2016
Corneal haze phenotype in Aldh3a1-null mice: In vivo confocal microscopy and tissue imaging mass spectrometry
Chen Y, Jester JV, Anderson DM, Marchitti SA, Schey KL, Thompson DC, Vasiliou V. Corneal haze phenotype in Aldh3a1-null mice: In vivo confocal microscopy and tissue imaging mass spectrometry. Chemico-Biological Interactions 2016, 276: 9-14. PMID: 28038895, DOI: 10.1016/j.cbi.2016.12.017.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAnimalsCorneaCorneal DiseasesCorneal StromaDiazepam Binding InhibitorDisease Models, AnimalDynamic Light ScatteringEpitheliumEpithelium, CornealHistonesLens, CrystallineLipidsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalPhenotypeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationConceptsImaging mass spectrometryCorneal crystallinsNon-catalytic functionsAcyl-CoA binding proteinFirst genetic animal modelCellular transparencyCorneal epithelial homeostasisCorneal hazeEndogenous proteinsKO miceLipid localizationMixed genetic backgroundKnockout miceCorneal phenotypeEpithelial homeostasisProtein profilesWild-type corneasBinding proteinFunctional roleGenetic backgroundLens cataractMass spectrometryConfocal microscopyMolecular changesPhenotype
2010
Structural and Functional Modifications of Corneal Crystallin ALDH3A1 by UVB Light
Estey T, Chen Y, Carpenter JF, Vasiliou V. Structural and Functional Modifications of Corneal Crystallin ALDH3A1 by UVB Light. PLOS ONE 2010, 5: e15218. PMID: 21203538, PMCID: PMC3006428, DOI: 10.1371/journal.pone.0015218.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAnimalsCatalytic DomainChromatography, High Pressure LiquidCrystallinsCysteineHumansKineticsOxidative StressPeptidesProtein ConformationRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpectrophotometryUltraviolet RaysConceptsActive site CysNon-native aggregationNon-covalent interactionsAldehyde dehydrogenase 3A1MALDI-TOF mass spectrometryMammalian corneal epitheliumCorneal crystallinsSpectroscopic studiesChemical modificationUV-induced damageCys residuesGlucose-6-phosphate dehydrogenaseTertiary structureMass spectrometryMultifaceted roleResult of aggregationALDH3A1Enzymatic activityCorneal proteinsUV-induced inactivationOxidative stressProteinFunctional modificationsResiduesDirect absorptionAldehyde 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