ArticleThe Journal of biological chemistry2013
Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.
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Who cites it
34 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.
- NADPH oxidases in Parkinson's disease: a systematic review.Molecular neurodegeneration · 2017Pooled it
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- Optimization of the Chemical Monoubiquitination System for Low-Solubility Protein: Achieving Balance Between Specificity and Yield.Current issues in molecular biology · 2026Article
- Overcoming Oxidative Stress in Parkinson's Disease: NADPH Oxidase 4 (NOX4) as a Potential Therapeutic Target.Antioxidants (Basel, Switzerland) · 2026Review
- Protein-Driven Copper Redox Regulation: Uncovering the Role of Disulphide Bonds and Allosteric Modulation.Angewandte Chemie (International ed. in English) · 2026Article
- NADPH oxidases: redox regulation of cell homeostasis and disease.Physiological reviews · 2025Review
- Statistical analysis of sequential motifs at biologically relevant protein-protein interfaces.Computational and structural biotechnology journal · 2024Article
- In silico design ofHeliyon · 2024Article
- TEMPRO: nanobody melting temperature estimation model using protein embeddings.Scientific reports · 2024Article
- A comprehensive molecular analysis of bovine coronavirus strains isolated from Brazil and comparison of a wild-type and cell culture-adapted strain associated with respiratory disease.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
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- A Cysteine Residue of Human Cytomegalovirus vMIA Protein Plays a Crucial Role in Viperin Trafficking to Control Viral Infectivity.Journal of virology · 2023Article
- Positional cloning identified HvTUBULIN8 as the candidate gene for round lateral spikelet (RLS) in barley (Hordeum vulgare L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2023Article
- Unprotected peptide macrocyclization and stapling via a fluorine-thiol displacement reaction.Nature communications · 2022Article
- CD34+ derived macrophage and dendritic cells display differential responses to paraquat.Toxicology in vitro : an international journal published in association with BIBRA · 2021Article
- Pathogenic perspective of missense mutations of ORF3a protein of SARS-CoV-2.Virus research · 2021Article
- DUOX1 in mammalian disease pathophysiology.Journal of molecular medicine (Berlin, Germany) · 2021Review
- Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.Nature structural & molecular biology · 2020Article
- Dual Oxidase-Induced Sustained Generation of Hydrogen Peroxide Contributes to Pharmacologic Ascorbate-Induced Cytotoxicity.Cancer research · 2020Article
- Pharmacological characterization of the seven human NOX isoforms and their inhibitors.Redox biology · 2019Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Intramolecular disulfide bond formation is promoted in oxidizing extracellular and endoplasmic reticulum compartments and often contributes to protein stability and function. DUOX1 and DUOX2 are distinguished from other members of the NOX protein family by the presence of a unique extracellular N-terminal region. These peroxidase-like domains lack the conserved cysteines that confer structural stability to mammalian peroxidases. Sequence-based structure predictions suggest that the thiol groups present are solvent-exposed on a single protein surface and are too distant to support intramolecular disulfide bond formation. To investigate the role of these thiol residues, we introduced four individual cysteine to glycine mutations in the peroxidase-like domains of both human DUOXs and purified the recombinant proteins. The mutations caused little change in the stabilities of the monomeric proteins, supporting the hypothesis that the thiol residues are solvent-exposed and not involved in disulfide bonds that are critical for structural integrity. However, the ability of the isolated hDUOX1 peroxidase-like domain to dimerize was altered, suggesting a role for these cysteines in protein-protein interactions that could facilitate homodimerization of the peroxidase-like domain or, in the full-length protein, heterodimeric interactions with a maturation protein. When full-length hDUOX1 was expressed in HEK293 cells, the mutations resulted in decreased H2O2 production that correlated with a decreased amount of the enzyme localized to the membrane surface rather than with a loss of activity or with a failure to synthesize the mutant proteins. These results support a role for the cysteine residues in intermolecular disulfide bond formation with the DUOX maturation factor DUOXA1.
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