ArticleNature communications2017
Structural basis for IL-1α recognition by a modified DNA aptamer that specifically inhibits IL-1α signaling.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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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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
30 citing papers in PubMed, 65 citations in OpenAlex.
- Overcoming sensitivity limitations in lateral flow immunoassays for small-molecule detection: from tracer engineering to assay format innovation.Analytical and bioanalytical chemistry · 2026Review
- Expedient single-round selection of hyper-modified aptamer targeting insulin receptor from over-represented dually nucleobase-modified DNA libraries.Nature communications · 2026Article
- Divalent aptamer-mediated clustering for extracellular vesicle separation.Communications biology · 2026Article
- Probing three-dimensional cyclooctatetraene for nucleobase modification in aptamer selection.Communications chemistry · 2025Article
- Nucleic acid aptamers in orthopedic diseases: promising therapeutic agents for bone disorders.Bone research · 2025Review
- Aptamers as a New Frontier in Molecular Cancer Imaging Technologies.Chemical & biomedical imaging · 2025Review
- Innovative Applications of Nucleic Acid Aptamers in Colorectal Cancer Diagnosis and Therapy: From Selection Optimization to Clinical Translation.International journal of nanomedicine · 2025Review
- Crossing the Halfway Point: Aptamer-Based, Highly Multiplexed Assay for the Assessment of the Proteome.Journal of proteome research · 2024Review
- Aptamer-functionalized nanomaterials (AFNs) for therapeutic management of hepatocellular carcinoma.Journal of nanobiotechnology · 2024Review
- Structural Insights into Protein-Aptamer Recognitions Emerged from Experimental and Computational Studies.International journal of molecular sciences · 2023Review
- Advances in the mechanisms and applications of inhibitory oligodeoxynucleotides against immune-mediated inflammatory diseases.Frontiers in pharmacology · 2023Review
- AMIGOS III: pseudo-torsion angle visualization and motif-based structure comparison of nucleic acids.Bioinformatics (Oxford, England) · 2022Article
- Aptamers used for molecular imaging and theranostics - recent developments.Theranostics · 2022Review
- Advances in aptamers against Aβ and applications in Aβ detection and regulation for Alzheimer's disease.Theranostics · 2022Review
- Structural Biology for the Molecular Insight between Aptamers and Target Proteins.International journal of molecular sciences · 2021Review
- Base-modified aptamers obtained by cell-internalization SELEX facilitate cellular uptake of an antisense oligonucleotide.Molecular therapy. Nucleic acids · 2021Article
- Inhibition of the Complement Alternative Pathway by Chemically Modified DNA Aptamers That Bind with Picomolar Affinity to Factor B.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- SELEX-based DNA Aptamer Selection: A Perspective from the Advancement of Separation Techniques.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021Review
- Lysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function.Frontiers in cell and developmental biology · 2021Review
- Role for IL-1 Family Cytokines in Fungal Infections.Frontiers in microbiology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
IL-1α is an essential cytokine that contributes to inflammatory responses and is implicated in various forms of pathogenesis and cancer. Here we report a naphthyl modified DNA aptamer that specifically binds IL-1α and inhibits its signaling pathway. By solving the crystal structure of the IL-1α/aptamer, we provide a high-resolution structure of this critical cytokine and we reveal its functional interaction interface with high-affinity ligands. The non-helical aptamer, which represents a highly compact nucleic acid structure, contains a wealth of new conformational features, including an unknown form of G-quadruplex. The IL-1α/aptamer interface is composed of unusual polar and hydrophobic elements, along with an elaborate hydrogen bonding network that is mediated by sodium ion. IL-1α uses the same interface to interact with both the aptamer and its cognate receptor IL-1RI, thereby suggesting a novel route to immunomodulatory therapeutics.The cytokine interleukin 1α (IL-1α) plays an important role in inflammatory processes. Here the authors use SELEX to generate a modified DNA aptamer which specifically binds IL-1α, present the structure of the IL-1α/aptamer complex and show that this aptamer inhibits the IL-1α signaling pathway.
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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.