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
2009
Control of extracellular matrix assembly along tissue boundaries via Integrin and Eph/Ephrin signaling
Jülich D, Mould AP, Koper E, Holley SA. Control of extracellular matrix assembly along tissue boundaries via Integrin and Eph/Ephrin signaling. Development 2009, 136: 2913-2921. PMID: 19641014, DOI: 10.1242/dev.038935.Peer-Reviewed Original Research
2006
Reconstructing and Deconstructing Agonist-Induced Activation of Integrin αIIbβ3
Han J, Lim CJ, Watanabe N, Soriani A, Ratnikov B, Calderwood DA, Puzon-McLaughlin W, Lafuente EM, Boussiotis VA, Shattil SJ, Ginsberg MH. Reconstructing and Deconstructing Agonist-Induced Activation of Integrin αIIbβ3. Current Biology 2006, 16: 1796-1806. PMID: 16979556, DOI: 10.1016/j.cub.2006.08.035.Peer-Reviewed Original ResearchConceptsIntegrin activationIntegrin affinityIntegrin beta cytoplasmic domainsIntegrin-associated complexesAgonist stimulationBeta cytoplasmic domainsIntegrin activation pathwaysProtein kinase CalphaExtracellular matrix assemblyBinding of talinSiRNA-mediated knockdownTumor cell metastasisRap effectorMulticellular animalsPhorbol myristate acetateSynthetic geneticsCytoplasmic domainRap1 GTPaseTransmembrane alphaActivation complexCytoskeletal proteinsTalinBeta subunitIntegrin αIIbβ3Cell adhesion
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