Evidence map›Paper›PMID 22625207›Full record

ArticleNanomedicine (London, England)2012

Citrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.

Bashir M Mohamed, Navin K Verma, Anthony M Davies, Aoife McGowan, Kieran Crosbie-Staunton, Adriele Prina-Mello, Dermot Kelleher, Catherine H Botting, Corey P Causey, Paul R Thompson and 5 more

Abstract read
In one paragraph

Article in Nanomedicine (London, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Mechanisms of Environment-Induced Autoimmunity.Annual review of pharmacology and toxicology · 2021
    Article
  11. Macrophage-Derived Extracellular Vesicles as Drug Delivery Systems for Triple Negative Breast Cancer (TNBC) Therapy.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
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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

15 authors.

Bashir M MohamedDepartment of Clinical Medicine, Trinity College Dublin, Ireland.
Navin K Verma
Anthony M Davies
Aoife McGowan
Kieran Crosbie-Staunton
Adriele Prina-Mello
Dermot Kelleher
Catherine H Botting
Corey P Causey
Paul R Thompson
Ger Jm Pruijn
Elena R Kisin
Alexey V Tkach
Anna A Shvedova
Yuri Volkov

Funding

Haloacetamidine based inactivators of Protein Arginine Deiminase 4R01GM079357 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI THOMPSON, PAUL R · 2007 to 2016
$3.3M
NIGMS NIH HHS GM079357NIGMS NIH HHS R01 GM079357
6 · The paper itself

Abstract

aimRapidly expanding manufacture and use of nanomaterials emphasize the requirements for thorough assessment of health outcomes associated with novel applications. Post-translational protein modifications catalyzed by Ca(2+)-dependent peptidylargininedeiminases have been shown to trigger immune responses including autoantibody generation, a hallmark of immune complexes deposition in rheumatoid arthritis. Therefore, the aim of the study was to assess if nanoparticles are able to promote protein citrullination. MATERIALS &

methodsHuman A549 and THP-1 cells were exposed to silicon dioxide, carbon black or single-walled carbon nanotubes. C57BL/6 mice were exposed to respirable single-walled carbon nanotubes. Protein citrullination, peptidylargininedeiminases activity and target proteins were evaluated.

resultsThe studied nanoparticles induced protein citrullination both in cultured human cells and mouse lung tissues. Citrullination occurred via the peptidylargininedeiminase-dependent mechanism. Cytokeratines 7, 8, 18 and plectins were identified as intracellular citrullination targets.

conclusionNanoparticle exposure facilitated post-translational citrullination of proteins.

Indexed as

AnimalsCalciumCarbonCell LineCitrullineFemaleHumansHydrolasesLungMiceMice, Inbred C57BLNanostructuresNanotubes, CarbonProtein-Arginine DeiminasesProtein Processing, Post-TranslationalProteinsCalciumCarbonCitrullineHydrolasesNanotubes, CarbonProtein-Arginine DeiminasesProteinsSilicon DioxideSoot

Identifiers

PMID22625207
PMCPMC3465773

What OpenQuestion holds

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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.