2019
Genetics and functions of the retinoic acid pathway, with special emphasis on the eye
Thompson B, Katsanis N, Apostolopoulos N, Thompson DC, Nebert DW, Vasiliou V. Genetics and functions of the retinoic acid pathway, with special emphasis on the eye. Human Genomics 2019, 13: 61. PMID: 31796115, PMCID: PMC6892198, DOI: 10.1186/s40246-019-0248-9.Peer-Reviewed Original ResearchConceptsRequirement of RAEmbryonic developmentRetinoic acidAnterior segment formationRetinoic acid pathwayRas signalingPotent morphogenEye developmentOptic cup formationPostnatal lethalitySegment formationAcid pathwayCup formationNormal developmentOptic vesicleMultistep processParacrine fashionPathwayRecent advancesMorphogensGenesGeneticsMutationsVesiclesLethalityExpression, 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 characteristicsResiduesUpdate on the human and mouse lipocalin (LCN) gene family, including evidence the mouse Mup cluster is result of an “evolutionary bloom”
Charkoftaki G, Wang Y, McAndrews M, Bruford EA, Thompson DC, Vasiliou V, Nebert DW. Update on the human and mouse lipocalin (LCN) gene family, including evidence the mouse Mup cluster is result of an “evolutionary bloom”. Human Genomics 2019, 13: 11. PMID: 30782214, PMCID: PMC6381713, DOI: 10.1186/s40246-019-0191-9.Peer-Reviewed Original ResearchConceptsMajor urinary protein genesKingdoms of lifeLipocalin gene familyGene familyMUP genesMouse genomeHuman genomeProtein geneChromosome 4Regulation of glucoseBarrel structurePhysiological processesΒ-strandsPhysiological functionsSecretory tissueGenesScent marksPseudogenesGenomeLipid metabolismBloomsEvidence pointsSyntenicImportant roleSteroid hormones
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
2015
Update of the human and mouse Fanconi anemia genes
Dong H, Nebert DW, Bruford EA, Thompson DC, Joenje H, Vasiliou V. Update of the human and mouse Fanconi anemia genes. Human Genomics 2015, 9: 32. PMID: 26596371, PMCID: PMC4657327, DOI: 10.1186/s40246-015-0054-y.Peer-Reviewed Original ResearchConceptsHUGO Gene Nomenclature CommitteeDNA repair pathwaysFanconi anemiaFanconi anemia (FA) complementation group proteinsRepair pathwaysFA DNA repair pathwayCommon DNA repair pathwaySet of genesFanconi anemia genesGene Nomenclature CommitteeNumber of genesFANC genesFA pathogenesisGenomic integrityEvolutionary phylogenyGroup proteinsMutant proteinsMouse orthologRoot symbolFA pathwayPhysiological functionsGenesBone marrow failureGenetic diseasesEvolutionary perspective
2013
Update of the human and mouse SERPINgene superfamily
Heit C, Jackson BC, McAndrews M, Wright MW, Thompson DC, Silverman GA, Nebert DW, Vasiliou V. Update of the human and mouse SERPINgene superfamily. Human Genomics 2013, 7: 22. PMID: 24172014, PMCID: PMC3880077, DOI: 10.1186/1479-7364-7-22.Peer-Reviewed Original ResearchConceptsHuman protein-coding genesMultiple paralogous genesProtein-coding genesParalogous genesSerine proteinase inhibitorFunctional genesSerpin geneIntracellular serpinsSerpin familyGenesProteinase inhibitorsSerpinsCancer metastasisFurther characterizationProteinTherapeutic targetChaperonesPseudogenesGenomeBlood clottingImmune functionPotential biomarkersInhibitorsTumorigenesisRoleALDH16A1 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 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 elementsCrystallins
2011
Update of the human secretoglobin (SCGB) gene superfamily and an example of 'evolutionary bloom' of androgen-binding protein genes within the mouse Scgb gene superfamily
Jackson BC, Thompson DC, Wright MW, McAndrews M, Bernard A, Nebert DW, Vasiliou V. Update of the human secretoglobin (SCGB) gene superfamily and an example of 'evolutionary bloom' of androgen-binding protein genes within the mouse Scgb gene superfamily. Human Genomics 2011, 5: 691. PMID: 22155607, PMCID: PMC3251818, DOI: 10.1186/1479-7364-5-6-691.Peer-Reviewed Original ResearchConceptsGene familyLarge gene familyNovel drug targetsMammalian lineagesProtein geneMammalian secretionsDrug targetsGenesMate selectionProteinSecretoglobinTissue repairBloomsBiological activityFamilyAndrogen-binding proteinPseudogenesHuman healthImportant roleModulation of inflammationLineagesSalivary glandsRoleTumorigenesisBetter understandingUpdate on the aldehyde dehydrogenase gene (ALDH) superfamily
Jackson B, Brocker C, Thompson DC, Black W, Vasiliou K, Nebert DW, Vasiliou V. Update on the aldehyde dehydrogenase gene (ALDH) superfamily. Human Genomics 2011, 5: 283. PMID: 21712190, PMCID: PMC3392178, DOI: 10.1186/1479-7364-5-4-283.Peer-Reviewed Original ResearchConceptsAldehyde dehydrogenase geneALDH genesDehydrogenase geneALDH family membersGene loss eventsBiotechnology Information gene databaseGamma-hydroxybutyric aciduriaWhole-genome sequencingCellular processesHuman genomeEnzymic detoxificationGene databaseExogenous aldehydesProtein sequencingType II hyperprolinaemiaCancer stem cellsEntire complementMolecular basisALDH enzymesGenesFamily membersStem cellsAldehyde metabolismRetinoic acidSjögren-Larsson syndrome