Ask about this productRelated genes to: NOX1 antibody
- Gene:
- DUOX1 NIH gene
- Name:
- dual oxidase 1
- Previous symbol:
- -
- Synonyms:
- NOXEF1, THOX1, LNOX1
- Chromosome:
- 15q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-30
- Date modifiied:
- 2016-01-15
- Gene:
- NOX1 NIH gene
- Name:
- NADPH oxidase 1
- Previous symbol:
- -
- Synonyms:
- NOH1, NOH-1, MOX1, GP91-2
- Chromosome:
- Xq22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-03-24
- Date modifiied:
- 2016-10-05
Related products to: NOX1 antibody
Related articles to: NOX1 antibody
- The seven isoforms of the NADPH oxidase (NOX) family-NOX1-5, DUOX1, and DUOX2-are multidomain enzymes that require distinct regulatory subunits for activation. These enzymes are major sources of reactive oxygen species (ROS), particularly the superoxide anion (O2·-), which exerts both cytotoxic and signalling effects. NADPH acts as a critical electron donor, maintaining cellular redox homeostasis and supporting anabolic metabolism. Dysregulated NOX activity has been linked to metabolic reprogramming in cancer and oxidative stress-induced complications in diabetes mellitus. - Source: PubMed
Publication date: 2026/08/27
Aziz NamraWal AnkitaAlvi InshrahTiwari SakshiYadav Ritu RaniSharma AayushKhan AbidaTandey Roshni - Nicotinamide adenine dinucleotide phosphate hydrogen (NADPH) oxidase is an important family of enzymes that produce reactive oxygen species (ROS) and consists of NOX1-5, DUOX1, and DUOX2. These enzymes exhibit diverse tissue distributions with different activation mechanisms involved. They play vital roles in several physiological processes, such as defense against pathogens, wound healing, regulation of gene expression, post-translational modification of proteins, cell signaling, and cell differentiation. The present review highlights an indispensable role of NOX expression and resulting ROS production on various biological processes, specifically focusing on cell differentiation at various stages of embryonic development and differentiation of monocytes to macrophages within the mononuclear phagocytic system. It also discusses the influence of altered expression of NOX isoforms on the fate of macrophage polarization either towards pro-inflammatory (M1) or anti-inflammatory (M2) macrophages. Additionally, it discusses how the dysregulation of the cellular expression of NOXs is involved in the development and progression of a variety of chronic human diseases including cardiovascular diseases, cancer, diabetes, neurological diseases, and autoimmune disorders. - Source: PubMed
Prasad AnkushKushwaha RenuAlugoju PhaniendraPospíšil PavelRathi Deepak - The NADPH oxidase (NOX) family comprises integral membrane-bound enzymes responsible for generating reactive oxygen species (ROS), with critical roles in immune defense, vascular regulation, and cellular signaling. However, their intrinsic hydrophobicity and membrane association created longstanding challenges for extensive research. In this study, we applied the QTY code - a simple protein design strategy that replaces hydrophobic residues leucine (L), isoleucine (I), valine (V), and phenylalanine (F) with hydrophilic yet structurally compatible residues glutamine (Q), threonine (T) and tyrosine (Y) - to generate QTY analogs of NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, DUOXA1 and CYBA with reduced hydrophobicity. Using AlphaFold 3, we predicted and superposed the structures of native and QTY-engineered analog proteins. Our results show strong structural resemblance between each pair, with root mean square deviation (RMSD) values below 1Å for six out of eight proteins examined. In addition, QTY substitution significantly reduced surface hydrophobicity, indicating improved water-solubility while preserving 3D structural fold integrity. Our findings demonstrate the potential of QTY-designed NOX variants with reduced hydrophobicity as surrogates for use in structural biology, monoclonal antibody discoveries, drug discovery, and other applications where native membrane proteins present experimental limitations. - Source: PubMed
Publication date: 2026/06/10
Hu TutuCheng RickChen EdwardZhang Shuguang - Lung adenocarcinoma (LUAD) is the pathological type with the highest proportion and heterogeneity in lung cancer. NADPH oxidase is an important enzyme in the biological respiratory chain that plays a decisive role in cell growth, regulation, and apoptosis, which translating seven gene families, namely NOX1-5 and DUOX1-2. The current study aimed to investigate the expression, and prognostic and immune-related roles of this gene family in early and advanced LUAD. Gene expression was examined using the Oncomine™ database, prognostic value was analyzed by Kaplan-Meier analysis, expression of NOX2 and NOX4 in early and locally advanced LUAD was validated using RT-qPCR, and the correlation of infiltrating immune cells was validated by tumor immune estimation resources (TIMER). Over-expressed NOX4 was associated with lower prognosis; NOX2 was found to be under-expressed in LUAD. Both NOX2 and NOX4 expression was positively related to tumor purity and had positive correlation with infiltrating levels of immune cells in TIMER. The data reflected the potential association of NADPH oxidase in early and locally advanced lung adenocarcinoma. Our data suggested that the combination of NOX4 suppression, NOX2 depression, and immunotherapy would improve clinical outcome in these tumors. - Source: PubMed
Publication date: 2026/06/10
Deng JingjingCao LinfengHou GouxinMa Xiaolong - Osteoporosis, the most prevalent skeletal disorder, is primarily driven by aberrantly increased osteoclast formation and/or activity. Targeting hyperactive osteoclasts remains the cornerstone of current therapeutic strategies. Crebanine (Cre), a natural isoquinoline-derived alkaloid with diverse pharmacological activities, has not yet been explored for osteoporosis treatment. This study aimed to evaluate the therapeutic potential of Cre against ovariectomy (OVX)-induced osteoporosis and elucidate its underlying mechanisms. Cre dose-dependently inhibited osteoclast differentiation, actin ring formation, and bone resorption by downregulating nuclear factor of activated T cells 1 (NFATc1) and key osteoclast-related genes. Simultaneously, Cre enhanced osteoblast differentiation and mineralization, upregulated osteoblast marker genes, and restored hydrogen peroxide-impaired alkaline phosphatase (ALP) activity impaired by hydrogen peroxide, indicating dual regulation of bone remodeling. Mechanistically, Cre activated sirtuin 1 (Sirt1), promoting p65 deacetylation, inactivated IκB kinase (IKK), and stabilized IκBα, thus inhibiting nuclear factor-kappaB (NF-κB) signaling. Additionally, Cre reduced reactive oxygen species (ROS) by upregulating antioxidant enzymes (heme oxygenase-1 (HO-1), catalase) and suppressing nicotinamide adenine dinucleotide (NAD) phosphate (NADPH) oxidases (NOX1/4). Furthermore, Cre specifically bound to the predicted site of receptor activator of NF-κB (RANK), blocking RANK ligand (RANKL)-RANK interaction and disrupting downstream protein kinase B (Akt) and mitogen-activated protein kinase (MAPK) signaling pathways. In the OVX mouse model, Cre significantly attenuated bone loss and osteoclastogenesis. Crucially, Cre showed no toxicity in liver or kidney function tests. Collectively, these findings demonstrate that Cre exerts dual therapeutic effects, inhibiting osteoclastogenesis via Sirt1-mediated NF-κB/ROS suppression and promoting osteoblast activity, providing a promising therapeutic strategy for osteoporosis. - Source: PubMed
Publication date: 2025/07/31
Zhang HaojieZhao XuanWang ZhengMiao JiansenHu XinliCui PengJin ChenZhao XibinLiang HaiboYe HantaoXu YiningChen XiaolongWang WeiLu Shibao