ArticleBiochemistry and biophysics reports2017
Peptide oligomers from ultra-short peptides using sortase.
Article in Biochemistry and biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 14 citations in OpenAlex.
- Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry.Journal of the American Chemical Society · 2025Article
- Production of constrained L-cyclo-tetrapeptides by epimerization-resistant direct aminolysis.Nature communications · 2024Article
- Broadening the scope of sortagging.RSC advances · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sortase A catalyzed ligation of ultra-short peptides leads to inter/intra-molecular transpeptidation to form either linear or cyclic oligomers dependent upon the peptide length. Cyclic peptides were the main products for peptides with more than 15aa. However, for ultra-short (<15aa) peptides, cyclic oligomers became predominant in prolonged reactions. Peptides with 1-3 aminoglycines were equally active but peptide oligomers from peptide containing more than one aminoglycine were prone to hydrolysis.
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Registered trials
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