Search

The presence of abnormally oriented grains (AOGs) in sputter-deposited aluminum scandium nitride (AlScN) films significantly degrades their physical properties, compromising the performance of bulk acoustic wave (BAW) devices. This study utilizes first-principles calculations to reveal that in tetrahedral wurtzite AlScN film-doped Sc atoms tend to aggregate at the second nearest-neighbor positions, forming dense ScN octahedral structures. The rock-salt (RS) ScN continued to grow due to further Sc aggregation. However, due to inadequate scandium flux, embryonic RS structures cannot be sustained, resulting in the nucleation of AOGs at the (111) faces of the octahedral ScN structure. Electron microscopy studies indicated that AOGs possess wurtzite structures and originate at tilted grain boundaries. These boundaries were characterized as RS ScN with more Sc atoms. This corroborated the theoretical predictions. BAW resonators and filters fabricated from sputter-deposited AlScN films demonstrate that AOGs degraded the piezoelectricity of AlScN, reducing the resonator’s electromechanical coupling coefficient (Keff2). Measurements showed that AOG density increased from edge to center of the 8 in. wafer, resulting in a 3% decrease in average Keff2in the resonators and a 137 MHz decrease in the filter bandwidth at 5 dB.

A simple but effective method for increasing the viewing angle of the integral imaging system was proposed. Unlike the existing methods, the viewing angle was extended through the fully effective utilization of the pixels within the elemental image array rather than the modifications to the system structures or the importing of extra devices. The relationships between the pixel positions and the viewing zone distributions were analyzed, the algorithm model for replacing the invalid pixels was built and then a method for generating full‐effective‐pixel elemental image array (FEP‐EIA) was proposed. Experiment results demonstrated that the viewing angle of the integral imaging system was significantly increased with the proposed method.

Inflammatory bowel disease (IBD) is a multifactorial chronic inflammation of the intestine and has become a global public health concern. A farnesoid X receptor (FXR) was recently reported to play a key role in hepatic-intestinal circulation, intestinal metabolism, immunity, and microbial regulation, and thus, it becomes a promising therapeutic target for IBD. In this study, we identified a series of nonbile acid FXR agonists, in which 33 novel compounds were designed and synthesized by the structure-based drug design strategy from our previously identified hit compound. Compound 33exhibited a potent FXR agonistic activity, high intestinal distribution, good anti-inflammatory activity, and the ability to repair the colon epithelium in a DSS-induced acute enteritis model. Based on the results of RNA-seq analysis, we further investigated the therapeutic potential of the combination of compound 33with 5-ASA. Overall, the results indicated that compound 33is a promising drug candidate for IBD treatment.

The UGA codon context of the Escherichia coli fdhF mRNA includes an element called the selenocysteine insertion sequence (SECIS) that is responsible for the UGA-directed incorporation of the amino acid selenocysteine into a protein. Here, we describe an extended fdhF SECIS that includes the information for an additional function: the prevention of UGA readthrough under conditions of selenium deficiency. This information is contained in a short mRNA region consisting of a single C residue adjacent to the UGA on its downstream side, and an additional segment consisting of the six nucleotides immediately upstream from it. These two regions act independently and additively, and probably through different mechanisms. The single C residue acts as itself; the upstream region acts at the level of the two amino acids, arginine and valine, for which it codes. These two codons at the 5′ side of the UGA correspond to the ribosomal E and P sites. Here, we present a model for the E. coli fdhF SECIS as a multifunctional RNA structure containing three functional elements. Depending on the availability of selenium, the SECIS enables one of two alternatives for the translational machinery: either selenocysteine incorporation into a polypeptide or termination of the polypeptide chain.

The essential trace element selenium (Se) is involved in the form of selenocysteine at the active site of several prokaryotic and eukaryotic proteins called selenoproteins. These proteins have recently attracted attention particularly in relation to their application to human health and new characteristics of the genetic code. We have recently described a selenium bioassay based on a recombinant DNA construct in which the expression of thelac′Zgene inEscherichia coliis proportionally and specifically driven by UGA-directed selenocysteine incorporation. Here we have further developed this bioassay for more rapid and sensitive detection and measurement of selenium that permits screening of the selenium status on agar plates. Again, the inclusion of selenium into thelac′Z-fusion product is reflected by the level of β-galactosidase activity, which in turn is reflected by the intensity of fluorescence on agar plates. This fluorescing agent is a 4-methylumbelliferyl moiety which is released through the cleavage by the enzyme of 4-methylumbelliferyl-β-d-galactoside. The intensity of the fluorescence is easily detected by uv irradiation and photographed by polaroid or video cameras.

The UGA codon, usually a stop codon, can also direct the incorporation into a protein of the modified amino acid selenocysteine. This UGA decoding process requires a cis‐acting mRNA element called `selenocysteine insertion sequence' (SECIS) that can form a stem–loop structure. In Escherichia coli the SECIS of the selenoprotein formate dehydrogenase (FdhH) mRNA has been previously described to consist of at least 40 nucleotides following the UGA codon. Here we determined the nature of the minimal SECIS required for the in vivo UGA‐directed selenocysteine incorporation in E.coli. Our study is based on extensive mutational analysis of the fdhF SECIS DNA located in a lac′Z fusion. We found that the whole stem–loop RNA structure of the E.colifdhF SECIS previously described is not required for the UGA‐directed selenocysteine incorporation in vivo. Rather, only its upper stem–loop structure of 17 nucleotides is necessary on the condition that it is located in a proper distance (11 nucleotides) from the UGA codon. Based on these observations, we present a new model for the minimal E.coli SECIS.