Egy 14. századi új Salamon: V. (Bölcs) Károly francia király

The result of in-hospital all mortality (P < 0.001; RR 3.23; 95% CI 2.28–4.57). (DOCX 54 kb

DataSheet1_In-situ reconstruction of CoBOx enables formation of Co for synthesis of benzylamine through reductive amination.docx

Cobalt (Co) as a substitute of noble-metal catalysts shows high catalytic capability for production of the widely used primary amines through the reductive amination. However, the synthesis of Co catalysts usually involves the introduction of organic compounds and the high-temperature pyrolysis, which is complicated and difficult for large-scale applications. Herein, we demonstrated a facile and efficient strategy for the preparation of Co catalysts through the in situ reconstruction of cobalt borate (CoBOx) during the reductive amination, delivering a high catalytic activity for production of benzylamine from benzaldehyde and ammonia. Initially, CoBOx was transformed into Co(OH)2 through the interaction with ammonia and subsequently reduced to Co nanoparticles by H2 under the reaction environments. The in situ generated Co catalysts exhibited a satisfactory activity and selectivity to the target product, which overmatched the commonly used Co/C, Pt or Raney Ni catalysts. We anticipate that such an in situ reconstruction of CoBOx by reactants during the reaction could provide a new approach for the design and optimization of catalysts to produce primary amines.</p

FoxM1 Promotes Glioma Cells Progression by Up-Regulating Anxa1 Expression

<div><p>Forkhead box M1 (FoxM1) is a member of the forkhead transcription factor family and is overexpression in malignant gliomas. However, the molecular mechanisms by which FoxM1lead to glioma carcinogenesis and progression are still not well known. In the present study, we show that Anxa1 was overexpression in gliomas and predicted the poor outcome. Furthermore, Anxa1 closely related to the FoxM1 expression and was a direct transcriptional target of FoxM1. Overexpression of FoxM1 up-regulated Anxa1 expression, whereas suppression of FoxM1 expression down-regulated Anxa1 expression in glioma cells. Finally, FoxM1 enhanced the proliferation, migration, and angiogenesis in Anxa1-dependent manner both <i>in vitro</i> and <i>in vivo</i>. Our findings provide both clinical and mechanistic evidences that FoxM1 contributes to glioma development by directly up-regulating Anxa1 expression.</p></div

Effect of FoxM1/Anxa1 expression on proliferation and migration of glioma cells <i>in vitro</i>.

<p><b>A,</b> RT-qPCR and Western blot analyses of FoxM1 and Anxa1 expression in stable pcDNA3.1-Anxa1-transfected U-87MG-RNAi cells (left) and Anxa1-shRNA-transfected SW0188-FoxM1 cells (right). <b>B,</b> Cells as in (A) were cultured in 96-well plates and analyzed by MTT assay. Cell proliferation curves were shown in 9 days. Three independent experiments were conducted. <b>C,</b> Cells as in (A) were examined for cell migration motility in 24-well plates with transwell chambers. Migrated cells were stained with crystal violet (upper) and counted under a light microscope (lower). Three independent experiments were conducted. <b>D,</b> the angiogenic potential of glioma cells was determined by endothelial cell tube formation assay. Capillary tube formation in each group was photographed and quantified. *<i>P</i><0.05.</p

Effects of altered FoxM1 expression on Anxa1 expression in human glioma cell lines.

<p><b>A,</b> Determination of FoxM1 and Anxa1 expression in human glioma cell lines using RT-qPCR (lower) and Western blot (upper). <b>B,</b> Up-regulation of Anxa1 mRNA and protein expression by overexpressing FoxM1. FoxM1 and Anxa1 expression levels in parental, control, and Hs683-FoxM1 and SW1088-FoxM1 cells by RT-qPCR (lower) and Western blot (upper). <b>C,</b> Down-regulation of Anxa1 mRNA and protein expression by depletion of FoxM1 expression. FoxM1 and Anxa1 expression in parental, control, and LN-229-RNAi and U-87MG-RNAi cells by RT-qPCR (lower) and Western blot (upper).</p

The Anxa1 as a transcriptional target of FoxM1.

