PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24518246-6 2014 Dual oxidase-2 (DUOX2), central to H(2)O(2) formation, was also synergistically induced by IL-13 and IFN-gamma. Hydrogen Peroxide 35-43 dual oxidase 2 Homo sapiens 0-14 25960956-1 2015 The production of H2O2, which is essential to thyroid hormone synthesis, involves two NADPH oxidases: dual oxidases 1 and 2 (DuOx1 and DuOx2). Hydrogen Peroxide 18-22 dual oxidase 2 Homo sapiens 135-140 25960956-11 2015 In conclusion, we show that DuOx2 expression is regulated by hormones and transcription factors involved in thyroid organogenesis and carcinogenesis, reinforcing the importance of the control of H2O2 generation in the thyroid. Hydrogen Peroxide 195-199 dual oxidase 2 Homo sapiens 28-33 26207686-9 2015 RT(2) PCR Profiler array analysis indicated that this combined regimen upregulated dual oxidase 2 (DUOX2), an enzyme functioning in the production of hydrogen peroxide, without upregulating genes involved in DNA repair. Hydrogen Peroxide 151-168 dual oxidase 2 Homo sapiens 84-98 26207686-9 2015 RT(2) PCR Profiler array analysis indicated that this combined regimen upregulated dual oxidase 2 (DUOX2), an enzyme functioning in the production of hydrogen peroxide, without upregulating genes involved in DNA repair. Hydrogen Peroxide 151-168 dual oxidase 2 Homo sapiens 100-105 24518246-6 2014 Dual oxidase-2 (DUOX2), central to H(2)O(2) formation, was also synergistically induced by IL-13 and IFN-gamma. Hydrogen Peroxide 35-43 dual oxidase 2 Homo sapiens 16-21 23545780-6 2013 Importantly, our study uncovers that the development of the antiviral state relies on DUOX2-dependent H2O2 production. Hydrogen Peroxide 102-106 dual oxidase 2 Homo sapiens 86-91 24053146-2 2014 This three-component system consists of the hydrogen peroxide (H2O2)-producing enzymes dual oxidase (Duox)1 and Duox2, thiocyanate (SCN(-)), and secreted lactoperoxidase (LPO). Hydrogen Peroxide 44-61 dual oxidase 2 Homo sapiens 112-117 24053146-2 2014 This three-component system consists of the hydrogen peroxide (H2O2)-producing enzymes dual oxidase (Duox)1 and Duox2, thiocyanate (SCN(-)), and secreted lactoperoxidase (LPO). Hydrogen Peroxide 63-67 dual oxidase 2 Homo sapiens 112-117 25248169-4 2014 The functional capacities of novel missense variants of DUOX2 were verified by measuring H2O2 generation in vitro. Hydrogen Peroxide 89-93 dual oxidase 2 Homo sapiens 56-61 25248169-7 2014 A functional analysis of the DUOX2 variants revealed that most variants, other than p.G206V and p.H678R, caused a significant reduction in H2O2 generation. Hydrogen Peroxide 139-143 dual oxidase 2 Homo sapiens 29-34 24492313-4 2014 RESULTS: DUOX2 with maturation partner DUOXA2 forms the predominant system for H2O2 production in human colon and is upregulated in active colitis. Hydrogen Peroxide 79-83 dual oxidase 2 Homo sapiens 9-14 23962049-10 2014 Using HEK-293 cells expressing Duox1 or Duox2 and endogenous H1R, histamine triggers an immediate intracellular calcium signal and H2O2 release. Hydrogen Peroxide 131-135 dual oxidase 2 Homo sapiens 40-45 20407074-2 2010 The molecule for H(2)O(2) production in the thyroid gland has been known as dual oxidase 2 (DUOX2). Hydrogen Peroxide 17-25 dual oxidase 2 Homo sapiens 76-90 23281318-2 2013 Dual oxidases (DUOX1 and DUOX2) are the H2 O2 -producing isoforms of the nicotinamide adenine dinucleotide phosphate (NADPH) oxidase family in the airway epithelium. Hydrogen Peroxide 40-45 dual oxidase 2 Homo sapiens 25-30 23404134-3 2013 The main enzymes composing the H2O2-generating system are the dual oxidase 2 (DUOX2) and the recently described DUOX maturation factor 2 (DUOXA2). Hydrogen Peroxide 31-35 dual oxidase 2 Homo sapiens 62-76 23404134-3 2013 The main enzymes composing the H2O2-generating