Cargando…
Copper Sources for Sod1 Activation
Copper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radica...
Autores principales: | Boyd, Stefanie D., Ullrich, Morgan S., Skopp, Amelie, Winkler, Duane D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7346115/ https://www.ncbi.nlm.nih.gov/pubmed/32517371 http://dx.doi.org/10.3390/antiox9060500 |
Ejemplares similares
-
Copper–zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1
por: Skopp, Amélie, et al.
Publicado: (2019) -
Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs)
por: Boyd, Stefanie D., et al.
Publicado: (2020) -
Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1)
por: Boyd, Stefanie D, et al.
Publicado: (2018) -
Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations
por: Tokuda, Eiichi, et al.
Publicado: (2016) -
“The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-R(1), for the Active Cry1Ab Toxin of Bacillus thuringiensis”
por: Liu, Li, et al.
Publicado: (2018)