Evidence map›Paper›PMID 36677618›Full record

ArticleMolecules (Basel, Switzerland)2023

Expression and Characterisation of the First Snail-Derived UDP-Gal: Glycoprotein-N-acetylgalactosamine β-1,3-Galactosyltransferase (T-Synthase) from

Marilica Zemkollari, Markus Blaukopf, Reingard Grabherr, Erika Staudacher

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

4 authors at 1 institution in 1 country.

Marilica ZemkollariDepartment of Chemistry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0001-7155-4113
Markus BlaukopfDepartment of Chemistry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Reingard GrabherrDepartment of Biotechnology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0002-4501-927X
Erika StaudacherDepartment of Chemistry, University of Natural Resources and Life Sciences, 1190 Vienna, Austria.ORCID 0000-0001-8282-1424
BOKU University · AT

Funding

Austrian Science Fund FWF P 33239FWF Austrian Science Fund P33239-B
6 · The paper itself

Abstract

UDP-Gal: glycoprotein-N-acetylgalactosamine β-1,3-galactosyltransferase (T-synthase, EC 2.4.1.122) catalyses the transfer of the monosaccharide galactose from UDP-Gal to GalNAc-Ser/Thr, synthesizing the core 1 mucin type O-glycan. Such glycans play important biological roles in a number of recognition processes. The crucial role of these glycans is acknowledged for mammals, but a lot remains unknown regarding invertebrate and especially mollusc O-glycosylation. Although core O-glycans have been found in snails, no core 1 β-1,3-galactosyltransferase has been described so far. Here, the sequence of the enzyme was identified by a BlastP search of the NCBI

Indexed as

BiomphalariaGalactosyltransferasesAcetylgalactosamineAmino Acid SequenceAnimalsCaenorhabditis elegansDrosophila melanogasterHumansMucinsPolysaccharidesUridine DiphosphateAcetylgalactosamineGalactosyltransferasesMucinsPolysaccharidesUridine DiphosphateBiomphalaria glabratamolluscO-glycosylationT-synthaseβ-1,3-galactosyltransferase

Identifiers

PMID36677618
PMCPMC9865085
OpenAlexW4313647053

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.