system are the dual oxidase 2 (DUOX2) and the recently described DUOX maturation factor 2 (DUOXA2). Hydrogen Peroxide 31-35 dual oxidase 2 Homo sapiens 78-83 22301785-4 2012 In humans, mutations in both DUOX2 and DUOXA2 can cause congenital hypothyroidism with partial iodide organification defects compatible with a role of DUOX2-generated H(2)O(2) in driving thyroid peroxidase activity. Hydrogen Peroxide 167-175 dual oxidase 2 Homo sapiens 29-34 22301785-4 2012 In humans, mutations in both DUOX2 and DUOXA2 can cause congenital hypothyroidism with partial iodide organification defects compatible with a role of DUOX2-generated H(2)O(2) in driving thyroid peroxidase activity. Hydrogen Peroxide 167-175 dual oxidase 2 Homo sapiens 151-156 21321110-1 2011 Dual oxidase 2 is a member of the NADPH oxidase (Nox) gene family that plays a critical role in the biosynthesis of thyroid hormone as well as in the inflammatory response of the upper airway mucosa and in wound healing, presumably through its ability to generate reactive oxygen species, including H2O2. Hydrogen Peroxide 299-303 dual oxidase 2 Homo sapiens 0-14 21321110-4 2011 Furthermore, increased Duox2/DuoxA2 expression was closely associated with a significant increase in the production of both intracellular reactive oxygen species and extracellular H2O2. Hydrogen Peroxide 180-184 dual oxidase 2 Homo sapiens 23-28 23404210-1 2013 Dual oxidase 2 (Duox2), one of the seven members of the NADPH oxidase gene family, plays a critical role in generating H2O2 for thyroid hormone biosynthesis and as an integral part of the host defense system of the respiratory epithelium and the gastrointestinal tract. Hydrogen Peroxide 119-123 dual oxidase 2 Homo sapiens 0-14 23404210-1 2013 Dual oxidase 2 (Duox2), one of the seven members of the NADPH oxidase gene family, plays a critical role in generating H2O2 for thyroid hormone biosynthesis and as an integral part of the host defense system of the respiratory epithelium and the gastrointestinal tract. Hydrogen Peroxide 119-123 dual oxidase 2 Homo sapiens 16-21 21367925-1 2011 CONTEXT: Dual oxidases (DUOX1 and DUOX2) play a crucial role in the generation of hydrogen peroxide required in the oxidation of iodide and the synthesis of thyroid hormone. Hydrogen Peroxide 82-99 dual oxidase 2 Homo sapiens 34-39 20511343-1 2010 DUOX1 and DUOX2 are members of the NADPH oxidase family that are specifically regulated to produce hydrogen peroxide in epithelia of the thyroid, gastrointestinal tract, and respiratory tract. Hydrogen Peroxide 99-116 dual oxidase 2 Homo sapiens 10-15 20122987-3 2010 The primary enzyme feeding H(2)O(2) to thyroid peroxidase is a heterodimeric NADPH oxidase complex of dual oxidase 2 (DUOX2) and DUOX maturation factor 2 (DUOXA2) at the apical plasma membrane. Hydrogen Peroxide 27-35 dual oxidase 2 Homo sapiens 102-116 20122987-3 2010 The primary enzyme feeding H(2)O(2) to thyroid peroxidase is a heterodimeric NADPH oxidase complex of dual oxidase 2 (DUOX2) and DUOX maturation factor 2 (DUOXA2) at the apical plasma membrane. Hydrogen Peroxide 27-35 dual oxidase 2 Homo sapiens 118-123 20407074-2 2010 The molecule for H(2)O(2) production in the thyroid gland has been known as dual oxidase 2 (DUOX2). Hydrogen Peroxide 17-25 dual oxidase 2 Homo sapiens 92-97 20407074-12 2010 Mutation of either DUOX2 or DUOXA2 gene is a newly recognized cause of hypothyroidism due to insufficient H(2)O(2) production. Hydrogen Peroxide 106-114 dual oxidase 2 Homo sapiens 19-24 19358684-3 2009 The dual oxidases DUOX1 and DUOX2 are the H(2)O(2)-producing isoforms of the NADPH oxidase family found in epithelial cells. Hydrogen Peroxide 42-50 dual oxidase 2 Homo sapiens 28-33 20187165-0 2010 Compound heterozygosity for a novel hemizygous missense mutation and a partial