An E2-ubiquitin thioester-driven approach to identify substrates modified with ubiquitin and ubiquitin-like molecules
Ubiquitination and ubiquitin-like modifications of proteins regulate multiple cellular processes but identifying substrates of specific E2 and E3 enzymes remains challenging. Here, the authors conjugate E2 enzymes with enrichable ubiquitin derivatives to identify substrates of specific E2/E3 pairs b...
Guardado en:
Autores principales: | Gábor Bakos, Lu Yu, Igor A. Gak, Theodoros I. Roumeliotis, Dimitris Liakopoulos, Jyoti S. Choudhary, Jörg Mansfeld |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/2f933e1692cc471fbb02a4f43cc71f65 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Orthogonal ubiquitin transfer identifies ubiquitination substrates under differential control by the two ubiquitin activating enzymes
por: Xianpeng Liu, et al.
Publicado: (2017) -
Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification
por: Lingmin Yuan, et al.
Publicado: (2021) -
Rpn11-mediated ubiquitin processing in an ancestral archaeal ubiquitination system
por: Adrian C. D. Fuchs, et al.
Publicado: (2018) -
The ubiquitin-like modifier FAT10 interferes with SUMO activation
por: Annette Aichem, et al.
Publicado: (2019) -
Identifying the ubiquitination targets of E6AP by orthogonal ubiquitin transfer
por: Yiyang Wang, et al.
Publicado: (2017)