Electrical and ferroelectric properties of rare-earth-doped Na0.5Bi4.0RE0.5Ti4O15 (RE = Eu, Gd and Dy) thin films

A study of the structural, electrical and ferroelectric properties of layered Aurivillius-type Na0.5Bi4.5Ti4O15 (NaBTi) and Na0.5Bi4.0RE0.5Ti4O15 (RE = Eu, Gd and Dy) thin films is reported. These films were fabricated on Pt-coated Si(100) substrates by using a chemical solution deposition method followed by a heat treatment. The rare-earth elements used as dopants, such as Eu, Gd and Dy, were found to be effective in improving the leakage current densities and the ferroelectric properties of the layered Na0.5Bi4.5Ti4O15 thin films without affecting their original Aurivillius structures. Based on the measured ferroelectric polarization-electric field (P−E) hysteresis loops, we found that the Gd-doped NaBTi thin film, among all the films, exhibited the highest ferroelectric remnant polarization of 2Pr = 37.4 μC/cm2 and a low coercive electric field of 2Ec = 187 kV/cm at an applied electric field of 475 kV/cm. Furthermore, the lowest value of the leakage current density of 6.12×107 A/cm2 at an applied electric field of 100 kV/cm was measured for the Gd-doped NaBTi thin film

Economical Valuation of Hypothetically Constructed Washland around a Wetland

Source: ICHE Conference Archive - https://mdi-de.baw.de/icheArchiv

A Robust and Low-Complexity Timing Synchronization Algorithm for ADSRC System

In this paper, a robust, low-complexity timing synchronization algorithm suitable for 5.9 GHz Dedicated Short Range Communications (DSRC) system is proposed. The proposed method uses cross-correlation technique to detect the starting point of both a short training symbol and the guard interval of the first long training symbol. This allows the proposed algorithm to have low-complex architecture. Compared to the scheme proposed by Chang and Kelly, the proposed algorithm attains considerably higher timing synchronization performance and significantly reduced computational complexity. Simulation results show that the proposed algorithm is robust and efficient in high-mobility environments and low signal-to-noise ratio (SNR) conditions

Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology

© Copyright © 2020 Kwak, Kim, Lee, Kim, Son and Shin. Most extracellular proteins are secreted via the classical endoplasmic reticulum (ER)/Golgi-dependent secretion pathway; however, some proteins, including a few danger-associated molecular patterns (DAMPs), are secreted via non-classical ER/Golgi-independent secretion pathways. The evolutionarily conserved high mobility group box1 (HMGB1) is a ubiquitous nuclear protein that can be released by almost all cell types. HMGB1 lacks signal peptide and utilizes diverse non-canonical secretion mechanisms for its extracellular export. Although the post-translational modifications of HMGB1 were demonstrated, the oxidation of HMGB1 and secretion mechanisms are not highlighted yet. We currently investigated that peroxiredoxins I and II (PrxI/II) induce the intramolecular disulfide bond formation of HMGB1 in the nucleus. Disulfide HMGB1 is preferentially transported out of the nucleus by binding to the nuclear exportin chromosome-region maintenance 1 (CRM1). We determined the kinetics of HMGB1 oxidation in bone marrow-derived macrophage as early as a few minutes after lipopolysaccharide treatment, peaking at 4 h while disulfide HMGB1 accumulation was observed within the cells, starting to secrete in the late time point. We have shown that HMGB1 oxidation status, which is known to determine the biological activity in extracellular HMGB1, is crucial for the secretion of HMGB1 from the nucleus. This review summarizes selected aspects of HMGB1 redox biology relevant to the induction and propagation of inflammatory diseases. We implicate the immunological significance and the need for novel HMGB1 inhibitors through mechanism-based studies

Cdk5 Phosphorylates Dopamine D2 Receptor and Attenuates Downstream Signaling

The dopamine D2 receptor (DRD2) is a key receptor that mediates dopamine-associated brain functions such as mood, reward, and emotion. Cyclin-dependent kinase 5 (Cdk5) is a proline-directed serine/threonine kinase whose function has been implicated in the brain reward circuit. In this study, we revealed that the serine 321 residue (S321) in the third intracellular loop of DRD2 (D2i3) is a novel regulatory site of Cdk5. Cdk5-dependent phosphorylation of S321 in the D2i3 was observed in in vitro and cell culture systems. We further observed that the phosphorylation of S321 impaired the agonist-stimulated surface expression of DRD2 and decreased G protein coupling to DRD2. Moreover, the downstream cAMP pathway was affected in the heterologous system and in primary neuronal cultures from p35 knockout embryos likely due to the reduced inhibitory activity of DRD2. These results indicate that Cdk5-mediated phosphorylation of S321 inhibits DRD2 function, providing a novel regulatory mechanism for dopamine signaling.X111111sciescopu

Effects of Promoter on the Formation of Gas Hydrate from Blast furnace Gas

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