deletion affecting the catalytic core of the H2O2-generating enzyme DUOX2 associated with transient congenital hypothyroidism. Hydrogen Peroxide 124-128 dual oxidase 2 Homo sapiens 147-152 19074510-1 2009 Dual oxidases (Duox1 and Duox2) are plasma membrane-targeted hydrogen peroxide generators that support extracellular hemoperoxidases. Hydrogen Peroxide 61-78 dual oxidase 2 Homo sapiens 25-30 19074510-8 2009 Duox1/Duoxa1alpha and Duox2/Duoxa2 pairs produce the highest levels of hydrogen peroxide, as they undergo Golgi-based carbohydrate modifications and form stable cell surface complexes. Hydrogen Peroxide 71-88 dual oxidase 2 Homo sapiens 22-27 18177232-1 2008 Dual oxidase (Duox) 1 and Duox2 are important sources of hydrogen peroxide production and play a role in host defense in airways. Hydrogen Peroxide 57-74 dual oxidase 2 Homo sapiens 26-31 15972824-0 2005 Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. Hydrogen Peroxide 47-51 dual oxidase 2 Homo sapiens 0-14 17374849-1 2007 Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. Hydrogen Peroxide 112-116 dual oxidase 2 Homo sapiens 0-14 17374849-1 2007 Dual oxidase 2 (DUOX2), a reduced NAD phosphate:O2 oxidoreductase flavoprotein, is a component of the thyrocyte H2O2 generator required for hormone synthesis at the apical plasma membrane. Hydrogen Peroxide 112-116 dual oxidase 2 Homo sapiens 16-21 17374849-3 2007 We have now used a DUOXA2 reconstituted system to provide the first characterization of natural DUOX2 missense variants (Q36H, R376W, D506N) at the molecular level, analyzing their impact on H2O2 generation, trafficking, stability, folding, and DUOXA2 interaction. Hydrogen Peroxide 191-195 dual oxidase 2 Homo sapiens 96-101 16111680-3 2005 Increasing evidence supports the hypothesis that the dual function NAD(P)H oxidases/peroxidases, Duox1 and Duox2, are important sources of regulated H2O2 production in respiratory tract epithelium. Hydrogen Peroxide 149-153 dual oxidase 2 Homo sapiens 107-112 18511861-9 2008 Duox1 and Duox2 localize to the apical plasma membrane of epithelial cells in major airways, salivary glands, and the gastrointestinal tract, and provide extracellular hydrogen peroxide to lactoperoxidase to produce antimicrobial hypothiocyanite ions. Hydrogen Peroxide 168-185 dual oxidase 2 Homo sapiens 10-15 16987008-2 2006 The human genome contains seven members of the Nox family: the superoxide-producing enzymes Nox1 through Nox5 and the dual oxidases Duox1 and Duox2 that release hydrogen peroxide but not superoxide. Hydrogen Peroxide 161-178 dual oxidase 2 Homo sapiens 142-147 16987011-2 2006 The DUOX1 and DUOX2 mRNAs were originally cloned from thyroid tissue, and the corresponding proteins were recognized as intricate components of the thyroid hormone synthesis process, providing hydrogen peroxide essential for the organification of iodide. Hydrogen Peroxide 193-210 dual oxidase 2 Homo sapiens 14-19 15972824-1 2005 Duox2 (and probably Duox1) is a glycoflavoprotein involved in thyroid hormone biosynthesis, as the thyroid H2O2 generator functionally associated with Tpo (thyroperoxidase). Hydrogen Peroxide 107-111 dual oxidase 2 Homo sapiens 0-5 15972824-3 2005 For the first time, we investigated the H2O2-generating activity in the particulate fractions from DUOX2- and DUOX1-transfected HEK293 and Chinese hamster ovary cells. Hydrogen Peroxide 40-44 dual oxidase 2 Homo sapiens 99-104 15972824-10 2005 These results suggest that post-translational modifications during the maturation process of Duox2 could be implicated in the mechanism of H2O2 formation by favoring intramolecular superoxide dismutation. Hydrogen Peroxide 139-143 dual oxidase 2 Homo sapiens 93-98 31678720-3 2020 Duox1 and Duox2 activities similarly produce intracellular protons but