Cargando…
S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions
Correct protein folding and inhibition of protein aggregation is facilitated by a cellular “quality control system” that engages a network of protein interactions including molecular chaperones and the ubiquitin proteasome system. Key chaperones involved in these regulatory mechanisms are the protei...
Autores principales: | Conway, Myra E., Harris, Matthew |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4399332/ https://www.ncbi.nlm.nih.gov/pubmed/25932462 http://dx.doi.org/10.3389/fchem.2015.00027 |
Ejemplares similares
-
The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration
por: Perri, Emma R., et al.
Publicado: (2016) -
Thioredoxin-interacting protein regulates protein disulfide isomerases and
endoplasmic reticulum stress
por: Lee, Samuel, et al.
Publicado: (2014) -
Protein disulfide isomerase a multifunctional protein with multiple physiological roles
por: Ali Khan, Hyder, et al.
Publicado: (2014) -
SOD1 aggregation in astrocytes following ischemia/reperfusion injury: a role of NO-mediated S-nitrosylation of protein disulfide isomerase (PDI)
por: Chen, Xueping, et al.
Publicado: (2012) -
Methods of measuring protein disulfide isomerase activity: a critical overview
por: Watanabe, Monica M., et al.
Publicado: (2014)