Enzymatic “Click” Ligation: Selective Cysteine Modification in Polypeptides Enabled by Promiscuous Glutathione S-Transferase
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Summary
Synthetic chemists have strived to develop a similar reaction toolkit with chemical orthogonality, selectivity and reactivity comparable to those of natural systems, but still face the difficulty of selectively differentiating between two chemically identical sites within a macromolecule.
- Type
- article
- Published
- 2013-11-01
- Cited by
- 55
- References
- 60
- OpenAlex
- https://openalex.org/W24222025
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:8624281
Keywords
Computer science
References
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- What makes an enzyme promiscuous?
Cited by
- Perfluorophenyl Derivatives as Unsymmetrical Linkers for Solid Phase Conjugation
- Development of new bioselective ligation reactions
- Convergent Diversity-Oriented Side-Chain Macrocyclization Scan for Unprotected Polypeptides
- Tunable heptamethine-azo dye conjugate as an NIR fluorescent probe for the selective detection of mitochondrial glutathione over cysteine and homocysteine.
- Click Chemistry in Complex Mixtures: Bioorthogonal Bioconjugation
- Plant GSTome: structure and functional role in xenome network and plant stress response.
- Externally stimulated click reactions for macromolecular syntheses
- Directed evolution of Tau class glutathione transferases reveals a site that regulates catalytic efficiency and masks co-operativity.
- Protein modification: Standing out from the crowd.
- π-Clamp Mediated Cysteine Conjugation
- Rapid biocompatible macrocyclization of peptides with decafluoro-diphenylsulfone
- The “Π-Clamp” Offers a Novel Strategy for Site-Selective Protein Modification
- Chemical Protein Modification through Cysteine
- Advances in chemical protein modification.
- Enzyme-Catalyzed Macrocyclization of Long Unprotected Peptides
- Fast and selective labeling of N-terminal cysteines at neutral pH via thiazolidino boronate formation
- In Vivo Site-Specific Protein Tagging with Diverse Amines Using an Engineered Sortase Variant.
- An Umpolung Approach for the Chemoselective Arylation of Selenocysteine in Unprotected Peptides
- Salt Effect Accelerates Site-Selective Cysteine Bioconjugation
- Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability.
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