DsbA is a redox-switchable mechanical chaperone

DsbA is a ubiquitous bacterial oxidoreductase that associates with substrates during and after translocation, yet its involvement in protein folding and translocation remains an open question. Here we demonstrate a redox-controlled chaperone activity of DsbA, on both cysteine-containing and cysteine...

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Detalles Bibliográficos
Autores principales: Eckels, Edward C., Chaudhuri, Deep, Chakraborty, Soham, Echelman, Daniel J., Haldar, Shubhasis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8386657/
https://www.ncbi.nlm.nih.gov/pubmed/34522308
http://dx.doi.org/10.1039/d1sc03048e

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8386657/
https://www.ncbi.nlm.nih.gov/pubmed/34522308
http://dx.doi.org/10.1039/d1sc03048e

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