Cargando…
Traceless and Site-Specific Ubiquitination of Recombinant Proteins
[Image: see text] Protein ubiquitination is a post-translational modification that regulates almost all aspects of eukaryotic biology. Here we discover the first routes for the efficient site-specific incorporation of δ-thiol-l-lysine (7) and δ-hydroxy-l-lysine (8) into recombinant proteins, via evo...
Autores principales: | Virdee, Satpal, Kapadnis, Prashant B., Elliott, Thomas, Lang, Kathrin, Madrzak, Julia, Nguyen, Duy P., Riechmann, Lutz, Chin, Jason W. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2011
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3135006/ https://www.ncbi.nlm.nih.gov/pubmed/21710965 http://dx.doi.org/10.1021/ja202799r |
Ejemplares similares
-
Genetically Directed Production of Recombinant, Isosteric and Nonhydrolysable Ubiquitin Conjugates
por: Stanley, Mathew, et al.
Publicado: (2016) -
Traceless enzymatic protein synthesis without ligation sites constraint
por: Li, Ruifeng, et al.
Publicado: (2021) -
An atypical ubiquitin ligase at the heart of neural development and programmed axon degeneration
por: Virdee, Satpal
Publicado: (2022) -
Chemical ubiquitination for decrypting a cellular
code
por: Stanley, Mathew, et al.
Publicado: (2016) -
An Ankyrin-repeat ubiquitin binding domain determines TRABID’s specificity for atypical ubiquitin chains
por: Licchesi, Julien D.F., et al.
Publicado: (2011)