Sort   by:  
 Page size 
The family of peroxiredoxins catalyzes the reduction of hydrogen peroxide (H2O2). Peroxiredoxin 4 (PRDX4) is the only peroxiredoxin located within the endoplasmic reticulum (ER) and is the highest expressed ER H2O2 scavenger. PRDX4 has emerged as an important player in numerous diseases and its over...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-10 | PXD024687 | Pride
To elucidate the regulatory network of PRDX4, we identified its interacting proteins through large-scale immunoprecipitation coupled with MS-based proteomics analysis. Notably, among the identified proteins, a E3 ubiquitin ligase ARIH1 potentially involved in PRDX4 degradation was enriched, with exh...
ORGANISM(S): Homo sapiens (Human) 
2026-01-29 | PXD073759 | Pride
NOX4 links metabolic regulation in pancreatic cancer to endoplasmic reticulum redox vulnerability and dependence on PRDX4
PDAC cells acquire metabolic changes that augment NADPH production and cytosolic redox homeostasis. Here we show that high NADPH levels drive activity of NADPH oxidase 4 (NOX4) expressed in the endoplasmic reticulum (ER) membrane. NOX4 produces H2O2 metabolized by Peroxiredoxin 4 (PRDX4) in the ER l...
ORGANISM(S): Homo sapiens 
2021-05-25 | GSE166165 | GEO
To determine the ubiquitinated sites on PRDX4, we analyzed ubiquitinated PRDX4 via MS, revealing modifications at six lysine residues. Point mutation analysis confirmed that K265 residue is the primary site for ARIH1-mediated PRDX4 ubiquitination. The K265 mutation (K265R) almost abolished PRDX4 ubi...
ORGANISM(S): Homo Sapiens 
2026-01-29 | PXD073745 |
Sort   by:  
 Page size