Cargando…
SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage
Copper-zinc superoxide dismutase (SOD1) has been proposed as one of the causative proteins of amyotrophic lateral sclerosis (ALS). The accumulation of non-native conformers, oligomers, and aggregates of SOD1 in motor neurons is considered responsible for this disease. However, it remains unclear whi...
Autores principales: | Yamazaki, Kosuke, Tahara, Shinya, Ohyama, Takumi, Kuroi, Kunisato, Nakabayashi, Takakazu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9273606/ https://www.ncbi.nlm.nih.gov/pubmed/35817830 http://dx.doi.org/10.1038/s41598-022-15701-w |
Ejemplares similares
-
Pro-Oxidant Activity of an ALS-Linked SOD1 Mutant in Zn-Deficient Form
por: Nagao, Chise, et al.
Publicado: (2020) -
Observation of liquid–liquid phase separation of ataxin-3 and quantitative evaluation of its concentration in a single droplet using Raman microscopy
por: Murakami, Kazuki, et al.
Publicado: (2021) -
Gallocin A, an Atypical Two-Peptide Bacteriocin with Intramolecular Disulfide Bonds Required for Activity
por: Proutière, Alexis, et al.
Publicado: (2023) -
Structure-activity relationships of the intramolecular disulfide bonds in coprisin, a defensin from the dung beetle
por: Lee, Jaeho, et al.
Publicado: (2014) -
Intramolecular Disulfide Bonds for Biogenesis of CALHM1 Ion Channel Are Dispensable for Voltage-Dependent Activation
por: Kwon, Jae Won, et al.
Publicado: (2021)