synthesize hydrogen peroxide directly instead of superoxide. Hydrogen Peroxide 82-99 dual oxidase 2 Homo sapiens 10-15 15591162-1 2005 The dual oxidase (Duox)2 flavoprotein is strongly expressed in the thyroid gland, where it plays a critical role in the synthesis of thyroid hormones by providing thyroperoxidase with H2O2. Hydrogen Peroxide 184-188 dual oxidase 2 Homo sapiens 18-24 15591162-7 2005 A Ca2+/NADPH-dependent H2O2-generating system was associated with Duox2 protein expression, which had the same biochemical characteristics as the NADPH oxidase in the thyroid. Hydrogen Peroxide 23-27 dual oxidase 2 Homo sapiens 66-71 15591162-10 2005 The discovery of Duox2 as a novel source of H2O2 in the digestive tract, particularly in the cecum and colon, makes it a new candidate mediator of physiopathological processes. Hydrogen Peroxide 44-48 dual oxidase 2 Homo sapiens 17-22 12824283-8 2003 Our observations suggest that Duox1 and Duox2 are novel H2O2 sources that can support LPO-mediated antimicrobial defense mechanisms on mucosal surfaces. Hydrogen Peroxide 56-60 dual oxidase 2 Homo sapiens 40-45 35429653-1 2022 Genetic variants affecting the function of dual oxidase 2 (DUOX2), the catalytic subunit of membrane-bound enzymes that produce hydrogen peroxide, are associated with very early-onset inflammatory bowel disease (VEO-IBD). Hydrogen Peroxide 128-145 dual oxidase 2 Homo sapiens 43-57 35429653-1 2022 Genetic variants affecting the function of dual oxidase 2 (DUOX2), the catalytic subunit of membrane-bound enzymes that produce hydrogen peroxide, are associated with very early-onset inflammatory bowel disease (VEO-IBD). Hydrogen Peroxide 128-145 dual oxidase 2 Homo sapiens 59-64 35429653-8 2022 Hydrogen peroxide generation upon ionomycin stimulation was lower in cells expressing R1212H-DUOX2 and F1490Y-DUOX2 than in those expressing WT-DUOX2. Hydrogen Peroxide 0-17 dual oxidase 2 Homo sapiens 110-115 35429653-8 2022 Hydrogen peroxide generation upon ionomycin stimulation was lower in cells expressing R1212H-DUOX2 and F1490Y-DUOX2 than in those expressing WT-DUOX2. Hydrogen Peroxide 0-17 dual oxidase 2 Homo sapiens 144-149 34019632-2 2021 Thyroid dyshormonogenesis is the main cause of congenital hypothyroidism in Chinese CH patients and DUOX2 is the most frequent mutated gene involved in H2O2 production. Hydrogen Peroxide 152-156 dual oxidase 2 Homo sapiens 100-105 34019632-3 2021 In human, the primary sources for H2O2 production are DUOX1 and DUOX2, while in zebrafish, there is only a single orthologue for DUOX1 and DUOX2. Hydrogen Peroxide 34-38 dual oxidase 2 Homo sapiens 64-69 11762710-1 2001 Duox2, and probably Duox1 are glycoflavoproteins involved in the thyroid H2O2 generator functionally associated to thyroperoxidase (TPO). Hydrogen Peroxide 73-77 dual oxidase 2 Homo sapiens 0-5 34197086-7 2021 In response to intracellular glutathione, Pt(II) is released from CPNP-Fc/Pt and triggers enzymatic cascade reactions with nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase) and superoxide dismutase to convert oxygen into H2O2. Hydrogen Peroxide 239-243 dual oxidase 2 Homo sapiens 123-174 32767144-12 2021 Essential functions include the oxidative burst by NOX2 as antimicrobial innate immune response; gastrointestinal NOX1 and DUOX2 generating low H2O2 concentrations sufficient to trigger antivirulence mechanisms; and thyroidal DUOX2 essential for providing H2O2 reduced by TPO to oxidize iodide to an iodinating form which is then attached to tyrosyls in TG. Hydrogen Peroxide 144-148 dual oxidase 2 Homo sapiens 123-128 31513783-0 2019 The Dual Oxidase Duox2 stabilized with DuoxA2 in an enzymatic complex at the surface of the cell produces extracellular H2O2 able to induce DNA damage in an inducible cellular model. Hydrogen Peroxide 