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View Article and Find Full Text PDFThe corrosion inhibitive capabilities of some ferrocene-based Schiff bases on aluminium alloy AA2219-T6 in acidic medium were investigated using Tafel polarization, electrochemical impedance spectroscopy (EIS), weight loss measurement, FT-IR spectroscopy and scanning electron microscopic (SEM) techniques. The influence of molecular configuration on the corrosion inhibition behavior has been explored by quantum chemical calculation. Ferrocenyl Schiff bases 4,4'-((((ethane-1,2-diylbis(oxy))bis(4,1-phenylene))bis(methaneylylidene))bis(azaneylylidene))bisferrocene (Fcua), 4,4'-((((ethane-1,2-diylbis(oxy))bis(2-methoxy-1,4-phenylene))bis(methaneylylidene))bis(azaneylylidene))bisferrocene (Fcub) and 4,4'-((((ethane-1,2-diylbis(oxy))bis(2-ethoxy-1,4-phenylene))bis(methaneylylidene))bis(azaneylylidene))bisferrocene (Fcuc) have been synthesized and characterized by FT-IR, H and C NMR spectroscopic studies.
View Article and Find Full Text PDFDuring mitosis, Bub1 kinase phosphorylates histone H2A-T120 to promote centromere sister chromatid cohesion through recruitment of shugoshin (Sgo) proteins. The regulation and dynamics of H2A-T120 phosphorylation are poorly understood. Using quantitative phosphoproteomics we show that Bub1 is autophosphorylated at numerous sites.
View Article and Find Full Text PDFKnl1 (also known as CASC5, UniProt Q8NG31) is an evolutionarily conserved scaffolding protein that is required for proper kinetochore assembly, spindle assembly checkpoint (SAC) function and chromosome congression. A number of recent reports have confirmed the prominence of Knl1 in these processes and provided molecular details and structural features that dictate Knl1 functions in higher organisms. Knl1 recruits SAC components to the kinetochore and is the substrate of certain protein kinases and phosphatases, the interplay of which ensures the exquisite regulation of the aforementioned processes.
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