ArticleMethods in molecular biology (Clifton, N.J.)2016
Crystallographic Pursuit of a Protein-RNA Aptamer Complex.
Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed, 9 citations in OpenAlex.
- Conformationally selective RNA aptamers allosterically modulate the β2-adrenoceptor.Nature chemical biology · 2016Article
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1 author at 1 institution in 1 country.
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Abstract
Only a few of the aptamers designed to selectively target proteins have been structurally characterized, such as those that target thrombin, von Willebrand factor, Plasmodium falciparum lactate dehydrogenase, interleukin 6, and platelet-derived growth factor B. Most of these aptamers are composed of DNA and were designed as therapeutics/diagnostics for targets found in human plasma. Recently, the crystal structure of a complex between an RNA aptamer and an intracellular target, G protein-coupled receptor kinase 2, was determined. Herein is described the overall approach used to isolate crystals that would allow the identification of the key interactions between aptamer and kinase. These strategies may be useful in structural characterization of other SELEX-generated RNA aptamer complexes.
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Registered trials
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