Evidence map›Paper›PMID 18694936›Full record

ArticleThe Journal of biological chemistry2008

Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase.

Martina Ulrich, Alina Petre, Nikolay Youhnovski, Franziska Prömm, Markus Schirle, Michael Schumm, Ralph S Pero, Alfred Doyle, James Checkel, Hirohito Kita and 11 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Current issues in molecular biology · 2024
    Article
  3. Review
  4. Review
  5. Article
  6. White blood cell count and eosinopenia as valuable tools for the diagnosis of bacterial infections in the ED.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2019
    Observational
  7. Article
  8. Review
  9. Article
  10. Article
  11. Eosinophil granule proteins: form and function.The Journal of biological chemistry · 2014
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Biology of the eosinophil.Advances in immunology · 2009
    Review
  18. Review
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

21 authors at 14 institutions in 7 countries.

Martina UlrichInstitute of Medical Microbiology and Hygiene, Universitätsklinikum Tübingen, Tübingen 72074, Germany.
Alina Petre
Nikolay Youhnovski
Franziska Prömm
Markus Schirle
Michael Schumm
Ralph S Pero
Alfred Doyle
James Checkel
Hirohito Kita
Nethaji Thiyagarajan
K Ravi Acharya
Peter Schmid-Grendelmeier
Hans-Uwe Simon
Heinz Schwarz
Masato Tsutsui
Hiroaki Shimokawa
Gabriel Bellon
James J Lee
Michael Przybylski
Gerd Döring
Mayo Clinic in Arizona · USUniversity of Konstanz · DEMayo Clinic · USUniversitätsklinikum Tübingen · DEUniversity of Bath · GBHospices Civils de Lyon · FRInstitute of Medical Microbiology and Hygiene · DEMax Planck Society · DENovartis (United States) · USTH Bingen University of Applied Sciences · DETohoku University · JPUniversity Hospital of Zurich · CHUniversity of Bern · CHUniversity of Occupational and Environmental Health Japan · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitration of tyrosine residues has been observed during various acute and chronic inflammatory diseases. However, the mechanism of tyrosine nitration and the nature of the proteins that become tyrosine nitrated during inflammation remain unclear. Here we show that eosinophils but not other cell types including neutrophils contain nitrotyrosine-positive proteins in specific granules. Furthermore, we demonstrate that the human eosinophil toxins, eosinophil peroxidase (EPO), major basic protein, eosinophil-derived neurotoxin (EDN) and eosinophil cationic protein (ECP), and the respective murine toxins, are post-translationally modified by nitration at tyrosine residues during cell maturation. High resolution affinity-mass spectrometry identified specific single nitration sites at Tyr349 in EPO and Tyr33 in both ECP and EDN. ECP and EDN crystal structures revealed and EPO structure modeling suggested that the nitrated tyrosine residues in the toxins are surface exposed. Studies in EPO(-/-), gp91phox(-/-), and NOS(-/-) mice revealed that tyrosine nitration of these toxins is mediated by EPO in the presence of hydrogen peroxide and minute amounts of NOx. Tyrosine nitration of eosinophil granule toxins occurs during maturation of eosinophils, independent of inflammation. These results provide evidence that post-translational tyrosine nitration is unique to eosinophils.

Indexed as

Protein Processing, Post-TranslationalAnimalsBinding SitesCrystallography, X-RayEosinophil PeroxidaseEosinophilsHumansInflammationLungMiceMice, Inbred C57BLMice, TransgenicNeurotoxinsNitrogenTyrosineEosinophil PeroxidaseNeurotoxinsNitrogenTyrosine

Identifiers

PMID18694936
PMCPMC2661412
OpenAlexW2097187926

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.