<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ogboo BC</submitter><funding>Associazione Italiana per la Ricerca sul Cancro</funding><funding>Airc Italian Foundation for Cancer Research</funding><funding>NHLBI NIH HHS</funding><funding>National Institutes of Health</funding><funding>State University of New York</funding><pagination>102298</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8956913</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>52</volume><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&lt;sub>2&lt;/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</pubmed_abstract><journal>Redox biology</journal><pubmed_title>Architecture of the NADPH oxidase family of enzymes.</pubmed_title><pmcid>PMC8956913</pmcid><funding_grant_id>R01 HL138708</funding_grant_id><funding_grant_id>R01 HL085646</funding_grant_id><funding_grant_id>IG19808</funding_grant_id><funding_grant_id>AG075491</funding_grant_id><funding_grant_id>HL085646</funding_grant_id><pubmed_authors>Maini A</pubmed_authors><pubmed_authors>van der Vliet A</pubmed_authors><pubmed_authors>Mattevi A</pubmed_authors><pubmed_authors>Scouten S</pubmed_authors><pubmed_authors>Grabovyy UV</pubmed_authors><pubmed_authors>Heppner DE</pubmed_authors><pubmed_authors>Ogboo BC</pubmed_authors></additional><is_claimable>false</is_claimable><name>Architecture of the NADPH oxidase family of enzymes.</name><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&lt;sub>2&lt;/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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jun</publication><modification>2025-04-04T22:04:22.776Z</modification><creation>2025-04-04T22:04:22.776Z</creation></dates><accession>S-EPMC8956913</accession><cross_references><pubmed>35334249</pubmed><doi>10.1016/j.redox.2022.102298</doi></cross_references></HashMap>