Evidence map›Paper›PMID 27517905›Full record

ReviewInternational journal of molecular sciences2016

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal).

Roxana E Teppa, Daniel Petit, Olga Plechakova, Virginie Cogez, Anne Harduin-Lepers

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. AcetylatedFrontiers in oncology · 2025
    Article
  3. Review
  4. Review
  5. A brief history of galectin evolution.Frontiers in immunology · 2023
    Article
  6. Article
  7. Clinical and Diagnostic Significance of Sialic Acids Determination in Biological Material.Biochemistry (Moscow) Supplement. Series B, Biomedical chemistry · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Polysialic Acid in the Immune System.Frontiers in immunology · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Sialylation and sialyltransferase in insects.Glycoconjugate journal · 2018
    Review
  18. Article
  19. 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 5 institutions in 2 countries.

Roxana E TeppaBioinformatics Unit, Fundación Instituto Leloir, Av. Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina. elinteppa@gmail.com.
Daniel PetitLaboratoire de Génétique Moléculaire Animale, UMR 1061 INRA, Université de Limoges Faculté des Sciences et Techniques, 123 avenue Albert Thomas, 87060 Limoges, France. daniel.petit@unilim.fr.
Olga PlechakovaFRABio-FR3688 CNRS, Univ. Lille, bât. C9, 59655 Villeneuve d'Ascq cedex, France. olga.plechakova@univ-lille1.fr.
Virginie CogezUniv. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, 59000 Lille, France. virginie.cogez@univ-lille1.fr.
Anne Harduin-LepersUniv. Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, 59000 Lille, France. anne.harduin@univ-lille1.fr.
Centre National de la Recherche Scientifique · FRFundación Instituto Leloir · ARUnité de Glycobiologie Structurale et Fonctionnelle · FRUniversité de Lille · FRUniversité de Limoges · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell-cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.

Indexed as

AnimalsN-Acetylneuraminic AcidPhylogenySialyltransferasesVertebratesN-Acetylneuraminic AcidSialyltransferasesevolutionfunctional genomicsmolecular phylogenysialic acidsialyltransferases

Identifiers

PMID27517905
PMCPMC5000683
OpenAlexW2478662014

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.