ArticleOrganic & biomolecular chemistry2016
Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions.
Article in Organic & biomolecular chemistry, 2016. 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, 7 citations in OpenAlex.
- Tyrosine bioconjugation - an emergent alternative.Organic & biomolecular chemistry · 2020Review
- DNA-Catalyzed Introduction of Azide at Tyrosine for Peptide Modification.Angewandte Chemie (International ed. in English) · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We evaluate the ability of hexahistidine (His6) tags on peptide and protein substrates to recruit deoxyribozymes for modifying those substrates. For two different deoxyribozymes, one that creates tyrosine-RNA nucleopeptides and another that phosphorylates tyrosine side chains, we find substantial improvements in yield, kobs, and Km for peptide substrates due to recruiting by His6/Cu(2+). However, the recruiting benefits of the histidine tag are not observed for larger protein substrates, likely because the tested deoxyribozymes either cannot access the target peptide segments or cannot function when these segments are presented in a structured protein context.
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Registered trials
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