ArticleThe Biochemical journal2013
Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Electric Field-Induced Release and Measurement Liquid Biopsy of Urinary Transcriptomics and Key Proteins from Normal and High-risk Pregnant Women.Reproductive sciences (Thousand Oaks, Calif.) · 2026Article
- Spatiotemporal dynamics of reactive oxygen species: implications for cellular homeostasis and redox therapies.Cellular & molecular biology letters · 2026Review
- QSOX1: A Mysterious Golgi-Localized Disulfide Bond Catalyst and an Emerging Cancer Regulator.Cancers · 2026Article
- (-)-Epigallocatechin-3-Gallate and Quercetin Inhibit Quiescin Sulfhydryl Oxidase 1 Secretion from Hepatocellular Carcinoma Cells.Antioxidants (Basel, Switzerland) · 2025Article
- QSOX1 Modulates Glioblastoma Cell Proliferation and Migration In Vitro and Invasion In Vivo.Cancers · 2024Article
- Effects of redox modulation on quiescin/sulfhydryl oxidase activity of melanoma cells.Molecular and cellular biochemistry · 2024Article
- Development of tandem antigen capture ELISAs measuring QSOX1 isoforms in plasma and serum.Free radical biology & medicine · 2024Article
- Secretion of the disulfide bond generating catalyst QSOX1 from pancreatic tumor cells into the extracellular matrix: association with extracellular vesicles and matrix proteins.Journal of extracellular biology · 2022Article
- Evaluation of dithiothreitol-oxidizing capacity (DOC) as a serum biomarker for chronic hepatitis B in patients exhibiting normal alanine aminotransferase levels: a pilot study towards better monitoring of disease.EClinicalMedicine · 2021Article
- Secretory mouse quiescin sulfhydryl oxidase 1 aggregates defected human and mouse spermatozoa in vitro and in vivo.iScience · 2021Article
- Unbiased Profiling of the Human Proinsulin Biosynthetic Interaction Network Reveals a Role for Peroxiredoxin 4 in Proinsulin Folding.Diabetes · 2020Article
- PI4KIIIβ is a therapeutic target in chromosome 1q-amplified lung adenocarcinoma.Science translational medicine · 2020Article
- Article
- Core fucosylated glycan-dependent inhibitory effect of QSOX1-S on invasion and metastasis of hepatocellular carcinoma.Cell death discovery · 2019Article
- Extracellular Thiol Isomerases and Their Role in Thrombus Formation.Antioxidants & redox signaling · 2016Review
- Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis.The Journal of biological chemistry · 2014Article
- The emerging role of QSOX1 in cancer.Antioxidants & redox signaling · 2014Review
- Disulfide bond generation in mammalian blood serum: detection and purification of quiescin-sulfhydryl oxidase.Free radical biology & medicine · 2014Article
- Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase.The Journal of biological chemistry · 2014Article
- Two phases of disulfide bond formation have differing requirements for oxygen.The Journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
QSOX1 (quiescin sulfhydryl oxidase 1) efficiently catalyses the insertion of disulfide bonds into a wide range of proteins. The enzyme is mechanistically well characterized, but its subcellular location and the identity of its protein substrates remain ill-defined. The function of QSOX1 is likely to involve disulfide formation in proteins entering the secretory pathway or outside the cell. In the present study, we show that this enzyme is efficiently secreted from mammalian cells despite the presence of a transmembrane domain. We identify internal cleavage sites and demonstrate that the protein is processed within the Golgi apparatus to yield soluble enzyme. As a consequence of this efficient processing, QSOX1 is probably functional outside the cell. Also, QSOX1 forms a dimer upon cleavage of the C-terminal domain. The processing of QSOX1 suggests a novel level of regulation of secretion of this potent disulfide catalyst and producer of hydrogen peroxide.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.