Evidence map›Paper›PMID 17194707›Full record

ArticleThe Journal of biological chemistry2007

XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity.

Josef Voglmeir, Regina Voglauer, Iain B H Wilson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. XYLT1 mutations in Desbuquois dysplasia type 2.American journal of human genetics · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Polycystic disease caused by deficiency in xylosyltransferase 2, an initiating enzyme of glycosaminoglycan biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2007
    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

3 authors at 3 institutions in 2 countries.

Josef VoglmeirDepartment für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria.
Regina Voglauer
Iain B H Wilson
BOKU University · ATFugro (Norway) · NOUniversity of Applied Arts Vienna · AT

Funding

Austrian Science Fund FWF P 18447
6 · The paper itself

Abstract

Peptide O-xylosyltransferase (EC 2.4.2.26) is the first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans. Cloning of cDNAs has previously shown that, whereas invertebrates generally have a single xylosyltransferase gene, vertebrate genomes encode two similar proteins, xylosyltransferase I and II (XT-I and XT-II). To date, enzymatic activity has only been demonstrated for the human XT-I, Caenorhabditis SQV-6, and Drosophila OXT isoforms. In the present study, we demonstrate that a soluble form of human XT-II expressed in the xylosyltransferase-deficient pgsA-745 (S745) Chinese hamster ovary cell line is indeed capable of catalyzing the transfer of xylose to a variety of peptide substrates; its enzyme activity was also proven using a Pichia-expressed form of XT-II. Its pH, temperature, and cation dependences are similar to those of XT-I expressed in either mammalian cells or yeast. Our data suggest that XT-I and XT-II are, at least in vitro, functionally identical.

Indexed as

AnimalsCatalysisCationsCHO CellsCloning, MolecularCricetinaeCricetulusHumansHydrogen-Ion ConcentrationPentosyltransferasesPeptidesProtein IsoformsSolubilityTemperatureUDP Xylose-Protein XylosyltransferaseXyloseCationsPentosyltransferasesPeptidesProtein IsoformsUDP Xylose-Protein XylosyltransferaseXylose

Identifiers

PMID17194707
PMCPMC2850172
OpenAlexW2059305916

What OpenQuestion holds

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LicenceTDM
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.