Evidence map›Paper›PMID 29440651›Full record

ArticleScientific reports2018

Reconstruction of the sialylation pathway in the ancestor of eukaryotes.

Daniel Petit, Elin Teppa, Ugo Cenci, Steven Ball, Anne Harduin-Lepers

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. Review
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  9. Article
  10. Vertebrate Alpha2,8-Sialyltransferases (ST8Sia): A Teleost Perspective.International journal of molecular sciences · 2020
    Article
  11. Article
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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 3 institutions in 2 countries.

Daniel PetitUniversité de Limoges, Laboratoire Pereine 123, av. A. Thomas, 87060, Limoges Cedex, France.
Elin TeppaBioinformatics Unit, Fundación Instituto Leloir -IIBBA CONICET, Av. Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina.
Ugo CenciUniversity of Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000, Lille, France.
Steven BallUniversity of Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000, Lille, France.
Anne Harduin-LepersUniversity of Lille, CNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, F 59000, Lille, France. anne.harduin@univ-lille1.fr.ORCID 0000-0002-1233-3799
Centre National de la Recherche Scientifique · FRConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversité de Limoges · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biosynthesis of sialylated molecules of crucial relevance for eukaryotic cell life is achieved by sialyltransferases (ST) of the CAZy family GT29. These enzymes are widespread in the Deuterostoma lineages and more rarely described in Protostoma, Viridiplantae and various protist lineages raising the question of their presence in the Last eukaryotes Common Ancestor (LECA). If so, it is expected that the main enzymes associated with sialic acids metabolism are also present in protists. We conducted phylogenomic and protein sequence analyses to gain insights into the origin and ancient evolution of ST and sialic acid pathway in eukaryotes, Bacteria and Archaea. Our study uncovered the unreported occurrence of bacterial GT29 ST and evidenced the existence of 2 ST groups in the LECA, likely originating from the endosymbiotic event that generated mitochondria. Furthermore, distribution of the major actors of the sialic acid pathway in the different eukaryotic phyla indicated that these were already present in the LECA, which could also access to this essential monosaccharide either endogenously or via a sialin/sialidase uptake mechanism involving vesicles. This pathway was lost in several basal eukaryotic lineages including Archaeplastida despite the presence of two different ST groups likely assigned to other functions.

Indexed as

Computational BiologyProtein Processing, Post-TranslationalAmino Acid SequenceEukaryotaN-Acetylneuraminic AcidPhylogenyN-Acetylneuraminic Acid

Identifiers

PMID29440651
PMCPMC5811610
OpenAlexW2806984929

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.