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
2013
An Inhibitory Antibody Blocks the First Step in the Dithiol/Disulfide Relay Mechanism of the Enzyme QSOX1
Grossman I, Alon A, Ilani T, Fass D. An Inhibitory Antibody Blocks the First Step in the Dithiol/Disulfide Relay Mechanism of the Enzyme QSOX1. Journal Of Molecular Biology 2013, 425: 4366-4378. PMID: 23867277, DOI: 10.1016/j.jmb.2013.07.011.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibodies, BlockingAntibodies, MonoclonalBinding SitesCell AdhesionCell MovementDisulfidesHumansKineticsModels, MolecularMolecular Sequence DataMultiprotein ComplexesOxidoreductases Acting on Sulfur Group DonorsProtein BindingProtein ConformationProtein Interaction Domains and MotifsSingle-Chain AntibodiesTolueneConceptsQuiescin sulfhydryl oxidase 1Catalyst of disulfide bond formationIntegrin-mediated cell survivalExtracellular matrixSulfhydryl oxidase 1Single-chain variantDisulfide bond formationOxidase domainTumor cell adhesionTight-binding inhibitorProtein dissectionSulfhydryl oxidase activityExtracellular matrix compositionOver-producedCell migrationCell survivalLaminin isoformsRecombinant versionCell adhesionInhibitory antibodiesCultured fibroblastsPotential therapeutic applicationsOxidase activityEnzymeLamininA Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function
Ilani T, Alon A, Grossman I, Horowitz B, Kartvelishvily E, Cohen S, Fass D. A Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function. Science 2013, 341: 74-76. PMID: 23704371, DOI: 10.1126/science.1238279.Peer-Reviewed Original ResearchConceptsQuiescin sulfhydryl oxidase 1Disulfide bond formationEndoplasmic reticulumExtracellular matrixCell-matrix adhesionSulfhydryl oxidase 1Extracellular catalysisGolgi apparatusEnzyme familyExtracellular matrix propertiesSecretory proteinsExtracellular matrix compositionInhibitory monoclonal antibodiesCysteine cross-linkingIncorporation of lamininCell migrationPhysiological functionsDisulfide catalystsMonoclonal antibodiesGolgiBond formationReticulumEnzymeProteinLaminin
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