AUTOMATIC NUMERICAL ELEMENT GENERATION BY BOUNDARY-FITTED CURVILINEAR COORDINATE SYSTEM

A method for dividing a two-dimensional multi-connected region of a complex shape into a set of triangular elements is developed. A region of a complex shape in the physical plane is divided into some simply connected subregions, and each subregion is mapped onto a square region in the transformed plane. The inverse functions of the mapping are determined by the solution to elliptic partial differential equations with the Dirichlet boundary conditions. After the square region is divided into a set of finite elements, each element is inversely mapped onto the subregions by use of the functions. The finite element data for the global region are made of those for the divided subregions

Carbon­yl(η5-cyclo­penta­dien­yl)(pyridine)(triethyl­stann­yl)iron(II)

In the title complex, [Fe(C5H5){Sn(C2H5)3}(C5H5N)(CO)], the Fe atom is coordinated by carbonyl, pyridine, triethyl­stannyl and cyclo­penta­dienyl ligands in a typical three-legged piano-stool configuration. The Fe—Sn and Fe—N bond distances are 2.5455 (13) and 1.984 (6) Å, respectively

Silencing Mediator of Retinoic Acid and Thyroid Hormone Receptor Regulates Enhanced Activation of Signal Transducer and Activator of Transcription 3 by Epstein-Barr Virus-Derived Epstein-Barr Nuclear Antigen 2

The Epstein-Barr virus (EBV)-encoded latency protein Epstein–Barr nuclear antigen 2 (EBNA2) is a nuclear transcriptional activator that is essential for EBV-induced cellular transformation. In a previous study, we demonstrated that EBNA2 interacts with signal transducer and activator of transcription 3 (STAT3), a signal transducer for an interleukin (IL)-6 family cytokine, and enhances its transcriptional activity. Here, we show that overexpression of a corepressor, silencing mediator of retinoic acid and thyroid hormone receptor (SMRT), decreases the EBNA2-mediated enhanced STAT3 activation. Furthermore, small-interfering RNA-mediated reduction of endogenous SMRT expression augments the EBNA2-mediated enhanced STAT3 activation. Importantly, EBNA2 reduces interactions between STAT3 and SMRT. These data demonstrate that EBNA2 acts as a transcriptional coactivator of STAT3 by influencing the SMRT corepressor complex

Physical and functional interactions between STAT3 and EBNA2

The Epstein-Barr virus (EBV)-encoded latency protein EBNA2 is a nuclear transcriptional activator that is essential for EBV-induced cellular transformation. Here, we show that EBNA2 interacts with STAT3, a signal transducer for an interleukin-6 family cytokine, and enhances the transcriptional activity of STAT3 by influencing its DNA-binding activity. Furthermore, EBNA2 cooperatively acts on STAT3 activation with LMP1. These data demonstrate that EBNA2 acts as a transcriptional coactivator of STAT3

Domenico Vandelli to Carl Linnaeus

Domenico Vandelli to Carl Linnaeu

Catalytic Synthesis of Cyclic and Linear Germoxanes Mediated by an Iron Complex

Six-membered cyclic germoxanes (R₂GeO)₃ were selectively prepared via the thermal reaction of (alkyl)₂GeH₂ in dimethylformamide (DMF). Linear metallagermoxanes with an E–O–Ge–O–E backbone (E = Si, Ge, Sn) were prepared by the reaction of Ph₂GeH₂ with R₃EH in DMF. Their cyclic and linear germoxane formations were achieved using an iron catalyst, (η-C₅H₅)­Fe­(CO)₂Me. An iron carbene complex was proposed to be an intermediate in the catalytic reaction

Catalytic Synthesis of Cyclic and Linear Germoxanes Mediated by an Iron Complex

Six-membered cyclic germoxanes (R₂GeO)₃ were selectively prepared via the thermal reaction of (alkyl)₂GeH₂ in dimethylformamide (DMF). Linear metallagermoxanes with an E–O–Ge–O–E backbone (E = Si, Ge, Sn) were prepared by the reaction of Ph₂GeH₂ with R₃EH in DMF. Their cyclic and linear germoxane formations were achieved using an iron catalyst, (η-C₅H₅)­Fe­(CO)₂Me. An iron carbene complex was proposed to be an intermediate in the catalytic reaction