Evidence map›Paper›PMID 25713063›Full record

ArticleThe Journal of biological chemistry2015

Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.

Monika Soudi, Martina Paumann-Page, Cedric Delporte, Katharina F Pirker, Marzia Bellei, Eva Edenhofer, Gerhard Stadlmayr, Gianantonio Battistuzzi, Karim Zouaoui Boudjeltia, Paul G Furtmüller and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. The role of peroxidasin in solid cancer progression.Biochemical Society transactions · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Inhibition of Myeloperoxidase.Handbook of experimental pharmacology · 2021
    Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. 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

12 authors at 2 institutions in 2 countries.

Monika SoudiFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Martina Paumann-PageFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Cedric Delportethe Laboratory of Pharmaceutical Chemistry and Analytical Platform of the Faculty of Pharmacy, Faculty of Pharmacy, Université Libre de Bruxelles, 1050 Brussels, Belgium.
Katharina F PirkerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Marzia Belleithe Departments of Life Sciences and.
Eva EdenhoferFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Gerhard StadlmayrFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Gianantonio BattistuzziChemistry and Geology, University of Modena and Reggio Emilia, 41125 Modena, Italy, and.
Karim Zouaoui Boudjeltiathe Laboratory of Experimental Medicine (ULB 222 Unit), CHU de Charleroi, A. Vésale Hospital, Université Libre de Bruxelles, 6110 Montigny-le-Tilleul, Belgium.
Paul G FurtmüllerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
Pierre Van Antwerpenthe Laboratory of Pharmaceutical Chemistry and Analytical Platform of the Faculty of Pharmacy, Faculty of Pharmacy, Université Libre de Bruxelles, 1050 Brussels, Belgium.
Christian ObingerFrom the Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria, christian.obinger@boku.ac.at.
BOKU University · ATUniversité Libre de Bruxelles · BE

Funding

Austrian Science Fund FWF P 25538Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links. The latter confers critical structural reinforcement to collagen IV scaffolds. Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines. The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported. The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0. Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation. This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.

Indexed as

Antigens, NeoplasmCatalysisCollagen Type IVGlycosylationHEK293 CellsHumansIronOxidation-ReductionPeroxidasesPeroxidasinProtein Structure, TertiaryReceptors, Interleukin-1Structure-Activity RelationshipAntigens, NeoplasmCollagen Type IVIronPeroxidasesPeroxidasinPXDN protein, humanReceptors, Interleukin-1CollagenExtracellular Matrix ProteinGlycosylationMetalloenzymePeroxidasePeroxidasinVascular Peroxidase

Identifiers

PMID25713063
PMCPMC4409251
OpenAlexW2071035804

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.