Title : Dysregulated Redox Regulation Contributes to Nuclear EGFR Localization and Pathogenicity in Lung Cancer.

Pub. Date : 2019 Mar 19

PMID : 30890751






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 These various outcomes could also be attenuated by silencing of glutathione S-transferase P1 (GSTP1), a mediator of metabolic alterations and drug resistance in various cancers, and a regulator of cysteine oxidation. Cysteine glutathione S-transferase pi 1 Homo sapiens
2 These various outcomes could also be attenuated by silencing of glutathione S-transferase P1 (GSTP1), a mediator of metabolic alterations and drug resistance in various cancers, and a regulator of cysteine oxidation. Cysteine glutathione S-transferase pi 1 Homo sapiens
3 Collectively, our findings indicate DUOX1 deficiency in lung cancers promotes dysregulated EGFR signaling and enhanced GSTP1-mediated turnover of EGFR cysteine oxidation, which result in enhanced nuclear EGFR localization and tumorigenic properties. Cysteine glutathione S-transferase pi 1 Homo sapiens