Evidence map›Paper›PMID 39477884›Full record

ReviewMolecular biomedicine2024

Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation.

Francesca Nencini, Alessandra Bettiol, Flavia Rita Argento, Serena Borghi, Elvira Giurranna, Giacomo Emmi, Domenico Prisco, Niccolò Taddei, Claudia Fiorillo, Matteo Becatti

Abstract readReview
In one paragraph

Review in Molecular biomedicine, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen.Protein science : a publication of the Protein Society · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Homocysteinylation of Fibrinogen: A Post-Translational Link to Thrombosis.International journal of molecular sciences · 2025
    Review
  20. 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

10 authors.

Francesca NenciniDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Alessandra BettiolDepartment of Experimental and Clinical Medicine, University of Firenze, Firenze, Italy.
Flavia Rita ArgentoDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Serena BorghiDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Elvira GiurrannaDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Giacomo EmmiDepartment of Medical, Surgical and Health Sciences, University of Trieste, Trieste, Italy.
Domenico PriscoDepartment of Experimental and Clinical Medicine, University of Firenze, Firenze, Italy.
Niccolò TaddeiDepartment of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Claudia Fiorillo *Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy.
Matteo Becatti *Department of Experimental and Clinical Biomedical Sciences "Mario Serio", University of Firenze, Firenze, Italy. matteo.becatti@unifi.it.

Funding

THE Tuscany Health Ecosystem CUP: B83C22003920001
6 · The paper itself

Abstract

Fibrinogen, a blood plasma protein with a key role in hemostasis and thrombosis, is highly susceptible to post-translational modifications (PTMs), that significantly influence clot formation, structure, and stability. These PTMs, which include acetylation, amidation, carbamylation, citrullination, dichlorination, glycation, glycosylation, guanidinylation, hydroxylation, homocysteinylation, malonylation, methylation, nitration, oxidation, phosphorylation and sulphation, can alter fibrinogen biochemical properties and affect its functional behavior in coagulation and fibrinolysis. Oxidation and nitration are notably associated with oxidative stress, impacting fibrin fiber formation and promoting the development of more compact and resistant fibrin networks. Glycosylation and glycation contribute to altered fibrinogen structural properties, often resulting in changes in fibrin clot density and susceptibility to lysis, particularly in metabolic disorders like diabetes. Acetylation and phosphorylation, influenced by medications such as aspirin, modulate clot architecture by affecting fiber thickness and clot permeability. Citrullination and homocysteinylation, although less studied, are linked to autoimmune conditions and cardiovascular diseases, respectively, affecting fibrin formation and stability. Understanding these modifications provides insights into the pathophysiology of thrombotic disorders and highlights potential therapeutic targets. This review comprehensively examines the current literature on fibrinogen PTMs, their specific sites, biochemical pathways, and their consequences on fibrin clot architecture, clot formation and clot lysis.

Indexed as

Blood CoagulationFibrinFibrinogenProtein Processing, Post-TranslationalAnimalsFibrinolysisGlycosylationHumansPhosphorylationProteolysisThrombosisFibrinFibrinogenFibrinFibrinogenPost-translational modificationsThrombosis

Identifiers

PMID39477884
PMCPMC11525374

What Socratic 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 Socratic graph.