
QSOX1 - Wikipedia
QSOX1 is a multi-domain disulfide catalyst. Unlike other disulfide catalysts, QSOX1 can both generate disulfides de novo and catalyze dithiol / disulfide exchange.
QSOX1 Gene - GeneCards | QSOX1 Protein | QSOX1 Antibody
Mar 30, 2025 · QSOX1 (Quiescin Sulfhydryl Oxidase 1) is a Protein Coding gene. Diseases associated with QSOX1 include Prostate Cancer. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and Innate Immune System.
Quiescin/sulfhydryl oxidase 1b (QSOX1b) induces migration and ...
QSOX1 catalyzes disulfide formation, by reducing molecular oxygen to hydrogen peroxide. Heckler et al. demonstrated, in recombinant human QSOX1, that the first two CxxC motifs are essential to oxidize model substrates, such as dithiothreitol (DTT) or reduced RNAse, since single mutations in the cysteine residues of the CxxC motifs result in ...
QSOX1 quiescin sulfhydryl oxidase 1 [ (human)]
Quiescin sulfhydryl oxidase 1 promotes sorafenib-induced ferroptosis in hepatocellular carcinoma by driving EGFR endosomal trafficking and inhibiting NRF2 activation. QSOX1 promotes mitochondrial apoptosis of hepatocellular carcinoma cells during anchorage-independent growth by inhibiting lipid synthesis.
High expression of QSOX1 reduces tumorogenesis, and is associated with ...
Oct 25, 2012 · We showed that the QSOX1 expression level is inversely correlated to the aggressiveness of breast tumors. Our results show that QSOX1 leads to a decrease in cell proliferation, clonogenic capacities and promotes adhesion to the extracellular matrix.
QSOX1 facilitates dormant esophageal cancer stem cells to
Oct 21, 2024 · Quiescent fibroblast-derived quiescin sulfhydryl oxidase 1 (QSOX1) promotes the expression of PD-L1 and its own expression in DCSCs by elevating the level of reactive oxygen species. Additionally, high QSOX1 in the dormant tumor niche contributes to …
Quiescin sulfhydryl oxidase (QSOX) is expressed in the human
Quiescin sulfhydryl oxidases (QSOXs) catalyze the formation of disulfide bonds in peptides and proteins, and in vertebrates comprise two proteins: QSOX1 and QSOX2. QSOX1, the most extensively studied type, has been implicated in protein folding, production of extracellular matrix, redox regulation, …
Quiescin Sulfhydryl Oxidase 1 Regulates the Proliferation, …
Quiescin sulfhydryl oxidase 1 (QSOX1) involves in the formation of disulfide bonds and participates in the protein folding process. In recent years, accumulating evidences have shown that QSOX1 is a biomarker for tumor development and prognosis. ...
Molecular Inhibitor of QSOX1 Suppresses Tumor Growth in vivo
We demonstrate that the small molecule, SBI-183, (i) inhibits QSOX1 enzymatic activity in vitro, (ii) binds to QSOX1, (iii) inhibits tumor cell growth and invasion in vitro, and (iv) reduces tumor size in two independent mouse models.
QSOX1 quiescin sulfhydryl oxidase 1 [Homo sapiens (human)]
Jan 4, 2025 · High QSOX1 expression is a strong and independent factor of reduced survival in breast cancer and may represent a biomarker for aggressive disease and a potential treatment target
Molecular Inhibitor of QSOX1 Suppresses Tumor Growth
Because short hairpin knockdowns (KD) of QSOX1 have been shown to suppress tumor growth and invasion in vitro and in vivo, we hypothesized that chemical compounds inhibiting QSOX1 enzymatic activity would also suppress tumor growth, invasion, and metastasis.
QSOX1 quiescin sulfhydryl oxidase 1 - NIH Genetic Testing …
QSOX1 regulates trophoblastic apoptosis in preeclampsia through hydrogen peroxide production. Li J, Tong C, Xu P, Wang L, Han TL, Wen L, Luo X, Tan B, Zhu F, Gui S, Gao R, Qi H, Baker PNLi J, et al. J Matern Fetal Neonatal Med, 2019 Nov. PMID 29712536
QUIESCIN Q6 SULFHYDRYL OXIDASE 1; QSOX1 - OMIM
Oct 28, 2013 · QSOX1 is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells. Ilani et al. (2013) examined the physiologic function for extracellular catalysis of de novo disulfide bond formation by QSOX1.
Human Quiescin-sulfhydryl Oxidase, QSOX1: Probing Internal …
The flavoprotein Quiescin-sulfhydryl oxidase (QSOX) rapidly inserts disulfide bonds into unfolded, reduced proteins with the concomitant reduction of oxygen to hydrogen peroxide. This study reports the first heterologous expression and enzymological …
The Emerging Role of QSOX1 in Cancer - PMC
Jul 7, 2014 · Recent Advances: Several groups have reported the over-expression of QSOX1 in breast, pancreas, and prostate cancers. A consensus is building that QSOX1 over-expression is important during tumor cell invasion, facilitating tumor cell migration at the tumor-stroma interface.
QSOX1 Inhibits Autophagic Flux in Breast Cancer Cells - PLOS
Jan 24, 2014 · The QSOX1 protein (Quiescin Sulfhydryl oxidase 1) catalyzes the formation of disulfide bonds and is involved in the folding and stability of proteins. More recently, QSOX1 has been associated with tumorigenesis and protection against cellular stress.
Quiescin Sulfhydryl Oxidase 1 Regulates the Proliferation ... - PubMed
Jun 17, 2020 · Background: Quiescin sulfhydryl oxidase 1 (QSOX1) involves in the formation of disulfide bonds and participates in the protein folding process. In recent years, accumulating evidences have shown that QSOX1 is a biomarker for tumor development and prognosis.
UniProt
Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide (PubMed: 17331072, PubMed: 18393449, PubMed: …
High expression of QSOX1 reduces tumorogenesis, and is …
Oct 25, 2012 · In our study, we demonstrate that QSOX1 could inhibit breast tumor development and aggressiveness, which is in agreement with our findings, indicating that a high QSOX1 expression is associated with a better survival for breast cancer patients.
Quiescin Sulfhydryl Oxidase 1 (QSOX1) Secreted by Lung Cancer …
Quiescin sulfhydryl oxidase (QSOX1) was selected as a biomarker candidate from the enriched proteins in the secretion of lung cancer cells. QSOX1 levels were higher in 82% (51 of 62 tissues) of lung cancer tissues compared to adjacent normal tissues.