Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR). The mechanisms of disulfide bond formation have mainly been studied...

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Detalles Bibliográficos
Autores principales: Palma, Arianna, Rettenbacher, Lukas A., Moilanen, Antti, Saaranen, Mirva, Pacheco-Martinez, Christian, Gasser, Brigitte, Ruddock, Lloyd
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10471769/
https://www.ncbi.nlm.nih.gov/pubmed/37652992
http://dx.doi.org/10.1038/s41598-023-41375-z

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10471769/
https://www.ncbi.nlm.nih.gov/pubmed/37652992
http://dx.doi.org/10.1038/s41598-023-41375-z

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