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...

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Detalles Bibliográficos
Autores principales: Weller, Caroline E., Dhall, Abhinav, Ding, Feizhi, Linares, Edlaine, Whedon, Samuel D., Senger, Nicholas A., Tyson, Elizabeth L., Bagert, John D., Li, Xiaosong, Augusto, Ohara, Chatterjee, Champak
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Article
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

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5056422/
https://www.ncbi.nlm.nih.gov/pubmed/27680493
http://dx.doi.org/10.1038/ncomms12979

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