ArticleNature communications2020
Fibrinogen function achieved through multiple covalent states.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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.
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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.
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Who cites it
30 citing papers in PubMed, 44 citations in OpenAlex.
- PRP-activating hyaluronic acid hydrogels for immune-modulatory osteoarthritis repair.Bioactive materials · 2027Article
- Hepatic Mechanisms and Therapeutic Target Underpinning Hypercoagulation in Obesity: Insights From Genetic and Transcriptomic Analyses.Exploration (Beijing, China) · 2026Article
- Evaluation of Alkaline-Labile Sulfane Sulfur in Biological Samples: The Influence of Hyperhomocysteinemia and Oxidative Stress.Biomolecules · 2026Article
- Multiple disulfide-bonded states confer extensive conformational diversity in fibrinogen.Protein science : a publication of the Protein Society · 2026Article
- Estimate of Numbers of Disulfide-Bonded Protein States.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Quantification of the Redox State of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Polyclonal Antibody Selection of Partially Disulfide-Bonded Protein States.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Method for Selection of Antithrombin Disulfide-Bonded Subsets.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Quantification of the Redox State of Integrin Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Using AlphaFold3 for the Interrogation of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Fibrin Glues: Proteins, Mechanism of Action, Classification, and Application.International journal of molecular sciences · 2025Review
- Allosteric Disulfide Bridges in Integrins: The Molecular Switches of Redox Regulation of Integrin-Mediated Cell Functions.Antioxidants (Basel, Switzerland) · 2025Review
- Patient anti-FVIII drug antibodies bind preferentially to a subset of FVIII covalent states.Blood advances · 2025Article
- In the flow, how fluid dynamics shapes amyloid formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fibrinogen post-translational modifications are biochemical determinants of fibrin clot properties and interactions.The FEBS journal · 2025Review
- Regulation of fibrinogen synthesis.Thrombosis research · 2024Review
- Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis.Journal of thrombosis and haemostasis : JTH · 2024Review
- Bioactivity, hemocompatibility, and inflammatory response of calcium incorporated sulfonated polyether ether ketone on mouse-derived bone marrow cells.Bioscience reports · 2024Article
- Fibrinogen and fibrin: synthesis, structure, and function in health and disease.Journal of thrombosis and haemostasis : JTH · 2023Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds link pairs of cysteine amino acids and their formation is assumed to be complete in the mature, functional protein. Here, we test this assumption by quantifying the redox state of disulfide bonds in the blood clotting protein fibrinogen. The disulfide status of fibrinogen from healthy human donor plasma and cultured human hepatocytes are measured using differential cysteine alkylation and mass spectrometry. This analysis identifies 13 disulfide bonds that are 10-50% reduced, indicating that fibrinogen is produced in multiple disulfide-bonded or covalent states. We further show that disulfides form upon fibrin polymerization and are required for a robust fibrin matrix that withstands the mechanical forces of flowing blood and resists premature fibrinolysis. The covalent states of fibrinogen are changed by fluid shear forces ex vivo and in vivo, indicating that the different states are dynamic. These findings demonstrate that fibrinogen exists and functions as multiple covalent forms.
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Registered trials
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.