Cargando…
Introduction of a More Glutaredoxin-like Active Site to PDI Results in Competition between Protein Substrate and Glutathione Binding
Proteins in the thioredoxin superfamily share a similar fold, contain a -CXXC- active site, and catalyze oxidoreductase reactions by dithiol-disulfide exchange mechanisms. Protein disulfide isomerase (PDI) has two -CGHC- active sites. For in vitro studies, oxidation/reduction of PDI during the catal...
Autores principales: | Saaranen, Mirva J., Alanen, Heli I., Salo, Kirsi E. H., Nji, Emmanuel, Kärkkäinen, Pekka, Schmotz, Constanze, Ruddock, Lloyd W. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9598436/ https://www.ncbi.nlm.nih.gov/pubmed/36290643 http://dx.doi.org/10.3390/antiox11101920 |
Ejemplares similares
-
Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease
por: Biterova, Ekaterina, et al.
Publicado: (2018) -
A molecular specificity code for the three mammalian KDEL receptors
por: Raykhel, Irina, et al.
Publicado: (2008) -
A molecular specificity code for the three mammalian KDEL receptors
por: Raykhel, Irina, et al.
Publicado: (2007) -
Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding
por: Moilanen, Antti, et al.
Publicado: (2018) -
Modulation of glutaredoxin in the lung and sputum of cigarette smokers and chronic obstructive pulmonary disease
por: Peltoniemi, Mirva J, et al.
Publicado: (2006)