Cargando…
Usa1 Protein Facilitates Substrate Ubiquitylation through Two Separate Domains
BACKGROUND: Defects in protein folding are recognized as the root of many neurodegenerative disorders. In the endoplasmic reticulum (ER), secretory proteins are subjected to a stringent quality control process to eliminate misfolded proteins by the ER-associated degradation (ERAD) pathway. A novel E...
Autores principales: | Kim, Ikjin, Li, Yue, Muniz, Paulina, Rao, Hai |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764048/ https://www.ncbi.nlm.nih.gov/pubmed/19898607 http://dx.doi.org/10.1371/journal.pone.0007604 |
Ejemplares similares
-
Poxviral ANKR/F-box Proteins: Substrate Adapters for Ubiquitylation and More
por: Ingham, Robert J., et al.
Publicado: (2022) -
Ubiquitylation Extends to Lipid Substrate for Restricting Bacterial Infection
por: Wang, Chaofeng, et al.
Publicado: (2021) -
Protein Ubiquitylation in Pancreatic Cancer
por: Bonacci, Thomas, et al.
Publicado: (2010) -
Rad4 Regulates Protein Turnover at a Postubiquitylation Step
por: Li, Yue, et al.
Publicado: (2010) -
Parkin recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MITOL
por: Koyano, Fumika, et al.
Publicado: (2019)