Optimization of the Field Plate Design of a 1200 V p-GaN Power High-Electron-Mobility Transistor.

This study optimized the field plate (FP) design (i.e., the number and positions of FP layers) of p-GaN power high-electron-mobility transistors (HEMTs) on the basic of simulations conducted using the technology computer-aided design software of Silvaco. Devices with zero, two, and three FP layers were designed. The FP layers of the HEMTs dispersed the electric field between the gate and drain regions. The device with two FP layers exhibited a high off-state breakdown voltage of 1549 V because of the long distance between its first FP layer and the channel. The devices were subjected to high-temperature reverse bias and high-temperature gate bias measurements to examine their characteristics, which satisfied the reliability specifications of JEDEC.

AlN Surface Passivation of GaN-Based High Electron Mobility Transistors by Plasma-Enhanced Atomic Layer Deposition.

We report a low current collapse GaN-based high electron mobility transistor (HEMT) with an excellent thermal stability at 150 °C. The AlN was grown by N2-based plasma enhanced atomic layer deposition (PEALD) and shown a refractive index of 1.94 at 633 nm of wavelength. Prior to deposit AlN on III-nitrides, the H2/NH3 plasma pre-treatment led to remove the native gallium oxide. The X-ray photoelectron spectroscopy (XPS) spectroscopy confirmed that the native oxide can be effectively decomposed by hydrogen plasma. Following the in situ ALD-AlN passivation, the surface traps can be eliminated and corresponding to a 22.1% of current collapse with quiescent drain bias (V DSQ) at 40 V. Furthermore, the high temperature measurement exhibited a shift-free threshold voltage (V th), corresponding to a 40.2% of current collapse at 150 °C. The thermal stable HEMT enabled a breakdown voltage (BV) to 687 V at high temperature, promising a good thermal reliability under high power operation.

The Possible Mechanism of Advanced Glycation End Products (AGEs) for Alzheimer's Disease.

Amyloid precursor protein (APP) has been modified by ß and γ-secretase that cause amyloid deposits (plaques) in neuronal cells. Glyceraldhyde-derived AGEs has been identified as a major source of neurotoxicity in Alzheimer's disease (AD). In a previous study, we demonstrated that glyceraldehyde-derived AGEs increase APP and Aß via ROS. Furthermore, the combination of AGEs and Aß has been shown to enhance neurotoxicity. In mice, APP expression is increased by tail vein injection of AGEs. This evidence suggests a correlation between AGEs and the development of AD. However, the role played by AGEs in the pathogenesis of AD remains unclear. In this report, we demonstrate that AGEs up-regulate APP processing protein (BACE and PS1) and Sirt1 expression via ROS, but do not affect the expression of downstream antioxidant genes HO-1 and NQO-1. Moreover, we found that AGEs increase GRP78 expression and enhance the cell death-related pathway p53, bcl-2/bax ratio, caspase 3. These results indicate that AGEs impair the neuroprotective effects of Sirt1 and lead to neuronal cell death via ER stress. Our findings suggest that AGEs increase ROS production, which stimulates downstream pathways related to APP processing, Aß production, Sirt1, and GRP78, resulting in the up-regulation of cell death related pathway. This in-turn enhances neuronal cell death, which leads to the development of AD.