Evidence map›Paper›PMID 18566887›Full record

ArticleGlycoconjugate journal2009

Assays of sialate-O-acetyltransferases and sialate-O-acetylesterases.

G Vinayaga Srinivasan, Roland Schauer

Abstract read
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In one paragraph

Article in Glycoconjugate journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Exploration of the Sialic Acid World.Advances in carbohydrate chemistry and biochemistry · 2018
    Review
  3. Review
  4. Article
  5. O-Acetylated sialic acids and their role in immune defense.Advances in experimental medicine and biology · 2011
    Article
  6. 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

2 authors at 1 institution in 1 country.

G Vinayaga SrinivasanBiochemisches Institut, Christian-Albrechts-Universität, Olshausenstr. 40, 24098 Kiel, Germany.
Roland Schauer
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The O-acetylation of sialic acids is one of the most frequent modifications of these monosaccharides and modulates many cell biological and pathological events. Sialic acid-specific O-acetyltransferases and O-acetylesterases are responsible for the metabolism of esterified sialic acids. Assays were developed for the analysis of the activities and specificities of these enzymes. The methods had to be varied in dependence on the substrate assayed, the kind of biological source, and the state of enzyme purity. With the new techniques the primary site of O-acetyl incorporation at C-7, catalyzed by the animal sialate-O-acetyltransferases studied, was ascertained. Correspondingly, this enzyme, for example from bovine submandibular gland, can be denominated as AcCoA:sialate-7-O-acetyltransferase (EC 2.3.1.45). Methods for assaying the activity of esterases de-O-acetylating sialic acids and their metabolic cooperation with the O-acetyltransferases are presented.

Indexed as

AcetylationAcetylesteraseAcetyltransferasesAnimalsCarboxylic Ester HydrolasesCattleChromatography, High Pressure LiquidChromatography, Thin LayerEnzyme AssaysFluorometryGammainfluenzavirusHumansLymphocytesN-Acetylneuraminic AcidAcetylesteraseAcetyltransferasesCarboxylic Ester HydrolasesN-Acetylneuraminic Acidsialate O-acetylesterasesialic acid O-acetyltransferase

Identifiers

PMID18566887
OpenAlexW2010897851

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.