{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ogboo BC"],"funding":["Associazione Italiana per la Ricerca sul Cancro","Airc Italian Foundation for Cancer Research","NHLBI NIH HHS","National Institutes of Health","State University of New York"],"pagination":["102298"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8956913"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52"],"pubmed_abstract":["The NADPH Oxidases (NOX) catalyze the deliberate production of reactive oxygen species (ROS) and are established regulators of redox-dependent processes across diverse biological settings. Proper management of their activity is controlled through a conserved electron transfer (ET) cascade from cytosolic NADPH substrate through the plasma membrane to extracellular O<sub>2</sub>. After decades-long investigations of their biological functions, including potential as drug targets, only very recently has atomic-resolution information of NOX enzymes been made available. In this graphical review, we summarize the present structural biology understanding of the NOX enzymes afforded by X-ray crystallography and cryo-electron microscopy. Combined molecular-level insights predominantly informed by D"],"journal":["Redox biology"],"pubmed_title":["Architecture of the NADPH oxidase family of enzymes."],"pmcid":["PMC8956913"],"funding_grant_id":["R01 HL138708","R01 HL085646","IG19808","AG075491","HL085646"],"pubmed_authors":["Maini A","van der Vliet A","Mattevi A","Scouten S","Grabovyy UV","Heppner DE","Ogboo BC"],"additional_accession":[]},"is_claimable":false,"name":"Architecture of the NADPH oxidase family of enzymes.","description":"The NADPH Oxidases (NOX) catalyze the deliberate production of reactive oxygen species (ROS) and are established regulators of redox-dependent processes across diverse biological settings. Proper management of their activity is controlled through a conserved electron transfer (ET) cascade from cytosolic NADPH substrate through the plasma membrane to extracellular O<sub>2</sub>. After decades-long investigations of their biological functions, including potential as drug targets, only very recently has atomic-resolution information of NOX enzymes been made available. In this graphical review, we summarize the present structural biology understanding of the NOX enzymes afforded by X-ray crystallography and cryo-electron microscopy. Combined molecular-level insights predominantly informed by D","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2025-04-04T22:04:22.776Z","creation":"2025-04-04T22:04:22.776Z"},"accession":"S-EPMC8956913","cross_references":{"pubmed":["35334249"],"doi":["10.1016/j.redox.2022.102298"]}}