2018
cis‐Proline mutants of quiescin sulfhydryl oxidase 1 with altered redox properties undermine extracellular matrix integrity and cell adhesion in fibroblast cultures
Javitt G, Grossman‐Haham I, Alon A, Resnick E, Mutsafi Y, Ilani T, Fass D. cis‐Proline mutants of quiescin sulfhydryl oxidase 1 with altered redox properties undermine extracellular matrix integrity and cell adhesion in fibroblast cultures. Protein Science 2018, 28: 228-238. PMID: 30367560, PMCID: PMC6295897, DOI: 10.1002/pro.3537.Peer-Reviewed Original ResearchConceptsQuiescin sulfhydryl oxidase 1Protein disulfide isomeraseSulfhydryl oxidase 1Thioredoxin superfamilyCatalyst of disulfide bond formationDisulfide isomeraseCis-prolineProtein disulfide isomerase familyEffects of such mutationsThioredoxin-fold proteinsCell adhesionAmino acidsEffects of mutationsExtracellular matrix assemblyCanonical amino acidsActive-site regionDisulfide bond formationRedox-active enzymesSuperfamily enzymesSequence homologyFibroblast culturesBacterial enzymesMutated residuesMutantsDistant member
2012
Catalysis of Disulfide Bond Formation by the Quiescin Sulfhydryl Oxidases
Alon A, Fass D. Catalysis of Disulfide Bond Formation by the Quiescin Sulfhydryl Oxidases. 2012 DOI: 10.1002/9780470015902.a0024168.Peer-Reviewed Original ResearchQuiescin sulfhydryl oxidase enzymesQuiescin sulfhydryl oxidaseDisulfide bond formationSubstrate proteinsProtein disulfide isomerase family proteinsSulfhydryl oxidaseProtein disulfide isomerase familyCatalysis of disulfide bond formationDithiol/disulfide exchange reactionsRedox-active disulfideDisulfide isomerase familyExtracellular matrix assemblyHigh-resolution viewSecretory pathwayFamily proteinsSuperfamily proteinsCatalytic machineryDomain duplicationExtracellular environmentMatrix assemblyRedox relayEnzymeProteinSide-chain dynamicsDisulfide bonds
2010
QSOX contains a pseudo‐dimer of functional and degenerate sulfhydryl oxidase domains
Alon A, Heckler E, Thorpe C, Fass D. QSOX contains a pseudo‐dimer of functional and degenerate sulfhydryl oxidase domains. FEBS Letters 2010, 584: 1521-1525. PMID: 20211621, DOI: 10.1016/j.febslet.2010.03.001.Peer-Reviewed Original ResearchConceptsQuiescin sulfhydryl oxidaseSubstrate proteinsCatalyzes formation of disulfide bondsSulfhydryl oxidaseProtein disulfide isomerase familyDisulfide isomerase familyFormation of disulfide bondsOxidase domainMonomeric enzymeERV familiesCysteine residuesCatalyze formationQuaternary structurePseudo-dimerDisulfide formationDisulfide bondsEnzymeProteinSubunitOxidaseCatalytic activityCrystal structureQSOX1CofactorFamily
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