ArticleDoklady. Biochemistry and biophysics2017
Oxidation-induced modification of the fibrinogen polypeptide chains.
Article in Doklady. Biochemistry and biophysics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Effects of Post-Translational Modifications of Fibrinogen on Clot Formation, Clot Structure, and Fibrinolysis: A Systematic Review.Arteriosclerosis, thrombosis, and vascular biology · 2020Pooled it
- Post-translational modifications in the insoluble fraction of platelet-poor plasma distinguish pre-COVID-19 Postural Orthostatic Tachycardia Syndrome, Long COVID, and Long COVID-POTS: a preliminary study.Cardiovascular diabetology · 2026Article
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Fibrinogen Oxidation and Thrombosis: Shaping Structure and Function.Antioxidants (Basel, Switzerland) · 2025Review
- Fibrinogen post-translational modifications are biochemical determinants of fibrin clot properties and interactions.The FEBS journal · 2025Review
- Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation.Molecular biomedicine · 2024Review
- Ascorbic acid prevents stress-induced hypercoagulability in overweight and obese individuals.Scientific reports · 2024Article
- Fibrin Clot Formation under Oxidative Stress Conditions.Antioxidants (Basel, Switzerland) · 2021Article
- Molecular Dynamic Simulations Suggest That Metabolite-Induced Post-Translational Modifications Alter the Behavior of the Fibrinogen Coiled-Coil Domain.Metabolites · 2021Article
- Article
- Hypochlorite-Induced Oxidative Modification of Fibrinogen.Doklady. Biochemistry and biophysics · 2019Article
- Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry.Doklady. Biochemistry and biophysics · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
By using the mass-spectrometry method, the oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains induced by its oxidation have been studied. The αC-region has been proven to be the most vulnerable target for the oxidizer (ozone) as compared with the other structural elements of the Aα chain. The Bβ chain mapping shows that the oxidative sites are localized within all the structural elements of the chain in which the β-nodule exhibits high susceptibility to oxidation. The γ chains are the least vulnerable to the oxidizer action. The results obtained demonstrate convincingly that the self-assembly centers dealing with interactions of knob "A": hole "a" are not involved in oxidative modification. It is concluded that the numerous oxidative sites revealed are mainly responsible for inhibiting lateral aggregation of protofibrils. The part of amino acid residues subjected to oxidation is supposed to carry out the antioxidant function.
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Registered trials
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