Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family.
Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox.
Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions.
NADPH oxidase-dependent acid production in airway epithelial cells.
Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.
Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium.
Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells.
ATP-mediated activation of the NADPH oxidase DUOX1 mediates airway epithelial responses to bacterial stimuli.
Caenorhabditis elegans and human dual oxidase 1 (DUOX1) "peroxidase" domains: insights into heme binding and catalytic activity.
The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA.
When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2.
Structures of human dual oxidase 1 complex in low-calcium and high-calcium states.
Dual oxidase 1 promotes antiviral innate immunity.
Dual NADPH oxidases DUOX1 and DUOX2 synthesize NAADP and are necessary for Ca(2+) signaling during T cell activation.
The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical plasma membrane in epithelial cells via their respective maturation factors DUOXA1 and DUOXA2.
Tyrosine is monoiodinated
Two DITs combine to form thyroxine
DIT and MIT combine to form triiodothyronine