2012
Aldehyde dehydrogenases in cellular responses to oxidative/electrophilicstress
Singh S, Brocker C, Koppaka V, Chen Y, Jackson BC, Matsumoto A, Thompson DC, Vasiliou V. Aldehyde dehydrogenases in cellular responses to oxidative/electrophilicstress. Free Radical Biology And Medicine 2012, 56: 89-101. PMID: 23195683, PMCID: PMC3631350, DOI: 10.1016/j.freeradbiomed.2012.11.010.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAldehyde DehydrogenaseAnimalsBacteriaCaenorhabditis elegansHumansNeoplastic Stem CellsOxidative StressPlantsReactive Oxygen SpeciesSaccharomyces cerevisiaeConceptsReactive oxygen speciesOxidative stressMulticellular speciesEukaryotic organismsElectrophilic stressExogenous aldehydesCancer stem cellsLiving systemsStress responseCellular responsesEnvironmental stressorsSimilar functionsAldehyde scavengerSpeciesStem cellsLipid peroxidationROS loadOxygen speciesElevated oxidative stressLipid membranesALDHALDH expressionOrganismsPathological processesPathological conditions
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 ResearchMeSH KeywordsCatalysisCatalytic DomainDimerizationGlutamate-Cysteine LigaseGlutathioneProtein SubunitsSaccharomyces cerevisiaeStructure-Activity RelationshipTwo-Hybrid System TechniquesConceptsGlutamate-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