Evidence map›Paper›PMID 36083779›Full record

ArticleJournal of thrombosis and haemostasis : JTH2022

Citrullinated fibrinogen forms densely packed clots with decreased permeability.

Imre Varjú, Erzsébet Tóth, Ádám Z Farkas, Veronika J Farkas, Erzsébet Komorowicz, Tímea Feller, Balázs Kiss, Miklós Z Kellermayer, László Szabó, András Wacha and 3 more

Open access · greenAbstract read
In one paragraph

Article in Journal of thrombosis and haemostasis : JTH, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 19 citations in OpenAlex.

  1. Observational
  2. Article
  3. Article
  4. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
  5. Review
  6. Article
  7. Deconstructing fibrin(ogen) structure.Journal of thrombosis and haemostasis : JTH · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Citrullination of matrisomal proteins in health and diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  14. Current insights into the role of citrullination in thrombosis.Current opinion in chemical biology · 2023
    Review
  15. Review
  16. Fibrin clot properties and thrombus composition in cirrhosis.Research and practice in thrombosis and haemostasis · 2023
    Article
  17. 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

13 authors at 3 institutions in 3 countries.

Imre VarjúProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, Massachusetts, USA.ORCID 0000-0001-6592-4800
Erzsébet TóthDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0003-2293-0631
Ádám Z FarkasDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0003-4612-380X
Veronika J FarkasDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-4101-7736
Erzsébet KomorowiczDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-4860-3498
Tímea FellerDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-9137-5881
Balázs KissDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-2347-5928
Miklós Z KellermayerDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-5553-6553
László SzabóDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-2472-5933
András WachaBiological Nanochemistry Research Group, Institute of Materials and Environmental Chemistry, Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.ORCID 0000-0002-9609-0893
Attila BótaBiological Nanochemistry Research Group, Institute of Materials and Environmental Chemistry, Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.ORCID 0000-0002-8636-1426
Colin LongstaffNational Institute for Biological Standards and Control, South Mimms, UK.ORCID 0000-0001-7608-208X
Krasimir KolevDepartment of Biochemistry, Institute of Biochemistry and Molecular Biology, Semmelweis University, Budapest, Hungary.ORCID 0000-0002-5612-004X
Semmelweis University · HUInstitute of Materials and Environmental Chemistry · HUNational Institute for Biological Standards and Control · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFibrin, the main scaffold of thrombi, is susceptible to citrullination by PAD (peptidyl arginine deiminase) 4, secreted from neutrophils during the formation of neutrophil extracellular traps. Citrullinated fibrinogen (citFg) has been detected in human plasma as well as in murine venous thrombi, and it decreases the lysability and mechanical resistance of fibrin clots.

objectiveTo investigate the effect of fibrinogen citrullination on the structure of fibrin clots.

methodsFibrinogen was citrullinated with PAD4 and clotted with thrombin. Scanning electron microscopy (SEM) and atomic force microscopy (AFM) were used to measure fiber thickness, fiber height/width ratio, and fiber persistence length in clots containing citFg. Fiber density was measured with laser scanning microscopy (LSM) and permeability measurements were carried out to estimate the porosity of the clots. The intra-fiber structure of fibrin was analyzed with small-angle X-ray scattering (SAXS).

resultsSEM images revealed a decrease in the median fiber diameter that correlated with the fraction of citFg in the clot, while the fiber width/length ratio remained unchanged according to AFM. With SAXS we observed that citrullination resulted in the formation of denser clots in line with increased fiber density shown by LSM. The permeability constant of citrullinated fibrin decreased more than 3-fold indicating significantly decreased porosity. SAXS also showed largely preserved periodicity in the longitudinal assembly of fibrin monomers.

conclusionThe current observations of thin fibers combined with dense packing and low porosity in the presence of citFg can provide a structural framework for the mechanical fragility and lytic resistance of citrullinated fibrin.

Indexed as

HemostaticsThrombosisAnimalsFibrinFibrinogenHumansMiceMicroscopy, Electron, ScanningPermeabilityScattering, Small AngleX-Ray DiffractionFibrinFibrinogenHemostaticsatomic force microscopycitrullinationfibrinprotein-arginine deiminasessmall-angle X-ray scattering

Identifiers

PMID36083779
PMCPMC9828116
OpenAlexW4295037520

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.