A Ce(III) phosphinate and a Ce(IV) phosphostibonate have been assembled by the reaction of a phosphinic acid and phosphostibonate with Ce(III) salts. Single crystal X-ray diffraction (SCXRD) studies reveal the formation of a rare triangular Ce(III) oxo-cluster [Ce(PhCHPO)]Cl(CHOH)(HO)] () and a fascinating hexanuclear oxo-cluster containing Ce(IV) ions [Ce (-ClCHSb)(μ-O)(μ-O)(-BuPO)(μ-OCH)] (). The molecular architecture of showcased an interesting correlation with platonic solids, wherein the Ce(IV), Sb(V), and P(V) ions were found to be present in vertices of an octahedron, a tetrahedron, and a cube, respectively.
View Article and Find Full Text PDFBackground: Kidney fibrosis is a hallmark of chronic kidney disease (CKD) and compromises the viability of transplanted human bone marrow-derived mesenchymal stromal cells (BM-MSCs). Hence, BM-MSCs were genetically-engineered to express the anti-fibrotic and renoprotective hormone, human relaxin-2 (RLX) and green fluorescent protein (BM-MSCs-eRLX + GFP), which enabled BM-MSCs-eRLX + GFP delivery via a single intravenous injection.
Methods: BM-MSCs were lentiviral-transduced with human relaxin-2 cDNA and GFP, under a eukaryotic translation elongation factor-1α promoter (BM-MSCs-eRLX + GFP) or GFP alone (BM-MSCs-eGFP).
Inspired by the intriguing nature of the metal-π interaction in organometallic chemistry, a novel 1D hybrid material has been designed. Herein, a functionalized tellurium allyl macrocycle (TAM) acts as a molecular building block and is knit together via silver-π interaction to obtain Ag-TAM. Ag is coordinated to two allyl groups and a phenyl ring in η mode.
View Article and Find Full Text PDFUnlabelled: Some negative-sense RNA viruses, including measles virus (MeV), share the characteristic that during their infection cycle, cytoplasmic inclusion bodies (IBs) are formed where components of the viral replication machinery are concentrated. As a foci of viral replication, how IBs act to enhance the efficiency of infection by affecting virus-host interactions remains an important topic of investigation. We previously established that upon MeV infection, the epigenetic host protein, WD repeat-containing protein 5 (WDR5), translocates to cytoplasmic viral IBs and facilitates MeV replication.
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