ArticleStructure (London, England : 1993)2009
A structural explanation for the antithrombotic activity of ARC1172, a DNA aptamer that binds von Willebrand factor domain A1.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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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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Who cites it
49 citing papers in PubMed, 90 citations in OpenAlex.
- Novel therapies for von Willebrand disease.Blood advances · 2026Review
- Von Willebrand Factor as a Therapeutic Target in Thrombotic Disorders.Thrombosis and haemostasis · 2026Review
- From randomness to recognition: modeling the evolution of DNA sequence information during enrichment for binding.Bioinformatics advances · 2026Article
- Predicting Single-Stranded DNA Oligonucleotides 3D Structures: An Open Issue.Computational and structural biotechnology journal · 2026Article
- Vorticity-Facilitated Platelet Aggregation: a High Expansion-Ratio Stenotic Microfluidic Platform Unravels the Role of Complex Flow Dynamics in Arterial Thrombosis.Advanced healthcare materials · 2025Article
- Direct Modeling of DNA and RNA Aptamers with AlphaFold 3: A Promising Tool for Predicting Aptamer Structures and Aptamer-Target Interactions.ACS synthetic biology · 2025Article
- 3D structure and stability prediction of DNA with multi-way junctions in ionic solutions.PLoS computational biology · 2025Article
- Review
- Recent Advances in Aptamers-Based Nanosystems for Diagnosis and Therapy of Cardiovascular Diseases: An Updated Review.International journal of nanomedicine · 2025Review
- The prospective approach for aptamers applied in the treatment and molecular diagnostics of ischemic stroke.Frontiers in pharmacology · 2025Review
- Conformation-specific RNA aptamers for phenotypic distinction between normal von Willebrand factor and type 2B von Willebrand disease.NAR molecular medicine · 2024Article
- Conformational activation and inhibition of von Willebrand factor by targeting its autoinhibitory module.Blood · 2024Article
- Structural Insights into Protein-Aptamer Recognitions Emerged from Experimental and Computational Studies.International journal of molecular sciences · 2023Review
- Success probability of high-affinity DNA aptamer generation by genetic alphabet expansion.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Single-molecule imaging of von Willebrand factor reveals tension-dependent self-association.Blood · 2021Article
- Von Willebrand factor: A key glycoprotein involved in thrombo-inflammatory complications of COVID-19.Chemico-biological interactions · 2021Review
- Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module.Nature communications · 2021Article
- Structural Biology for the Molecular Insight between Aptamers and Target Proteins.International journal of molecular sciences · 2021Review
- A new drug for an old concept: aptamer to von Willebrand factor for prevention of arterial and microvascular thrombosis.Haematologica · 2020Article
- Factors Affecting the Formation and Treatment of Thrombosis by Natural and Synthetic Compounds.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
ARC1172 is a 41-mer DNA aptamer selected to bind the A1 domain of von Willebrand factor (VWF). A derivative of ARC1172 with modifications to increase intravascular survival inhibits carotid artery thrombosis in a Cynomolgus macaque model and inhibits VWF-dependent platelet aggregation in humans, suggesting that such aptamers may be useful to prevent or treat thrombosis. In the crystal structure of a VWF A1-ARC1172 complex, the aptamer adopts a three-stem structure of mainly B-form DNA with three noncanonical base pairs and 9 unpaired residues, 6 of which are stabilized by base-base or base-deoxyribose stacking interactions. The aptamer-protein interface is characterized by cation-pi interactions involving Arg, Lys, and Gln residues, often stabilized by H-bonds with adjacent bases. The ARC1172 binding site on the A1 domain overlaps with that of botrocetin and clashes with glycoprotein Ibalpha binding at an adjacent site, which accounts for the antithrombotic activity of ARC1172 and related aptamers.
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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.