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
2018
Aldehyde Dehydrogenases☆
Vasiliou V, Thompson D, Petersen D. Aldehyde Dehydrogenases☆. 2018, 146-163. DOI: 10.1016/b978-0-12-801238-3.99183-9.Peer-Reviewed Original ResearchAldehyde dehydrogenasesAldehyde dehydrogenase geneType II hyperprolinemiaTransgenic knockout mouse modelKnockout mouse modelHuman genomeHigh aldehyde dehydrogenase (ALDH) activityDehydrogenase geneExogenous aldehydesCancer stem cellsMolecular basisPhysiological processesDependent enzymesAldehyde dehydrogenase activityMicrophthalmia/anophthalmiaAldehyde dehydrogenaseStem cellsOxidative damageDehydrogenasesSjögren-Larsson syndromeGenesDehydrogenase activityLate-onset Alzheimer's diseasePivotal roleOxidation of aldehydes
2012
Aldehyde dehydrogenases: From eye crystallins to metabolic disease and cancer stem cells
Vasiliou V, Thompson DC, Smith C, Fujita M, Chen Y. Aldehyde dehydrogenases: From eye crystallins to metabolic disease and cancer stem cells. Chemico-Biological Interactions 2012, 202: 2-10. PMID: 23159885, PMCID: PMC4128326, DOI: 10.1016/j.cbi.2012.10.026.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsAldehyde dehydrogenaseHuman ALDH genesALDH gene familyNon-catalytic activitiesEukaryotic genomesGene familyALDH genesCancer stem cellsMolecular basisDependent enzymesStem cellsAldehyde metabolismOxidative stressNicotinamide adenine dinucleotideOxidation of aldehydesPathophysiological processesAdenine dinucleotideDehydrogenaseMetabolic diseasesGenomeImportant roleEmbryogenesisGenesStructural elementsCrystallinsOcular aldehyde dehydrogenases: Protection against ultraviolet damage and maintenance of transparency for vision
Chen Y, Thompson DC, Koppaka V, Jester JV, Vasiliou V. Ocular aldehyde dehydrogenases: Protection against ultraviolet damage and maintenance of transparency for vision. Progress In Retinal And Eye Research 2012, 33: 28-39. PMID: 23098688, PMCID: PMC3570594, DOI: 10.1016/j.preteyeres.2012.10.001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsAldehyde dehydrogenasePutative regulatory functionTaxon-specific mannerNon-catalytic functionsRetinoic acid signalingALDH proteinsMaintenance of transparencyCellular transparencyAcid signalingCorneal crystallinsExogenous aldehydesEye developmentOxygen-induced damageCorneal cell proliferationStructural roleRegulatory functionsException of rabbitsMost mammalsRetinaldehyde dehydrogenasesLens crystallinsALDH1A1 proteinMammalian corneaAnimal speciesCell proliferationDependent oxidation
2011
Ultraviolet Radiation: Cellular Antioxidant Response and the Role of Ocular Aldehyde Dehydrogenase Enzymes
Marchitti SA, Chen Y, Thompson DC, Vasiliou V. Ultraviolet Radiation: Cellular Antioxidant Response and the Role of Ocular Aldehyde Dehydrogenase Enzymes. Eye & Contact Lens Science & Clinical Practice 2011, 37: 206-213. PMID: 21670692, PMCID: PMC3356694, DOI: 10.1097/icl.0b013e3182212642.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsReactive oxygen speciesCombat reactive oxygen speciesImportant enzymatic antioxidantsAldehyde dehydrogenaseReduction-oxidation homeostasisOxidative damageConstant oxidative stressAldehyde dehydrogenase enzymeCellular antioxidant responseOxidative stressUnique roleCellular membranesCellular responsesAntioxidant defense systemSuperoxide dismutasesAntioxidant responseEnvironmental insultsDownstream effectsDefense systemGlutathione reductaseEnzymatic antioxidantsOxygen speciesDehydrogenase enzymeNicotinamide adenine dinucleotide phosphateNonenzymatic antioxidants
2010
Aldehyde Dehydrogenase 1B1: Molecular Cloning and Characterization of a Novel Mitochondrial Acetaldehyde-Metabolizing Enzyme
Stagos D, Chen Y, Brocker C, Donald E, Jackson BC, Orlicky DJ, Thompson DC, Vasiliou V. Aldehyde Dehydrogenase 1B1: Molecular Cloning and Characterization of a Novel Mitochondrial Acetaldehyde-Metabolizing Enzyme. Drug Metabolism And Disposition 2010, 38: 1679-1687. PMID: 20616185, PMCID: PMC2957164, DOI: 10.1124/dmd.110.034678.Peer-Reviewed Original ResearchMeSH KeywordsAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsBaculoviridaeBlotting, WesternCell LineCloning, MolecularEthanolGenetic VectorsHumansImmunohistochemistryInsectaMaleMiceMice, Inbred C57BLMice, KnockoutMitochondriaMolecular Sequence DataNADOrgan SpecificityOxidation-ReductionPlasmidsRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationConceptsEthanol-induced damageRecent population studiesQuantitative polymerase chain reactionPolymerase chain reactionAldehyde dehydrogenase
1995
Apparent monomorphism of ALDH2 in seven American Indian populations
Novoradovsky A, Kidd J, Kidd K, Goldman D. Apparent monomorphism of ALDH2 in seven American Indian populations. Alcohol 1995, 12: 163-167. PMID: 7772269, DOI: 10.1016/0741-8329(94)00086-7.Peer-Reviewed Original ResearchConceptsNew World populationsSouth American Indian populationsALDH2 geneMitochondrial aldehyde dehydrogenaseNorth American populationsALDH2 cDNAALDH2 functionRestriction endonucleasesAldehyde dehydrogenaseConformation polymorphism techniqueSouth American IndiansGenesAllele-specific amplificationAllelesStudied individualsPolymorphism techniquePolymorphismAmerican populationFragmentsAmerican Indian populationsCDNAALDH2EndonucleaseVariantsPopulation
1989
Phenobarbital-inducible Aldehyde Dehydrogenase in the Rat cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats
Dunn TJ, Koleske AJ, Lindahl R, Pitot HC. Phenobarbital-inducible Aldehyde Dehydrogenase in the Rat cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats. Journal Of Biological Chemistry 1989, 264: 13057-13065. PMID: 2753900, DOI: 10.1016/s0021-9258(18)51595-7.Peer-Reviewed Original ResearchConceptsComplete nucleotide sequenceSpecific gene expressionAldehyde dehydrogenaseAmino acid sequenceGlutathione S-transferase YaRat cDNA sequenceStrong conservationCDNA sequenceNucleotide sequenceMRNA speciesAcid sequenceGene expressionCytosolic isozymeMolecular massAmino acidsCytochrome P-450eMultiple pathwaysMRNAResponsive allelesMRNA levelsSequenceRegulationCytochrome P-450bDehydrogenaseP-450e
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