ArticleChembiochem : a European journal of chemical biology2017
Irreversible Protein Labeling by Paal-Knorr Conjugation.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Controlling Residual Protein Impurities in Active Pharmaceutical Ingredients (APIs) by Derivative Size-Exclusion High-Performance Liquid Chromatography (SEC-HPLC).AAPS PharmSciTech · 2026Article
- Multiphoton lithography with protein photoresists.Materials today. Bio · 2024Article
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- Article
- A Paal-Knorr agent for chemoproteomic profiling of targets of isoketals in cells.Chemical science · 2021Article
- Hydrolysis of 5-methylfuran-2-yl to 2,5-dioxopentanyl allows for stable bio-orthogonal proximity-induced ligation.Communications chemistry · 2021Article
- A fluorescent target-guided Paal-Knorr reaction.RSC advances · 2020Article
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Authors and funding
3 authors.
Funding
Abstract
The application of new chemical reactions in a biological context has advanced bioconjugation methods for both fundamental research and commercial arenas. Recent adaptations of reactions such as Huisgen 1,3-dipolar or Diels-Alder cycloadditions have enabled the labeling of specific residues in biomolecules by the attachment of molecules carrying azides, alkynes, or strained alkenes. Although these are fundamental tools, there is a need for the discovery of reactions that can label native proteins. We report herein the adaptation of the Paal-Knorr reaction to label lysine residues in proteins via pyrrole linkages.
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