Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing cond...
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| Auteurs principaux: | , , , , , , , , , , |
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| Format: | article |
| Langue: | EN |
| Publié: |
Nature Portfolio
2016
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| Sujets: | |
| Accès en ligne: | https://doaj.org/article/b48cef68f3dc4e9fa4b70b0add885ae3 |
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| Résumé: | Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing conditions. |
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