Cargando…
RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination
Attachment of ubiquitin (Ub) to proteins is one of the most abundant and versatile of all posttranslational modifications and affects outcomes in essentially all physiological processes. RING E3 ligases target E2 Ub-conjugating enzymes to the substrate, resulting in its ubiquitination. However, the...
Autores principales: | Kiss, Leo, Clift, Dean, Renner, Nadine, Neuhaus, David, James, Leo C. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7900206/ https://www.ncbi.nlm.nih.gov/pubmed/33619271 http://dx.doi.org/10.1038/s41467-021-21443-6 |
Ejemplares similares
-
Trim-Away ubiquitinates and degrades lysine-less and N-terminally acetylated substrates
por: Kiss, Leo, et al.
Publicado: (2023) -
A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
por: Kiss, Leo, et al.
Publicado: (2019) -
A lysine ring in HIV capsid pores coordinates IP6 to drive mature capsid assembly
por: Renner, Nadine, et al.
Publicado: (2021) -
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
por: Wang, Xiangyi S., et al.
Publicado: (2023) -
Administrative Arrangements for the Construction of the Intersecting Storage Rings
Publicado: (1965)