120-124 dual oxidase 2 Homo sapiens 17-22 31513783-1 2019 Thyroid hormone synthesis requires H2O2, produced by two NADPH oxidases, Duox1 and Duox2. Hydrogen Peroxide 35-39 dual oxidase 2 Homo sapiens 83-88 31513783-6 2019 By normalizing H2O2 extracellular production by Duox or DuoxA membrane expression, we have demonstrated that the most active enzymatic complex is Duox2/DuoxA2, compared to Duox1/DuoxA1. Hydrogen Peroxide 15-19 dual oxidase 2 Homo sapiens 146-151 31513783-10 2019 The present data demonstrate for the first time that H2O2 produced by the Duox2/DuoxA2 cell surface enzymatic complex could provoke potential mutagenic DNA damage in an inducible cellular model, and highlight the importance of the co-expressed partner in the activity and stability of Duox/DuoxA complexes. Hydrogen Peroxide 53-57 dual oxidase 2 Homo sapiens 74-79 31548328-1 2019 Dual oxidase 2 (DUOX2) generates H2O2 that plays a critical role in both host defense and chronic inflammation. Hydrogen Peroxide 33-37 dual oxidase 2 Homo sapiens 16-21 31548328-8 2019 These data suggest a functional association between DUOX2-mediated H2O2 production and induced DNA damage in gastrointestinal malignancies. Hydrogen Peroxide 67-71 dual oxidase 2 Homo sapiens 52-57 31083324-2 2019 Thyroid H2O2 is generated by a member of the family of NADPH oxidase enzymes (NOX-es), termed dual oxidase 2 (DUOX2). Hydrogen Peroxide 8-12 dual oxidase 2 Homo sapiens 94-108 31548328-1 2019 Dual oxidase 2 (DUOX2) generates H2O2 that plays a critical role in both host defense and chronic inflammation. Hydrogen Peroxide 33-37 dual oxidase 2 Homo sapiens 0-14 31083324-2 2019 Thyroid H2O2 is generated by a member of the family of NADPH oxidase enzymes (NOX-es), termed dual oxidase 2 (DUOX2). Hydrogen Peroxide 8-12 dual oxidase 2 Homo sapiens 110-115 31083324-5 2019 Inappropriate DUOX2-generated H2O2 production results in thyroid hypofunction in rodent models. Hydrogen Peroxide 30-34 dual oxidase 2 Homo sapiens 14-19 31172466-1 2019 The dual oxidase (DUOX) enzymes (DUOX1 and DUOX2) are unique hydrogen peroxide (H2O2)-producing members of the NADPH oxidase (NOX) family, structurally distinguished from their related NOX isoforms by the presence of an additional N-terminal extracellular domain. Hydrogen Peroxide 61-78 dual oxidase 2 Homo sapiens 43-48 30318012-7 2019 NADPH oxidase includes five NOX and two dual oxidases (DUOX1 and DUOX2) subfamilies that through the production of superoxide and hydrogen peroxide, play key roles in oxidative stress and several signaling pathways involved in early and late effects of ionizing radiation. Hydrogen Peroxide 130-147 dual oxidase 2 Homo sapiens 65-70 31172499-10 2019 DUOX2 function should be carefully evaluated using an in vitro assay wherein (1) DUOXA2 is co-expressed, (2) H2O2 production is activated, (3) and DUOX2 membrane expression is precisely analyzed. Hydrogen Peroxide 109-113 dual oxidase 2 Homo sapiens 0-5 28633507-1 2017 Context: The DUOX2 enzyme generates hydrogen peroxide (H2O2), a crucial electron acceptor for the thyroid peroxidase-catalyzed iodination and coupling reactions mediating thyroid hormone biosynthesis. Hydrogen Peroxide 36-53 dual oxidase 2 Homo sapiens 13-18 29845893-1 2018 BACKGROUND: Dual oxidases (DUOX1 and DUOX2) were initially identified as H2O2 sources involved in thyroid hormone synthesis. Hydrogen Peroxide 73-77 dual oxidase 2 Homo sapiens 37-42 29845893-2 2018 Congenital hypothyroidism (CH) resulting from inactivating mutations in the DUOX2 gene highlighted that DUOX2 is the major H2O2 provider to thyroperoxidase. Hydrogen Peroxide 123-127 dual oxidase 2 Homo sapiens 76-81 29845893-2 2018 Congenital hypothyroidism (CH) resulting from inactivating mutations in the DUOX2 gene highlighted that DUOX2 is the major H2O2 provider