Evidence map›Paper›PMID 22976969›Full record

ArticleChemistry & biodiversity2012

Molecular evolution, structure, and function of peroxidasins.

Monika Soudi, Marcel Zamocky, Christa Jakopitsch, Paul G Furtmüller, Christian Obinger

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biodiversity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Peroxidasin is required for full viability in development and for maintenance of tissue mechanics in adults.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022
    Review
  8. Article
  9. Article
  10. Inhibition of Myeloperoxidase.Handbook of experimental pharmacology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Inhibitory Anti-Peroxidasin Antibodies in Pulmonary-Renal Syndromes.Journal of the American Society of Nephrology : JASN · 2018
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Monika SoudiDepartment of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology at BOKU - University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna.
Marcel Zamocky
Christa Jakopitsch
Paul G Furtmüller
Christian Obinger
BOKU University · ATSlovak Academy of Sciences · SK

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Peroxidasins represent the subfamily 2 of the peroxidase-cyclooxygenase superfamily and are closely related to chordata peroxidases (subfamily 1) and peroxinectins (subfamily 3). They are multidomain proteins containing a heme peroxidase domain with high homology to human lactoperoxidase that mediates one- and two-electron oxidation reactions. Additional domains of the secreted and glycosylated metalloproteins are type C-like immunoglobulin domains, typical leucine-rich repeats, as well as a von Willebrand factor C module. These are typical motifs of extracellular proteins that mediate protein-protein interactions. We have reconstructed the phylogeny of this new family of oxidoreductases and show the presence of four invertebrate clades as well as one vertebrate clade that includes also two different human representatives. The variability of domain assembly in the various clades was analyzed, as was the occurrence of relevant catalytic residues in the peroxidase domain based on the knowledge of catalysis of the mammalian homologues. Finally, the few reports on expression, localization, enzymatic activity, and physiological roles in the model organisms Drosophila melanogaster, Caenorhabditis elegans, and Homo sapiens are critically reviewed. Roles attributed to peroxidasins include antimicrobial defense, extracellular matrix formation, and consolidation at various developmental stages. Many research questions need to be solved in future, including detailed biochemical/physical studies and elucidation of the three dimensional structure of a model peroxidasin as well as the relation and interplay of the domains and the in vivo functions in various organisms including man.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsChordataExtracellular Matrix ProteinsHumansModels, MolecularMolecular Sequence DataPeroxidasePeroxidasesPeroxidasinPhylogenySequence AlignmentExtracellular Matrix ProteinsPeroxidasePeroxidasesPeroxidasin

Identifiers

PMID22976969
PMCPMC3533774
OpenAlexW2036174322

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.