Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
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Summary
It is shown that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents and incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.
- Type
- article
- Published
- 2001-12-18
- Cited by
- 839
- References
- 42
- Access
- Open access
- OpenAlex
- https://openalex.org/W2083541735
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:15934279
Keywords
Methionine, Biochemistry, Amino acid, Chemical ligation, Recombinant DNA
References
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- Probing Protein Structure and Function with an Expanded Genetic Code
Cited by
- Diels-Alder ligation of peptides and proteins.
- Protein engineering for directed immobilization.
- Tandem C-2 functionalization-intramolecular azide-alkyne 1,3-dipolar cycloaddition reaction: a convenient route to highly diversified 9H-benzo[b]pyrrolo[1,2-g][1,2,3]triazolo[1,5-d][1,4]diazepines.
- Evaluation of the Interaction between Phosphohistidine Analogues and Phosphotyrosine Binding Domains
- Self-assembly of synthetic and biological components in water using cucurbit[8]uril
- Designed ankyrin repeat proteins (DARPins) from research to therapy.
- New sphingolipid probes for metabolism and trafficking studies
- Chemical modification of viruses and virus-like particles.
- Ensemble fluorescence resonance energy transfer analysis of RNA polymerase clamp conformation
- Development and Application of Synthetic Lipid Probes to Study and Mimic Lipid Function
- Formation of ubiquitin dimers via azide-alkyne click reaction.
- Erweiterung des genetischen Codes von Candida albicans zur Analyse von Protein-Protein Interaktionen in vivo
- Chemoselective modification of viral proteins bearing metabolically introduced "clickable" amino acids and sugars.
- Bioorthogonal chemistry: implications for pretargeted nuclear (PET/SPECT) imaging and therapy.
- Multisite clickable modification of proteins using lipoic acid ligase.
- DNA Nanostructures as Programmable Biomolecular Scaffolds.
- The potential of bioorthogonal chemistry for correlative light and electron microscopy: a call to arms
- Gel-Free Proteomics
- Design and development of a site specific protein patterning technique for use in a microfluidic antibody separation device
- Streamlined Extract Preparation for E. coli-Based Cell-Free Protein Synthesis and Rapid Site-Specific Incorporation of Unnatural Amino Acids in Proteins
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