ArticleFEBS open bio2018
Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.
Article in FEBS open bio, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 4 citations in OpenAlex.
- Specific inhibition of FGF5-induced cell proliferation by RNA aptamers.Scientific reports · 2021Article
- Nucleic Acid Aptamer: A Novel Potential Diagnostic and Therapeutic Tool for Leukemia.OncoTargets and therapy · 2019Review
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Authors and funding
10 authors at 8 institutions in 1 country.
Funding
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Abstract
Since the invention of systematic evolution of ligands by exponential enrichment, many short oligonucleotides (or aptamers) have been reported that can bind to a wide range of target molecules with high affinity and specificity. Previously, we reported an RNA aptamer that shows high affinity to the Runt domain (RD) of the AML1 protein, a transcription factor with roles in haematopoiesis and immune function. From kinetic and thermodynamic studies, it was suggested that the aptamer recognises a large surface area of the RD, using numerous weak interactions. In this study, we identified the secondary structure by nuclear magnetic resonance spectroscopy and performed a mutational study to reveal the residue critical for binding to the RD. It was suggested that the large contact area was formed by a DNA-mimicking motif and a multibranched loop, which confers the high affinity and specificity of binding.
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