ArticleJournal of the American Chemical Society2017
Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 69 citations in OpenAlex.
- TagC-RED: An Infrared-Triggered Retro-Ene Reaction for Deep-Tissue Bioconjugation.Journal of the American Chemical Society · 2026Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Manganese-Catalyzed Electrochemical Diazidation of Dehydroalanine Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Seleno-relaxin analogues: effect of internal and external diselenide bonds on the foldability and a fibrosis-related factor of endometriotic stromal cells.RSC chemical biology · 2024Article
- Efficient Segmental Isotope Labeling of Integral Membrane Proteins for High-Resolution NMR Studies.Journal of the American Chemical Society · 2024Article
- Selenium chemistry for spatio-selective peptide and protein functionalization.Nature reviews. Chemistry · 2024Review
- The semisynthesis of nucleolar human selenoprotein H.Chemical science · 2023Article
- Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine.Nature communications · 2022Article
- Semisynthesis of Homogeneous, Active Granulocyte Colony-Stimulating Factor Glycoforms.Angewandte Chemie (International ed. in English) · 2022Article
- Expressed Protein Selenoester Ligation.Angewandte Chemie (International ed. in English) · 2022Article
- Expressed Protein Selenoester Ligation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Using selenocysteine-specific reporters to screen for efficient tRNAMethods in enzymology · 2022Article
- Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S.Methods in enzymology · 2022Article
- Compensatory Protection of Thioredoxin-Deficient Cells from Etoposide-Induced Cell Death by Selenoprotein W via Interaction with 14-3-3.International journal of molecular sciences · 2021Article
- Site-Selective Modification of Peptides and Proteins via Interception of Free-Radical-Mediated Dechalcogenation.Angewandte Chemie (International ed. in English) · 2020Article
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020Article
- Article
- From Synthesis to Characterization of Site-Selective PEGylated Proteins.Frontiers in pharmacology · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Employing selenocysteine-containing protein fragments to form the amide bond between respective protein fragments significantly extends the current capabilities of the widely used protein engineering method, expressed protein ligation. Selenocysteine-mediated ligation is noteworthy for its high yield and efficiency. However, it has so far been restricted to solid-phase synthesized seleno-peptides and thus constrained by where the selenocysteine can be positioned. Here we employ heterologously expressed seleno-fragments to overcome the placement and size restrictions in selenocysteine-mediated chemical ligation. Following ligation, the selenocysteine can be deselenized into an alanine or serine, resulting in nonselenoproteins. This greatly extends the flexibility in selecting the conjugation site in expressed protein ligations with no influence on native cysteines. Furthermore, the selenocysteine can be used to selectively introduce site-specific protein modifications. Therefore, selenocysteine-mediated expressed protein ligation simplifies incorporation of post-translational modifications into the protein scaffold.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.