Evidence map›Paper›PMID 29730795›Full record

ReviewHistochemistry and cell biology2018

From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.

Herbert Kaltner, Gabriel García Caballero, Anna-Kristin Ludwig, Joachim C Manning, Hans-Joachim Gabius

Abstract readReview
PubMed Publisher
In one paragraph

Review in Histochemistry and cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. What is the Sugar Code?Chembiochem : a European journal of chemical biology · 2022
    Review
  3. IntroducingMethods in molecular biology (Clifton, N.J.) · 2022
    Article
  4. Exploring the Galectin Network by Light and Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  5. Lentil lectin derived fromEmerging microbes & infections · 2021
    Article
  6. The marriage of chemokines and galectins as functional heterodimers.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Galectin-Glycan Interactions: Guidelines for Monitoring byChemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  13. In focus in HCB.Histochemistry and cell biology · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. TIM-3 and CEACAM1 do not interact in cis and in trans.European journal of immunology · 2020
    Article
  18. How galectins have become multifunctional proteins.Histology and histopathology · 2020
    Review
  19. Review
  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.

Herbert KaltnerInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany.
Gabriel García CaballeroInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany.
Anna-Kristin LudwigInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany.
Joachim C ManningInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany.
Hans-Joachim GabiusInstitute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany. gabius@tiph.vetmed.uni-muenchen.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

About 60 years ago, the efforts to identify blood group-specific haemagglutinins in plant extracts by broad-scale testing were beginning to make a large panel of these proteins available as laboratory tools. Their ability to 'read' cell surface signals like antibodies do was the reason for W. C. Boyd to call them lectins, from Latin legere (to read). These proteins turned out to be as widely present in nature as glycans (polysaccharides or carbohydrate chains of cellular glycoconjugates) are. Since carbohydrates have the virtue to facilitate high-density coding in a minimum of space and lectins (initially mostly from plants called phytohaemagglutinins) turned out to be receptors for glycans, their pairing made many applications possible. Most prominently, these proteins were instrumental to map glycome complexity and sites of product generation during glycan assembly in the cell. The detection of mammalian (tissue) lectins and the emerging evidence for intimate molecular recognition between this class of receptors and their (glycoconjugate) counterreceptors substantiate that understanding the rules of the sugar code is presently a major challenge.

Indexed as

HistocytochemistryAnimalsHumansLectinsPhenotypePolysaccharidesLectinsPolysaccharidesGalectinGlycocalyxGlycosylationHaemagglutininSugar code

Identifiers

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.