ArticleNature structural & molecular biology2020
Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.
Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 62 citations in OpenAlex.
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- From Defense to Disease: NADPH Oxidase in Cellular Function and Dysregulation.Journal of immunology research · 2026Review
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- NADPH oxidases: redox regulation of cell homeostasis and disease.Physiological reviews · 2025Review
- Structural and mechanistic insights into Streptococcus pneumoniae NADPH oxidase.Nature structural & molecular biology · 2024Article
- Structural basis of human NOX5 activation.Nature communications · 2024Article
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- Genome-Wide Identification of the Ferric Chelate Reductase (Plants (Basel, Switzerland) · 2024Article
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- NADPH Oxidases: From Molecular Mechanisms to Current Inhibitors.Journal of medicinal chemistry · 2023Review
- Antioxidant, Collagenase Inhibitory, and Antibacterial Effects of Bioactive Peptides Derived from Enzymatic Hydrolysate ofMarine drugs · 2023Article
- A predicted structure of NADPH Oxidase 1 identifies key components of ROS generation and strategies for inhibition.PloS one · 2023Article
- High-throughput screening of caterpillars as a platform to study host-microbe interactions and enteric immunity.Nature communications · 2022Article
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- Structure of the core human NADPH oxidase NOX2.Nature communications · 2022Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
DUOX1, an NADPH oxidase family member, catalyzes the production of hydrogen peroxide. DUOX1 is expressed in various tissues, including the thyroid and respiratory tract, and plays a crucial role in processes such as thyroid hormone biosynthesis and innate host defense. DUOX1 co-assembles with its maturation factor DUOXA1 to form an active enzyme complex. However, the molecular mechanisms for activation and regulation of DUOX1 remain mostly unclear. Here, I present cryo-EM structures of the mammalian DUOX1-DUOXA1 complex, in the absence and presence of substrate NADPH, as well as DUOX1-DUOXA1 in an unexpected dimer-of-dimers configuration. These structures reveal atomic details of the DUOX1-DUOXA1 interaction, a lipid-mediated NADPH-binding pocket and the electron transfer path. Furthermore, biochemical and structural analyses indicate that the dimer-of-dimers configuration represents an inactive state of DUOX1-DUOXA1, suggesting an oligomerization-dependent regulatory mechanism. Together, my work provides structural bases for DUOX1-DUOXA1 activation and regulation.
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