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 ResearchConceptsActive 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 absorption
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