to thyroperoxidase. Hydrogen Peroxide 123-127 dual oxidase 2 Homo sapiens 104-109 31172466-1 2019 The dual oxidase (DUOX) enzymes (DUOX1 and DUOX2) are unique hydrogen peroxide (H2O2)-producing members of the NADPH oxidase (NOX) family, structurally distinguished from their related NOX isoforms by the presence of an additional N-terminal extracellular domain. Hydrogen Peroxide 80-84 dual oxidase 2 Homo sapiens 43-48 29373314-1 2018 Duox2 belongs to the large family of NADPH-oxidase enzymes that are implicated in immune response, vasoregulation, hormone synthesis, cell growth and differentiation via the regulated synthesis of H2O2 and reactive oxygen species. Hydrogen Peroxide 197-201 dual oxidase 2 Homo sapiens 0-5 29373314-3 2018 Now, using the CRISPR/Cas9-mediated genome editing we demonstrate that the extreme C-terminal region of Duox2 is required for PDGF-stimulated activity of Duox2 and H2O2 production. Hydrogen Peroxide 164-168 dual oxidase 2 Homo sapiens 104-109 29373314-5 2018 We found that nonsense substitution of the last 23 amino acids in Duox2 results in complete loss of PDGF stimulation of intracellular H2O2 and fibroblast migration, yet these mutations have no effects on the expression of Duox2 and other NADPH-oxidases in cells. Hydrogen Peroxide 134-138 dual oxidase 2 Homo sapiens 66-71 29272487-1 2017 Background: DUOX2 and DUOXA2 form the predominant H2O2-producing system in human colorectal mucosa. Hydrogen Peroxide 50-54 dual oxidase 2 Homo sapiens 12-17 28633507-1 2017 Context: The DUOX2 enzyme generates hydrogen peroxide (H2O2), a crucial electron acceptor for the thyroid peroxidase-catalyzed iodination and coupling reactions mediating thyroid hormone biosynthesis. Hydrogen Peroxide 55-59 dual oxidase 2 Homo sapiens 13-18 27864363-2 2016 OSCN- is generated by the catalysis of peroxidases using thiocyanate transported via several anion transporters, including pendrin/SLC26A4 and hydrogen peroxide (H2O2) generated by Duox1 and Duox2. Hydrogen Peroxide 143-160 dual oxidase 2 Homo sapiens 191-196 28648510-1 2017 After the identification of thyroid H2O2 generation system (DUOX) and of its maturation factors (DUOXA), defects in DUOX2 and/or DUOXA2 were rapidly recognized as the possible cause of congenital hypothyroidism (CH) due to thyroid dyshormonogenesis. Hydrogen Peroxide 36-40 dual oxidase 2 Homo sapiens 116-121 28648510-5 2017 Finally, the hypotheses to explain the phenotypic variability of the DUOX2/A2 mutations are discussed, such as the existence of other H2O2 generating systems, the age variability in thyroid hormones requirements, the differences in ethnicity, in iodine intake, and in the methodological approaches. Hydrogen Peroxide 134-138 dual oxidase 2 Homo sapiens 69-74 27864363-2 2016 OSCN- is generated by the catalysis of peroxidases using thiocyanate transported via several anion transporters, including pendrin/SLC26A4 and hydrogen peroxide (H2O2) generated by Duox1 and Duox2. Hydrogen Peroxide 162-166 dual oxidase 2 Homo sapiens 191-196 27637085-0 2016 Dual oxidase 2 and pancreatic adenocarcinoma: IFN-gamma-mediated dual oxidase 2 overexpression results in H2O2-induced, ERK-associated up-regulation of HIF-1alpha and VEGF-A. Hydrogen Peroxide 106-110 dual oxidase 2 Homo sapiens 0-14 27637085-0 2016 Dual oxidase 2 and pancreatic adenocarcinoma: IFN-gamma-mediated dual oxidase 2 overexpression results in H2O2-induced, ERK-associated up-regulation of HIF-1alpha and VEGF-A. Hydrogen Peroxide 106-110 dual oxidase 2 Homo sapiens 65-79 27637085-2 2016 We found previously that exposure of pancreatic ductal adenocarcinoma cells to the pro-inflammatory cytokine IFN-gamma increased DUOX2 expression (but not other NADPH oxidases) leading to long-lived H2O2 production. Hydrogen Peroxide 199-203 dual oxidase 2 