ArticlePloS one2015
Identification and Mechanistic Analysis of a Novel Tick-Derived Inhibitor of Thrombin.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 38 citations in OpenAlex.
- Skin Deep: Uncovering the Early Events of Crimean-Congo Hemorrhagic Fever Virus at the Tick-Host-Virus Interface.Viruses · 2026Review
- An Enabling Peptide Ligation Induced by Thiol-Salicylaldehyde Ester for Chemical Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Prospection of Peptide Inhibitors of Thrombin from Diverse Origins Using a Machine Learning Pipeline.Bioengineering (Basel, Switzerland) · 2023Article
- Comparative Analysis of Roots fromMolecules (Basel, Switzerland) · 2023Article
- Purification and characterization of thrombin from camel plasma: interaction with camel tick salivary gland thrombin inhibitor.Journal, genetic engineering & biotechnology · 2023Article
- Host Immune Responses to Salivary Components - A Critical Facet of Tick-Host Interactions.Frontiers in cellular and infection microbiology · 2022Review
- Article
- Tick host immunity: vector immunomodulation and acquired tick resistance.Trends in immunology · 2021Review
- Rapid assembly and profiling of an anticoagulant sulfoprotein library.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Deciphering Biological Processes at the Tick-Host Interface Opens New Strategies for Treatment of Human Diseases.Frontiers in physiology · 2019Review
- Chemical Equilibrium at the Tick-Host Feeding Interface:A Critical Examination of Biological Relevance in Hematophagous Behavior.Frontiers in physiology · 2019Review
- Article
- Serine Protease Inhibitors in Ticks: An Overview of Their Role in Tick Biology and Tick-Borne Pathogen Transmission.Frontiers in cellular and infection microbiology · 2017Review
- The Essential Role of Tick Salivary Glands and Saliva in Tick Feeding and Pathogen Transmission.Frontiers in cellular and infection microbiology · 2017Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
A group of peptides from the salivary gland of the tick Hyalomma marginatum rufipes, a vector of Crimean Congo hemorrhagic fever show weak similarity to the madanins, a group of thrombin-inhibitory peptides from a second tick species, Haemaphysalis longicornis. We have evaluated the anti-serine protease activity of one of these H. marginatum peptides that has been given the name hyalomin-1. Hyalomin-1 was found to be a selective inhibitor of thrombin, blocking coagulation of plasma and inhibiting S2238 hydrolysis in a competitive manner with an inhibition constant (Ki) of 12 nM at an ionic strength of 150 mM. It also blocks the thrombin-mediated activation of coagulation factor XI, thrombin-mediated platelet aggregation, and the activation of coagulation factor V by thrombin. Hyalomin-1 is cleaved at a canonical thrombin cleavage site but the cleaved products do not inhibit coagulation. However, the C-terminal cleavage product showed non-competitive inhibition of S2238 hydrolysis. A peptide combining the N-terminal parts of the molecule with the cleavage region did not interact strongly with thrombin, but a 24-residue fragment containing the cleavage region and the C-terminal fragment inhibited the enzyme in a competitive manner and also inhibited coagulation of plasma. These results suggest that the peptide acts by binding to the active site as well as exosite I or the autolysis loop of thrombin. Injection of 2.5 mg/kg of hyalomin-1 increased arterial occlusion time in a mouse model of thrombosis, suggesting this peptide could be a candidate for clinical use as an antithrombotic.
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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.