2019
Expression, purification and crystallization of the novel Xenopus tropicalis ALDH16B1, a homologue of human ALDH16A1
Pantouris G, Dioletis E, Chen Y, Thompson DC, Vasiliou V, Lolis EJ. Expression, purification and crystallization of the novel Xenopus tropicalis ALDH16B1, a homologue of human ALDH16A1. Chemico-Biological Interactions 2019, 304: 168-172. PMID: 30894314, PMCID: PMC6746316, DOI: 10.1016/j.cbi.2019.03.009.Peer-Reviewed Original ResearchConceptsAldehyde dehydrogenaseCritical Cys residuesPreliminary crystallographic analysisGenomic analysisSf9 cellsCys residuesALDH16A1Novel familyLower animalsSize exclusion chromatographyActive siteStructure determinationMetabolomics studiesCrystallographic analysisCellsMammalsHomologuesGenesExclusion chromatographyFishStructural characteristicsFrogsPathogenesis of goutUnique structural characteristicsResidues
2014
Human ALDH1B1 Polymorphisms may Affect the Metabolism of Acetaldehyde and All-trans retinaldehyde—In Vitro Studies and Computational Modeling
Jackson BC, Reigan P, Miller B, Thompson DC, Vasiliou V. Human ALDH1B1 Polymorphisms may Affect the Metabolism of Acetaldehyde and All-trans retinaldehyde—In Vitro Studies and Computational Modeling. Pharmaceutical Research 2014, 32: 1648-1662. PMID: 25413692, PMCID: PMC4382438, DOI: 10.1007/s11095-014-1564-3.Peer-Reviewed Original ResearchAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAldehydesAmino Acid SequenceComputer SimulationHumansModels, BiologicalModels, MolecularMolecular Sequence DataNitroglycerinPolymorphism, GeneticProtein ConformationRetinaldehydeSubstrate Specificity
2013
ALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1
Vasiliou V, Sandoval M, Backos DS, Jackson BC, Chen Y, Reigan P, Lanaspa MA, Johnson RJ, Koppaka V, Thompson DC. ALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1. Chemico-Biological Interactions 2013, 202: 22-31. PMID: 23348497, PMCID: PMC3746320, DOI: 10.1016/j.cbi.2012.12.018.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsSingle nucleotide polymorphismsSuch protein-protein interactionsCoiled-coil domainImportant cysteine residuesMissense single nucleotide polymorphismMost mammalian speciesALDH domainHuman cell linesALDH16A1Cysteine residuesMammalian speciesProtein structureUnique memberKey enzymeEtiology of goutGenesNucleotide polymorphismsHPRT activityProteinAcid metabolismCell linesLong formIntriguing possibilityLower animals
2012
Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2
Jackson BC, Holmes RS, Backos DS, Reigan P, Thompson DC, Vasiliou V. Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2. Chemico-Biological Interactions 2012, 202: 11-21. PMID: 23247008, PMCID: PMC3687035, DOI: 10.1016/j.cbi.2012.11.022.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsAnuraComputer SimulationEvolution, MolecularGenomicsHumansMiceModels, MolecularMolecular Sequence DataPhylogenyProtein Interaction Domains and MotifsProtein Structure, TertiarySequence AlignmentConceptsMitochondrial enzymesGenomes of birdsRepresentative vertebrate speciesProtein-protein interactionsAmino acid sequenceVertebrate genomesComparative genomicsMolecular evolutionALDH2 geneEarly vertebratesVertebrate speciesPhylogenetic analysisBioinformatics analysisAcid sequenceMammalian speciesSubunit sequencesBiological aldehydesHuman ALDH2Coenzyme bindingInactivating mutationALDH2 mutantGenesALDH1B1HeterotetramerizationGenomeAldehyde Dehydrogenase Inhibitors: a Comprehensive Review of the Pharmacology, Mechanism of Action, Substrate Specificity, and Clinical Application
Koppaka V, Thompson DC, Chen Y, Ellermann M, Nicolaou KC, Juvonen RO, Petersen D, Deitrich RA, Hurley TD, Vasiliou V. Aldehyde Dehydrogenase Inhibitors: a Comprehensive Review of the Pharmacology, Mechanism of Action, Substrate Specificity, and Clinical Application. Pharmacological Reviews 2012, 64: 520-539. PMID: 22544865, PMCID: PMC3400832, DOI: 10.1124/pr.111.005538.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsRetinoic acid signalingSuperfamily of enzymesCellular defense mechanismsALDH isozymesCellular homeostasisMechanism of actionAcid signalingCorneal crystallinsSubstrate specificityIsozyme-selective inhibitorsALDH enzymesToxicological functionsKey enzymeHuman ALDHHuman diseasesHuman cancersDefense mechanismsPharmacological inhibitionToxicological roleReactive aldehydesALDH inhibitorsIsozymesEnzymeUltraviolet radiation-induced damagePivotal role