Evidence map›Paper›PMID 31922250›Full record

ReviewHistology and histopathology2020

How galectins have become multifunctional proteins.

Gabriel García Caballero, Herbert Kaltner, Tanja J Kutzner, Anna-Kristin Ludwig, Joachim C Manning, Sebastian Schmidt, Fred Sinowatz, Hans-Joachim Gabius

Abstract readReview
PubMed Publisher
In one paragraph

Review in Histology and histopathology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Seminal Plasma Glycoproteins as Potential Ligands of Lectins Engaged in Immunity Regulation.International journal of environmental research and public health · 2022
    Review
  13. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Exploring the Galectin Network by Light and Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  18. IntroducingMethods in molecular biology (Clifton, N.J.) · 2022
    Article
  19. What Happens If a Human Galectin Enters the Endoplasmic Reticulum?Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  20. Examining Galectin Gene Regulation by Reporter Assays.Methods in molecular biology (Clifton, N.J.) · 2022
    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

8 authors at 1 institution in 1 country.

Gabriel García CaballeroInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Herbert KaltnerInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Tanja J KutznerInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Anna-Kristin LudwigInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Joachim C ManningInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Sebastian SchmidtInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Fred SinowatzInstitute of Anatomy, Histology and Embryology, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany. gabius@tiph.vetmed.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DE

Funding

- -
6 · The paper itself

Abstract

Having identified glycans of cellular glycoconjugates as versatile molecular messages, their recognition by sugar receptors (lectins) is a fundamental mechanism within the flow of biological information. This type of molecular interplay is increasingly revealed to be involved in a wide range of (patho)physiological processes. To do so, it is a vital prerequisite that a lectin (and its expression) can develop more than a single skill, that is the general ability to bind glycans. By studying the example of vertebrate galectins as a model, a total of five relevant characteristics is disclosed: i) access to intra- and extracellular sites, ii) fine-tuned gene regulation (with evidence for co-regulation of counterreceptors) including the existence of variants due to alternative splicing or single nucleotide polymorphisms, iii) specificity to distinct glycans from the glycome with different molecular meaning, iv) binding capacity also to peptide motifs at different sites on the protein and v) diversity of modular architecture. They combine to endow these lectins with the capacity to serve as multi-purpose tools. Underscoring the arising broad-scale significance of tissue lectins, their numbers in terms of known families and group members have steadily grown by respective research that therefore unveiled a well-stocked toolbox. The generation of a network of (ga)lectins by evolutionary diversification affords the opportunity for additive/synergistic or antagonistic interplay in situ, an emerging aspect of (ga)lectin functionality. It warrants close scrutiny. The realization of the enormous potential of combinatorial permutations using the five listed features gives further efforts to understand the rules of functional glycomics/lectinomics a clear direction.

Indexed as

GalectinsAnimalsBinding SitesBiological EvolutionCell DifferentiationGalactoseGalectin 1Galectin 3Gene Expression RegulationGlycoconjugatesHumansLigandsPeptidesPolysaccharidesReceptors, Cell SurfaceGalactoseGalectin 1Galectin 3GalectinsGlycoconjugatesLGALS1 protein, humanLigandsPeptidesPolysaccharidesReceptors, Cell Surface

Identifiers

PMID31922250
OpenAlexW3003839889

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.