Homo sapiens 129-134 27637085-3 2016 To elucidate the pathophysiology of DUOX2-mediated H2O2 formation in the pancreas further, we demonstrate here that IFN-gamma-treated BxPC-3 and CFPAC-1 pancreatic cancer cells (known to increase DUOX2 expression) produce significant levels of intracellular oxidants and extracellular H2O2 which correlate with concomitant up-regulation of VEGF-A and HIF-1alpha transcription. Hydrogen Peroxide 51-55 dual oxidase 2 Homo sapiens 36-41 27637085-3 2016 To elucidate the pathophysiology of DUOX2-mediated H2O2 formation in the pancreas further, we demonstrate here that IFN-gamma-treated BxPC-3 and CFPAC-1 pancreatic cancer cells (known to increase DUOX2 expression) produce significant levels of intracellular oxidants and extracellular H2O2 which correlate with concomitant up-regulation of VEGF-A and HIF-1alpha transcription. Hydrogen Peroxide 285-289 dual oxidase 2 Homo sapiens 36-41 29435108-1 2018 Mutations in the dual oxidase 2 gene (DUOX2) impair hydrogen peroxide (H2O2) production and cause dyshormonogenesis. Hydrogen Peroxide 52-69 dual oxidase 2 Homo sapiens 17-31 27373512-7 2016 We examined the effects of a variant in DUOX2 on hydrogen peroxide production in HEK293 cells. Hydrogen Peroxide 49-66 dual oxidase 2 Homo sapiens 40-45 27174022-6 2016 Thyrocytes express dual oxidase 2, which produces most of the H2O2 for thyroid hormone synthesis. Hydrogen Peroxide 62-66 dual oxidase 2 Homo sapiens 19-33 29435108-1 2018 Mutations in the dual oxidase 2 gene (DUOX2) impair hydrogen peroxide (H2O2) production and cause dyshormonogenesis. Hydrogen Peroxide 52-69 dual oxidase 2 Homo sapiens 38-43 29435108-1 2018 Mutations in the dual oxidase 2 gene (DUOX2) impair hydrogen peroxide (H2O2) production and cause dyshormonogenesis. Hydrogen Peroxide 71-75 dual oxidase 2 Homo sapiens 17-31 29435108-1 2018 Mutations in the dual oxidase 2 gene (DUOX2) impair hydrogen peroxide (H2O2) production and cause dyshormonogenesis. Hydrogen Peroxide 71-75 dual oxidase 2 Homo sapiens 38-43 29435108-6 2018 The effects of DUOX2 mutations were characterized by H2O2 production assays and cycloheximide (CHX) chase experiments. Hydrogen Peroxide 53-57 dual oxidase 2 Homo sapiens 15-20 26823467-7 2016 Duox2 up-regulation stoichiometrically increases H2O2 and proton production. Hydrogen Peroxide 49-53 dual oxidase 2 Homo sapiens 0-5 26823467-0 2016 Dual Oxidase 2 (Duox2) Regulates Pannexin 1-mediated ATP Release in Primary Human Airway Epithelial Cells via Changes in Intracellular pH and Not H2O2 Production. Hydrogen Peroxide 146-150 dual oxidase 2 Homo sapiens 0-14 26823467-0 2016 Dual Oxidase 2 (Duox2) Regulates Pannexin 1-mediated ATP Release in Primary Human Airway Epithelial Cells via Changes in Intracellular pH and Not H2O2 Production. Hydrogen Peroxide 146-150 dual oxidase 2 Homo sapiens 16-21 26261005-1 2015 BACKGROUND & AIMS: Dual oxidase 2 (DUOX2), a hydrogen-peroxide generator at the apical membrane of gastrointestinal epithelia, is up-regulated in patients with inflammatory bowel disease (IBD) before the onset of inflammation, but little is known about its effects. Hydrogen Peroxide 49-66 dual oxidase 2 Homo sapiens 23-37 26261005-1 2015 BACKGROUND & AIMS: Dual oxidase 2 (DUOX2), a hydrogen-peroxide generator at the apical membrane of gastrointestinal epithelia, is up-regulated in patients with inflammatory bowel disease (IBD) before the onset of inflammation, but little is known about its effects. Hydrogen Peroxide 49-66 dual oxidase 2 Homo sapiens 39-44 25761904-3 2015 DUOX2 forms with its maturation factor, DUOX activator 2 (DUOXA2), a stable complex at the cell surface that is crucial for the H2O2-generating activity, but the nature of their interaction is unknown. Hydrogen Peroxide 128-132 dual oxidase 2 Homo sapiens 0-5