3 resultados para eumeninine mastoparan ER

em CentAUR: Central Archive University of Reading - UK


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The new erbium(III) complex of picolinic acid (Hpic), ["Bu4N][Er(pic)(4)].5.5H(2)O, was synthesized and the crystal structure determined by single-crystal X-ray diffraction. The compound was further characterized using IR, Raman, H-1 NMR and elemental analysis. The picolinate ligands (pic(-)) are coordinated through N,O-chelation to the erbium cations, as shown by X-ray diffraction and spectroscopic results, leading to an eight coordinate complex. Photoluminescence measurements were performed for this compound which exhibits infrared emission. (C) 2003 Elsevier B.V. All rights reserved.

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The effect of the direction of external electric field on the shear stress of an ER fluid has been studied by molecular-dynamics simulation. Due to the formation of inclined chains, the shear stress strongly depends on the direction of the field, and it may be very large under some special field direction. And theoretical model of ideal microstructure of ER fluids has proved this result. Thus the ER effect may be greatly enhanced just by choosing an optimum direction for the field without any additional requirement, suggesting a promising way to the practical application of ER fluids.

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Crosstalk between nuclear receptors is important for conversion of external and internal stimuli to a physiologically meaningful response by cells. Previous studies from this laboratory have demonstrated crosstalk between the estrogen (ER) and thyroid hormone receptors (TR) on two estrogen responsive physiological promoters, the preproenkephalin and oxytocin receptor gene promoter. Since ERa and ERb are isoforms possessing overlapping and distinct transactivation properties, we hypothesized that the interaction of ERa and b with the various TR isoforms would not be equivalent. To explore this hypothesis, the consensus estrogen response element (ERE)derived from the Xenopus vitellogenin gene is used to investigate the differences in interaction between ERa and b isoforms and the different TR isoforms in fibroblast cells. Both the ER isoforms transactivate from the consensus ERE, though ERa transactivates to a greater extent than ERb. Although neither of the TRb isoforms have an effect on ERa transactivation from the consensus ERE, the liganded TRa1 inhibits the ERa transactivation from the consensus ERE. In contrast, the liganded TRa1 facilitates ERb-mediated transactivation. The crosstalk between the TRb isoforms with the ERa isoform, on the consensus ERE, is different from that with the ERb isoform. The use of a TRa1 mutant, which is unable to bind DNA, abolishes the ability of the TRa1 isoform to interact with either of the ER isoforms. These differences in nuclear receptor crosstalk reveal an important functional difference between isoforms, which provides a novel mechanism for neuroendocrine integration.