Cargando…
Identification of Natural Product Sulfuretin Derivatives as Inhibitors for the Endoplasmic Reticulum Redox Protein ERO1α
[Image: see text] The flavin adenine dinucleotide containing endoplasmic reticulum oxidoreductase-1 α (ERO1α) catalyzes the de novo disulfide bond formation of secretory and transmembrane proteins and contributes toward proper protein folding. Recently, increased ERO1α expression has been shown to c...
Autores principales: | Johnson, Brennan D., Kaulagari, Sridhar Reddy, Chen, Wei-Chih, Hayes, Karen, Geldenhuys, Werner J., Hazlehurst, Lori A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9312093/ https://www.ncbi.nlm.nih.gov/pubmed/35892127 http://dx.doi.org/10.1021/acsbiomedchemau.1c00062 |
Ejemplares similares
-
The Role of ERO1α in Modulating Cancer Progression and Immune Escape
por: Johnson, Brennan D., et al.
Publicado: (2020) -
Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
por: Benham, Adam M., et al.
Publicado: (2013) -
The Hypothermic Influence on CHOP and Ero1-α in an Endoplasmic Reticulum Stress Model of Cerebral Ischemia
por: Poone, Gagandip K., et al.
Publicado: (2015) -
Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases
por: Araki, Kazutaka, et al.
Publicado: (2013) -
Overexpression of Endoplasmic Reticulum Oxidoreductin 1-α (ERO1L) Is Associated with Poor Prognosis of Gastric Cancer
por: Seol, So-Young, et al.
Publicado: (2016)