ArticleJournal of the American Chemical Society2010
Design of single-stranded nucleic acid binding peptides based on nucleocapsid CCHC-box zinc-binding domains.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 5 citations in OpenAlex.
- Characterization of a male specific region containing a candidate sex determining gene in Atlantic cod.Scientific reports · 2019Article
- Mechanisms of Lin28-mediated miRNA and mRNA regulation--a structural and functional perspective.International journal of molecular sciences · 2013Review
- Engineering RNA-binding proteins for biology.The FEBS journal · 2013Review
- The prospects for designer single-stranded RNA-binding proteins.Nature structural & molecular biology · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The solution structures of nucleocapsid (NC)-like CCHC zinc-binding domains bound to nucleic acid targets have revealed that these domains bind guanosine residues within single-stranded nucleic acids. Here, we have performed initial studies examining the potential use of NC-like CCHC zinc-binding domains as modules to construct single-stranded nucleic acid binding peptides. The affinity for guanosine-containing single-stranded deoxyribooligonucleotides increases with the number of CCHC domains in the peptide. The length of the linker between domains affects the spacing of guanosine residues in oligonucleotides that are preferentially bound. These studies provide a proof of principle that NC-like CCHC zinc-binding domains can be utilized as a basis for designing peptides that bind specific single-stranded nucleic acid sequences.
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Registered trials
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