformationGlycoproteinsLectinsPolysaccharides

Identifiers

PMID25621423
PMCPMC6272290
OpenAlexW2021726664

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.