ArticleNature chemistry2017
Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors.
Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 91 citations in OpenAlex.
- Discovery of a Reversible Sub-Picomolar Thrombin Inhibitor Using DCC.Angewandte Chemie (International ed. in English) · 2026Article
- Direct mapping of tyrosine sulfation states in native peptides by nanopore.Nature chemical biology · 2025Article
- Development of supramolecular anticoagulants with on-demand reversibility.Nature biotechnology · 2025Article
- Whole Genome Sequencing Reveals Clade-Specific Genetic Variation in Blacklegged Ticks.Ecology and evolution · 2025Article
- Inhibition of Cancer Cell Migration and Invasion In Vitro by Recombinant Tyrosine-Sulfated Haemathrin, A Thrombin Inhibitor.International journal of molecular sciences · 2024Article
- Inhibitory effect of recombinant tyrosine‑sulfated madanin‑1, a thrombin inhibitor, on the behavior of MDA‑MB‑231 and SKOV3 cellsMolecular medicine reports · 2024Article
- Harmony of Protein Tags and Chimeric Molecules Empowers Targeted Protein Ubiquitination and Beyond.Cells · 2024Review
- Recombinant neorudin and its active metabolite hirudin: the fateFrontiers in pharmacology · 2024Article
- Engineering sulfonate group donor regeneration systems to boost biosynthesis of sulfated compounds.Nature communications · 2023Article
- Prospection of Peptide Inhibitors of Thrombin from Diverse Origins Using a Machine Learning Pipeline.Bioengineering (Basel, Switzerland) · 2023Article
- Histone tyrosine sulfation by SULT1B1 regulates H4R3me2a and gene transcription.Nature chemical biology · 2023Article
- Designing Smaller, Synthetic, Functional Mimetics of Sulfated Glycosaminoglycans as Allosteric Modulators of Coagulation Factors.Journal of medicinal chemistry · 2023Review
- A draft of the genome of the Gulf Coast tick, Amblyomma maculatum.Ticks and tick-borne diseases · 2023Article
- Purification and characterization of thrombin from camel plasma: interaction with camel tick salivary gland thrombin inhibitor.Journal, genetic engineering & biotechnology · 2023Article
- Site-Specific Incorporation of Sulfotyrosine into Proteins in Mammalian Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Unleashing the potential of noncanonical amino acid biosynthesis to create cells with precision tyrosine sulfation.Nature communications · 2022Article
- Plant immunity: Rice XA21-mediated resistance to bacterial infection.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Current Advances in Aptamer-based Biomolecular Recognition and Biological Process Regulation.Chemical research in Chinese universities · 2022Review
- Potential Mechanisms of Transmission of Tick-Borne Viruses at the Virus-Tick Interface.Frontiers in microbiology · 2022Review
- Improving treatment for acute ischemic stroke-Clot busting innovation in the pipeline.Frontiers in medical technology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Madanin-1 and chimadanin are two small cysteine-free thrombin inhibitors that facilitate blood feeding in the tick Haemaphysalis longicornis. Here, we report a post-translational modification-tyrosine sulfation-of these two proteins that is critical for potent anti-thrombotic and anticoagulant activity. Inhibitors produced in baculovirus-infected insect cells displayed heterogeneous sulfation of two tyrosine residues within each of the proteins. One-pot ligation-desulfurization chemistry enabled access to homogeneous samples of all possible sulfated variants of the proteins. Tyrosine sulfation of madanin-1 and chimadanin proved crucial for thrombin inhibitory activity, with the doubly sulfated variants three orders of magnitude more potent than the unmodified inhibitors. The three-dimensional structure of madanin-1 in complex with thrombin revealed a unique mode of inhibition, with the sulfated tyrosine residues binding to the basic exosite II of the protease. The importance of tyrosine sulfation within this family of thrombin inhibitors, together with their unique binding mode, paves the way for the development of anti-thrombotic drug leads based on these privileged scaffolds.
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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.