ArticleArchives of biochemistry and biophysics2011
Structural stability and heme binding potential of the truncated human dual oxidase 2 (DUOX2) peroxidase domain.
Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.
- NADPH oxidases in Parkinson's disease: a systematic review.Molecular neurodegeneration · 2017Pooled it
- NADPH oxidases: redox regulation of cell homeostasis and disease.Physiological reviews · 2025Review
- A genome-wide association study provides insights into the genetic etiology of 57 essential and non-essential trace elements in humans.Communications biology · 2024Article
- NOX Inhibitors: From Bench to Naxibs to Bedside.Handbook of experimental pharmacology · 2021Article
- Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their RegulationPhysiological reviews · 2019Review
- Heme peroxidase HPX-2 protects Caenorhabditis elegans from pathogens.PLoS genetics · 2019Article
- Genetic disorders coupled to ROS deficiency.Redox biology · 2015Review
- Evolution of NADPH Oxidase Inhibitors: Selectivity and Mechanisms for Target Engagement.Antioxidants & redox signaling · 2015Review
- The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release.The Journal of biological chemistry · 2015Article
- NADPH oxidases: a perspective on reactive oxygen species production in tumor biology.Antioxidants & redox signaling · 2014Review
- The SKPO-1 peroxidase functions in the hypodermis to protect Caenorhabditis elegans from bacterial infection.Genetics · 2014Article
- Recent insights into the cell biology of thyroid angiofollicular units.Endocrine reviews · 2013Review
- Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.The Journal of biological chemistry · 2013Article
- NADPH oxidase biology and the regulation of tyrosine kinase receptor signaling and cancer drug cytotoxicity.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The essential role of human dual oxidase 2 (hDUOX2) in thyroid hormone biosynthesis defines this member of the NOX/DUOX family, whose absence due to mutation has been directly related to disease, specifically hypothyroidism. Both human DUOX isoforms, hDUOX1 and hDUOX2, are expressed in thyroid tissue; however, hDUOX1 cannot compensate for inactivation of hDUOX2, suggesting that each enzyme is differentially regulated and/or functions in a unique manner. In efforts to uncover relevant structural and functional differences we have expressed and purified the peroxidase domain of hDUOX2(1-599) for direct comparison with the previously studied hDUOX1(1-593). As was shown for hDUOX1, the truncated hDUOX2 domain purifies without a bound heme co-factor and displays no peroxidase activity. However, hDUOX2(1-599) displays greater stability than hDUOX1(1-593). Surprisingly, upon titration with heme, both isoforms bind heme with a low micromolar affinity, demonstrating that they retain a heme binding site. A conformational difference in the full-length protein and/or a protein-protein interaction may be required to increase the heme binding affinity.
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Registered trials
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