Evidence map›Paper›PMID 16120058›Full record

ArticleThe Biochemical journal2005

Molecular cloning and expression of a human hST8Sia VI (alpha2,8-sialyltransferase) responsible for the synthesis of the diSia motif on O-glycosylproteins.

Mélanie Teintenier-Lelièvre, Sylvain Julien, Sylvie Juliant, Yann Guerardel, Martine Duonor-Cérutti, Philippe Delannoy, Anne Harduin-Lepers

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cutting Edge: Enhanced Antitumor Immunity in ST8Sia6 Knockout Mice.Journal of immunology (Baltimore, Md. : 1950) · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Polysialic Acid in the Immune System.Frontiers in immunology · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Mélanie Teintenier-LelièvreUnité de Glycobiologie Structurale et Fonctionnelle, CNRS UMR 8576, IFR 118, GDR CNRS 2590, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
Sylvain Julien
Sylvie Juliant
Yann Guerardel
Martine Duonor-Cérutti
Philippe Delannoy
Anne Harduin-Lepers
Centre National de la Recherche Scientifique · FRUnité de Glycobiologie Structurale et Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Based on BLAST analysis of the human and mouse genome databases using the human CMP sialic acid; alpha2,8-sialyltransferase cDNA (hST8Sia I; EC 2.4.99.8), a putative sialyltransferase gene, was identified on human chromosome 10. The genomic organization was found to be similar to that of hST8Sia I and hST8Sia V. Transcriptional expression analysis showed that the newly identified gene was constitutively expressed at low levels in various human tissues and cell lines. We have isolated a full-length cDNA clone from the breast cancer cell line MCF-7 that encoded a type II membrane protein of 398 amino acid residues with the conserved motifs of sialyltransferases. We have established a mammary cell line (MDA-MB-231) stably transfected with the full-length hST8Sia VI and the analysis of sialylated carbohydrate structures expressed at the cell surface clearly indicated the disappearance of Neu5Acalpha2-3-sialylated structures. The transient expression of a truncated soluble form of the enzyme in either COS-7 cells or insect Sf-9 cells led to the production of an active enzyme in which substrate specificity was determined. Detailed substrate specificity analysis of the hST8Sia VI recombinant enzyme in vitro, revealed that this enzyme required the trisaccharide Neu5Acalpha2-3Galbeta1-3GalNAc (where Neu5Ac is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) to generate diSia (disialic acid) motifs specifically on O-glycans.

Indexed as

Gene Expression Regulation, EnzymologicAmino Acid SequenceAnimalsBase SequenceBinding SitesCell LineChromosome MappingChromosomes, Human, Pair 10Cloning, MolecularGlycoproteinsHumansMiceMolecular Sequence DataPhytohemagglutininsPolysaccharidesProtein Bindingalpha2,8-sialyltransferase VIGlycoproteinsleukoagglutinins, plantsPhytohemagglutininsPolysaccharidesSialyltransferases

Identifiers

PMID16120058
PMCPMC1316308
OpenAlexW2060751446

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.