ArticleScientific reports2019
RGD-independent binding of Russell's Viper venom Kunitz-type protease inhibitors to platelet GPIIb/IIIa receptor.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 14 citations in OpenAlex.
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Structural, Biochemical Characterization and Molecular Mechanism of Cerastokunin: A New Kunitz-Type Peptide with Potential Inhibition of Thrombin, Factor Xa and Platelets.The protein journal · 2024Article
- Unravelling Surface Modification Strategies for Preventing Medical Device-Induced Thrombosis.Advanced healthcare materials · 2024Review
- State-of-the-art review - A review on snake venom-derived antithrombotics: Potential therapeutics for COVID-19-associated thrombosis?International journal of biological macromolecules · 2021Review
- Evolutionary Aspects of the Structural Convergence and Functional Diversification of Kunitz-Domain Inhibitors.Journal of molecular evolution · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study elucidates the platelet-modulating properties of two snake venom Kunitz-type serine protease inhibitors, Rusvikunin and Rusvikunin-II, from Russell's Viper venom, their native and reconstituted complexes, and two synthetic custom peptides (developed from the platelet-binding region of Rusvikunin-II) against mammalian platelet-rich plasma (PRP) and washed platelets. The Rusvikunins and their complexes demonstrated concentration-dependent deaggregation and aggregation of washed platelets independent of von Willebrand factor and/or fibrinogen requirement. At lower concentrations they abolished collagen and ADP-induced platelet aggregation, but at higher concentrations, they progressively decreased the inhibition of ADP-induced aggregation and potentiated the effect of collagen on PRP. Rusvikunin complex/Rusvikunin-II bound to and induced RGD-independent aggregation of α-chymotrypsin-treated platelets. Molecular docking studies suggested interaction of Rusvikunin-II and custom peptides with platelet GPIIb/IIIa receptor, which was validated by spectrofluorometry analysis and ELISA. This study reports, for the first time, an RGD-independent binding of a snake venom component to the platelet GPIIb/IIIa receptor.
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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.