ArticleChemical science2024
Rapid flow-based synthesis of post-translationally modified peptides and proteins: a case study on MYC's transactivation domain.
Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Pharmacological targeting of oncogenic condensates in cancer: mechanistic insights and therapeutic opportunities.Acta pharmacologica Sinica · 2026Review
- Stirring glycopeptides away from the constraints of solid-phase synthesis misconceptions.Frontiers in molecular biosciences · 2026Article
- Aspartimide Formation and Its Prevention in Fmoc Chemistry Solid Phase Peptide Synthesis.Chembiochem : a European journal of chemical biology · 2025Review
- A Versatile "Synthesis Tag" (SynTag) for the Chemical Synthesis of Aggregating Peptides and Proteins.Journal of the American Chemical Society · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein interactions of c-Myc (MYC) are often regulated by post-translational modifications (PTMs), such as phosphorylation, and crosstalk thereof. Studying these interactions requires proteins with unique PTM patterns, which are challenging to obtain by recombinant methods. Standard peptide synthesis and native chemical ligation can produce such modified proteins, but are time-consuming and therefore typically limited to the study of individual PTMs. Herein, we report the development of flow-based methods for the rapid synthesis of phosphorylated MYC sequences (up to 84 AA), and demonstrate the versatility of this approach for the incorporation of other PTMs (
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