Cargando…
Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis
Dissociation of superoxide dismutase 1 dimers is enhanced by glutathionylation, although the dissociation constants reported to date are imprecise. We have quantified the discreet dissociation constants for wild-type superoxide dismutase 1 and six naturally occurring sequence variants, in their unmo...
Autores principales: | McAlary, Luke, Yerbury, Justin J., Aquilina, J. Andrew |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834562/ https://www.ncbi.nlm.nih.gov/pubmed/24253732 http://dx.doi.org/10.1038/srep03275 |
Ejemplares similares
-
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
por: McAlary, Luke, et al.
Publicado: (2019) -
Corrigendum: Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
por: McAlary, Luke, et al.
Publicado: (2020) -
Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity
por: McAlary, Luke, et al.
Publicado: (2016) -
Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises
por: McAlary, Luke, et al.
Publicado: (2020) -
A copper chaperone–mimetic polytherapy for SOD1-associated amyotrophic lateral sclerosis
por: McAlary, L., et al.
Publicado: (2022)