Evidence map›Paper›PMID 20947662›Full record

ArticleGlycobiology2011

The human Cas1 protein: a sialic acid-specific O-acetyltransferase?

Sigrid Arming, Dirk Wipfler, Juliane Mayr, Anette Merling, Ulrike Vilas, Roland Schauer, Reinhard Schwartz-Albiez, Reinhard Vlasak

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 63 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Role ofInternational journal of molecular sciences · 2026
    Article
  6. Identification and Evaluation of CMP-Sialic Acids.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Loss of sialic acid side-chainProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Influenza D virus utilizes both 9-Journal of virology · 2024
    Article
  15. Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024
    Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Role of Sialyl-Cells · 2021
    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 3 institutions in 2 countries.

Sigrid ArmingDepartment of Molecular Biology, University Salzburg, Austria.
Dirk Wipfler
Juliane Mayr
Anette Merling
Ulrike Vilas
Roland Schauer
Reinhard Schwartz-Albiez
Reinhard Vlasak
University of Salzburg · ATGerman Cancer Research Center · DEHeidelberg University · DE

Funding

Austrian Science Fund FWF L 608
6 · The paper itself

Abstract

Sialic acids are important sugars at the reducing end of glycoproteins and glycolipids. They are among many other functions involved in cell-cell interactions, host-pathogen recognition and the regulation of serum half-life of glycoproteins. An important modification of sialic acids is O-acetylation, which can alter or mask the biological properties of the parent sialic acid molecule. The nature of mammalian sialate-O-acetyltransferases (EC 2.3.1.45) involved in their biosynthesis is still unknown. We have identified the human CasD1 (capsule structure1 domain containing 1) gene as a candidate to encode the elusive enzyme. The human CasD1 gene encodes a protein with a serine-glycine-asparagine-histidine hydrolase domain and a hydrophobic transmembrane domain. Expression of the Cas1 protein tagged with enhanced green fluorescent protein in mammalian and insect cells directed the protein to the medial and trans-cisternae of the Golgi. Overexpression of the Cas1 protein in combination with α-N-acetyl-neuraminide α-2,8-sialyltransferase 1 (GD3 synthase) resulted in an up to 40% increased biosynthesis of 7-O-acetylated ganglioside GD3. By quantitative real-time polymerase chain reaction, we found up to 5-fold increase in CasD1 mRNA in tumor cells overexpressing O-Ac-GD3. CasD1-specific small interfering RNA reduced O-acetylation in tumor cells. These results suggest that the human Cas1 protein is directly involved in O-acetylation of α2-8-linked sialic acids.

Indexed as

AcetylationAcetyltransferasesAmino Acid SequenceCarbohydrate EpimerasesCatalytic DomainCell LineCloning, MolecularData MiningGene Knockdown TechniquesHumansLymphocytesMolecular Sequence DataN-Acetylneuraminic AcidProtein Structure, TertiaryRNA InterferenceSequence AlignmentAcetyltransferasesCarbohydrate EpimerasesCASD1 protein, humandermatan sulfate epimerase 1, mouseN-Acetylneuraminic Acid

Identifiers

PMID20947662
PMCPMC7108626
OpenAlexW2119688627

What OpenQuestion holds

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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.