Evidence map›Paper›PMID 32863239›Full record

ArticleRedox biology2020

Myeloperoxidase-derived damage to human plasma fibronectin: Modulation by protein binding and thiocyanate ions (SCN

Siriluck Vanichkitrungruang, Christine Y Chuang, Clare L Hawkins, Michael J Davies

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Myeloperoxidase impairs mucociliary transport on human airway epithelium.bioRxiv : the preprint server for biology · 2025
    Article
  3. Review
  4. Halogenation Activity of Mammalian Heme Peroxidases.Antioxidants (Basel, Switzerland) · 2022
    Review
  5. Heme Peroxidases at Unperturbed and Inflamed Mucous Surfaces.Antioxidants (Basel, Switzerland) · 2021
    Review
  6. Article
  7. Article
  8. The Dual Role of Myeloperoxidase in Immune Response.International journal of molecular sciences · 2020
    Review
  9. 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

4 authors at 1 institution in 2 countries.

Siriluck VanichkitrungruangThe Heart Research Institute, Newtown, NSW, Australia; Faculty of Medicine, The University of Sydney, NSW, Australia; Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Denmark.
Christine Y ChuangDepartment of Biomedical Sciences, Panum Institute, University of Copenhagen, Denmark.
Clare L HawkinsThe Heart Research Institute, Newtown, NSW, Australia; Faculty of Medicine, The University of Sydney, NSW, Australia; Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Denmark.
Michael J DaviesThe Heart Research Institute, Newtown, NSW, Australia; Faculty of Medicine, The University of Sydney, NSW, Australia; Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Denmark. Electronic address: davies@sund.ku.dk.
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelial cell dysfunction is an early event in cardiovascular disease and atherosclerosis. The origin of this dysfunction is unresolved, but accumulating evidence implicates damaging oxidants, including hypochlorous acid (HOCl), a major oxidant produced by myeloperoxidase (MPO), during chronic inflammation. MPO is released extracellularly by activated leukocytes and binds to extracellular molecules including fibronectin, a major matrix glycoprotein involved in endothelial cell binding. We hypothesized that MPO binding might influence the modifications induced on fibronectin, when compared to reagent HOCl, with this including alterations to the extent of damage to protein side-chains, modified structural integrity, changes to functional domains, and impact on naïve human coronary artery endothelial cell (HCAEC) adhesion and metabolic activity. The effect of increasing concentrations of the alternative MPO substrate thiocyanate (SCN

Indexed as

PeroxidaseThiocyanatesFibronectinsHumansHydrogen PeroxideHypochlorous AcidProtein BindingFibronectinsHydrogen PeroxideHypochlorous AcidPeroxidaseThiocyanatesEndothelial cellExtracellular matrixFibronectinHypochlorous acidHypothiocyanous acidMyeloperoxidaseProtein oxidation

Identifiers

PMID32863239
PMCPMC7378696
OpenAlexW3041944498

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.