RESUMEN
We report the magnetic-field-assisted electric-field-controlled domain switching of a magnetic single domain in a multiferroic/magnetoelectric Ni nanochevrons/[Pb(Mg1/3Nb2/3)O3]0.68-[PbTiO3]0.32 (PMN-PT) layered structure. Initially, a magnetic field was applied in the transverse direction across single-domain Ni nanochevrons to transform each of them into a two-domain state. Subsequently, an electric field was applied to the layered structure, exerting the converse magnetoelectric effect to transform/release the two-domain Ni nanochevrons into one of two possible single-domain states. Finally, the experimental results showed that approximately 50% of the single-domain Ni nanochevrons were switched permanently after applying our approach (i.e., the magnetization direction was permanently rotated by 180 degrees). These results mark important advancements for future nanoelectromagnetic systems.
RESUMEN
Focal adhesion kinase (FAK) and human p70 ribosomal S6 kinase (S6K1) are non-receptor protein tyrosine plays a vital role in cell signaling pathways, such as cell proliferation, survival, and migration. In this study, the 3D structure of FAK (PDB ID: 2AL6) and S6K1 (3A60) were chosen for docking 60 natural compounds attempted to identify novel and specific inhibitors from them. The 30 selected molecules with high scores were further analyzed using DSSTox tools and DS 3.5 ADMET software. Based on a high docking score and energy interaction, 3 of the 9 candidate compounds, neferine B, neferine A, and antroquinonol D, were identified and the inhibitory activity of these compounds were subsequently validated in the C6 glioma cell line. All three selected compounds show potential effects on cell viability by MTT assay. Neferine B, neferine A, and antroquinonol D showed an IC50 value of 10-, 12-, and 16-µM, respectively. Moreover, these compounds decreased the p-FAk and p-S6k1 proteins in a dose-dependent manner. The results of best docked neferine B, neferine A, and antroquinonol D have the potential for further development as a supplement to treat tumorigenesis and metastasis.
Asunto(s)
Productos Biológicos/análisis , Productos Biológicos/farmacología , Ensayos de Selección de Medicamentos Antitumorales , Proteína-Tirosina Quinasas de Adhesión Focal/antagonistas & inhibidores , Simulación del Acoplamiento Molecular , Inhibidores de Proteínas Quinasas/análisis , Inhibidores de Proteínas Quinasas/farmacología , Proteínas Quinasas S6 Ribosómicas/antagonistas & inhibidores , Animales , Productos Biológicos/química , Línea Celular Tumoral , Proliferación Celular/efectos de los fármacos , Proteína-Tirosina Quinasas de Adhesión Focal/metabolismo , Ensayos Analíticos de Alto Rendimiento , Humanos , Enlace de Hidrógeno , Inhibidores de Proteínas Quinasas/química , Ratas , Proteínas Quinasas S6 Ribosómicas/metabolismo , Interfaz Usuario-ComputadorRESUMEN
A plethora of algorithmic assemblers have been proposed for the de novo assembly of genomes, however, no individual assembler guarantees the optimal assembly for diverse species. Optimizing various parameters in an assembler is often performed in order to generate the most optimal assembly. However, few efforts have been pursued to take advantage of multiple assemblies to yield an assembly of high accuracy. In this study, we employ various state-of-the-art assemblers to generate different sets of contigs for bacterial genomes. A tool, named CISA, has been developed to integrate the assemblies into a hybrid set of contigs, resulting in assemblies of superior contiguity and accuracy, compared with the assemblies generated by the state-of-the-art assemblers and the hybrid assemblies merged by existing tools. This tool is implemented in Python and requires MUMmer and BLAST+ to be installed on the local machine. The source code of CISA and examples of its use are available at http://sb.nhri.org.tw/CISA/.