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 mutantGenesALDH1B1HeterotetramerizationGenome
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-Ionization