Cargando…
The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α
Disulfide formation in newly synthesized proteins entering the mammalian endoplasmic reticulum is catalyzed by protein disulfide isomerase (PDI), which is itself thought to be directly oxidized by Ero1α. The activity of Ero1α is tightly regulated by the formation of noncatalytic disulfides, which ne...
Autores principales: | Chambers, Joseph E., Tavender, Timothy J., Oka, Ojore B. V., Warwood, Stacey, Knight, David, Bulleid, Neil J. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2937950/ https://www.ncbi.nlm.nih.gov/pubmed/20657012 http://dx.doi.org/10.1074/jbc.M110.156596 |
Ejemplares similares
-
Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases
por: Shepherd, Colin, et al.
Publicado: (2014) -
Substrate Specificity of the Oxidoreductase ERp57 Is Determined Primarily
by Its Interaction with Calnexin and
Calreticulin
por: Jessop, Catherine E., et al.
Publicado: (2009) -
OTUB1 non-catalytically stabilizes the E2 ubiquitin-conjugating enzyme UBE2E1 by preventing its autoubiquitination
por: Pasupala, Nagesh, et al.
Publicado: (2018) -
A broad-spectrum antiviral molecule, QL47, selectively inhibits eukaryotic translation
por: de Wispelaere, Mélissanne, et al.
Publicado: (2020) -
Quantitative Cell-based Protein Degradation Assays to Identify and Classify Drugs That Target the Ubiquitin-Proteasome System
por: Chou, Tsui-Fen, et al.
Publicado: (2011)