Cargando…
Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically. They are important for the regulation of the fu...
Autores principales: | Kalinina, Elena, Novichkova, Maria |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7838997/ https://www.ncbi.nlm.nih.gov/pubmed/33467703 http://dx.doi.org/10.3390/molecules26020435 |
Ejemplares similares
-
The Role of S-Nitrosylation and S-Glutathionylation of Protein Disulphide Isomerase in Protein Misfolding and Neurodegeneration
por: Halloran, M., et al.
Publicado: (2013) -
S-Glutathionylation and S-Nitrosylation in Mitochondria: Focus on Homeostasis and Neurodegenerative Diseases
por: Vrettou, Sofia, et al.
Publicado: (2022) -
Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites
por: Müller-Schüssele, Stefanie J., et al.
Publicado: (2021) -
Redox regulation of the proteasome via S-glutathionylation()
por: Demasi, Marilene, et al.
Publicado: (2013) -
Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease
por: Musaogullari, Aysenur, et al.
Publicado: (2020)