Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding
Protein S-sulfenylation is a posttranslational modification that can act as a sensor of redox oxidative stress. Here the authors show that, following mechanical unfolding, sulfenic acid drives disulfide bond reformation and guides non-enzymatic oxidative folding.
Guardado en:
Autores principales: | Amy E. M. Beedle, Steven Lynham, Sergi Garcia-Manyes |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2016
|
Materias: | |
Acceso en línea: | https://doaj.org/article/15bb57049a77463cbe99c276049de68e |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Tailoring protein nanomechanics with chemical reactivity
por: Amy E. M. Beedle, et al.
Publicado: (2017) -
Direct cysteine sulfenylation drives activation of the Src kinase
por: David E. Heppner, et al.
Publicado: (2018) -
SVM-SulfoSite: A support vector machine based predictor for sulfenylation sites
por: Hussam J. AL-barakati, et al.
Publicado: (2018) -
Forcing the reversibility of a mechanochemical reaction
por: Amy E. M. Beedle, et al.
Publicado: (2018) -
Machine learning differentiates enzymatic and non-enzymatic metals in proteins
por: Ryan Feehan, et al.
Publicado: (2021)