2016
ALDH3A1 Plays a Functional Role in Maintenance of Corneal Epithelial Homeostasis
Koppaka V, Chen Y, Mehta G, Orlicky DJ, Thompson DC, Jester JV, Vasiliou V. ALDH3A1 Plays a Functional Role in Maintenance of Corneal Epithelial Homeostasis. PLOS ONE 2016, 11: e0146433. PMID: 26751691, PMCID: PMC4708999, DOI: 10.1371/journal.pone.0146433.Peer-Reviewed Original ResearchConceptsCorneal cell proliferationCorneal epithelial homeostasisCell proliferationALDH3A1 expressionEpithelial homeostasisHuman corneal epithelial cell lineDouble knockout miceAnti-proliferation effectCorneal epithelial cell lineCorneal epithelial proliferationAldehyde dehydrogenase 1A1Epithelial cell lineCorneal differentiation markersInner ocular tissuesInverse associationFunctional roleEpithelial proliferationKnockout miceP53 expressionCorneal epitheliumOcular tissuesMouse corneaCalcium concentrationMRNA levelsEpithelial differentiation
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
2007
Interaction between the catalytic and modifier subunits of glutamate-cysteine ligase
Yang Y, Chen Y, Johansson E, Schneider SN, Shertzer HG, Nebert DW, Dalton TP. Interaction between the catalytic and modifier subunits of glutamate-cysteine ligase. Biochemical Pharmacology 2007, 74: 372-381. PMID: 17517378, DOI: 10.1016/j.bcp.2007.02.003.Peer-Reviewed Original ResearchConceptsGlutamate-cysteine ligaseHeterodimer formationEnzyme structure-function relationshipsTwo-hybrid systemGlutathione biosynthesis pathwayPrimary amino acid sequenceC-terminal regionAmino acid sequenceN-terminal regionStructure-function relationshipsBiosynthesis pathwayRegulatory subunitCatalytic subunitDeletion analysisRate-limiting enzymeTertiary structureModifier subunitAmino acidsPoint mutationsSubunitsGCLCGSH inhibitionLigaseEnzyme activityGCLM