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Aromatic thiol-mediated cleavage of N–O bonds enables chemical ubiquitylation of folded proteins
Access to protein substrates homogenously modified by ubiquitin (Ub) is critical for biophysical and biochemical investigations aimed at deconvoluting the myriad biological roles for Ub. Current chemical strategies for protein ubiquitylation, however, employ temporary ligation auxiliaries that are r...
| Autores principales: | , , , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Nature Publishing Group
2016
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5056422/ https://www.ncbi.nlm.nih.gov/pubmed/27680493 http://dx.doi.org/10.1038/ncomms12979 |