<p><b>A,</b> transactivation of the Anxa1 promoter in SW1088-FoxM1 cells (left) and repression of the Anxa1 promoter in U-87MG-RNAi cells (right). Activation was calculated relative to SW1088 cells and inhibition was calculated as a percentage relative to U-87MG cells. Three independent experiments were conducted. <b>B,</b> Sequence and position of putative FoxM1 binding site on the Anxa1 promoter. <b>C,</b> ChIP assays were done with SW1088, SW1088-FoxM1, U-87MG and U-87MG-RNAi cells. Chromatin fragments of the cells were immunoprecipitated with anti-FoxM1 antibody (top) or negative control IgG (middle) and subjected to PCR. We subjected 1% of the total cell lysates to PCR before immunoprecipitation as inputs (bottom). <b>D,</b> schematic structure of the Anxa1 promoter. The sequence of the FoxM1 binding site is shown in both wild-type (WT) and mutant (Mut) forms. <b>E,</b> Luciferase activity with or without mutation in Anxa1 promoter. SW1088-FoxM1, U-87MG-RNAi, controls and parental cells were transfected with the wild-type Anxa1 promoter or its mutant. Three independent experiments were conducted. *<i>P</i><0.01.</p

Effect of FoxM1/Anxa1 expression on glioma growth in the brains of nude mice.

<p><b>A,</b> Glioma cells (1×10⁶) were implanted intracranially into nude mice. Mice were euthanized when they were moribund or on day 90. * Incidence: number of mice with tumor/number of mice injected. <b>B,</b> Kaplan-Meier estimates of overall survival time in nude injected with glioma cells (P<0.001). <b>C,</b> Morphologic alteration of the xenograft tumors was analyzed by H&E. D, CD31expression level in xenograft tumors was analyzed by IHC.</p

Highly Efficient Au Nanocatalysts for Heterogeneous Continuous-Flow Reactions Using Hollow CeO₂ Microspheres as a Functional Skeleton

Hollow Au/CeO₂ as a highly efficient and stable heterogeneous catalyst is successfully used for a continuous-flow reaction. The hollow CeO₂ microspheres with thicknesses of 21 nm as functional supports can greatly improve the catalytic activity and stability of the Au nanoparticles. The catalytic activity of hollow Au/CeO₂ catalysts is 4.5 times higher than the Au catalysts without the hollow structure under the same reaction conditions for the reduction of 4-nitrophenol. Meanwhile, the hollow structure also accelerates the mass transfer of reactant for the continuous-flow system. A high turnover number of 65.7 mol h^–1 mol_Au^–1 is yielded for hollow Au/CeO₂ catalysts at a flow rate of 250 mL h^–1 with remarkable stability for a continuous-flow 4-nitrophenol reduction reaction. The present continuous-flow system exhibits a huge potential for the automation treatment of pollutant 4-nitrophenol

Expression of FoxM1 and Anxa1 in human normal brain and glioma tissues.

<p><b>A,</b> Anxa1 and FoxM1 mRNA expression by RT-qPCR. The mRNA expression was analyzed in 30 matched primary glioblastoma tissues and the adjacent normal brain tissues. B, FoxM1 expression levels correlated positively with Anxa1 expression levels in glioblastoma samples (Pearson’s correlation test r = 0.364; <i>P</i> = 0.048). <b>C,</b> Headmay of a glioblastoma microarray data set from ONCOMINE data showing the expression levels of FoxM1 and Anxa1. The FoxM1 expression is correlated with Anxa1 expression (r = 0.327, <i>P</i><0.0001). <b>D,</b> FoxM1 and Anxa1 protein expression levels in 4 matched primary glioblastoma tissues and the adjacent normal brain tissues by Western blot analysis. <b>E and F,</b> Kaplan-Meier estimates of overall survival time in patients who had a glioblastoma with different Anxa1 or FoxM1 expression.</p

Preparation of a spirooxazine grafted PMMA and its photochromic properties

<p>A novel spirooxazine (SO) compound was designed and synthesized. Macromolecular materials, called SO-g-hPMMAs (where the g means grafting and the h means partial hydrolysis), were prepared using PMMA (polymethylmethacrylate) with different degrees of hydrolysis. SO-g-5%hPMMA was prepared by reacting SO-containing active C-Br bonds with 5% partially hydrolyzed PMMA. The SO was characterized using ¹H NMR and infrared. Beyond that, photochromic properties were studied in detail. We discuss the effects of hydrochloric acids and hPMMAs of different hydrolysis degrees on photochromic properties of SO-g-hPMMA. Additionally, mechanical properties of the material were studied. Results indicate that the colored ring-opening form (PMC) of SO-g-hPMMA exhibits a good performance in terms of thermal stability, in contrast to the homologous SO. Experiments additionally demonstrate that hydrochloric acid improves the PMC’s thermal stability. SO-g-9%hPMMA demonstrated a good performance of photochromic properties compared to those with different degrees of hydrolysis.</p