Mechanically induced pseudo-magnetic fields in the excitonic fine structures of droplet epitaxial quantum dots

We present numerical investigations based on the Luttinger-Kohn four-band $k \cdot p$ theory and, accordingly, establish a quantitatively valid model of the excitonic fine structures of droplet epitaxial GaAs/AlGaAs quantum dots under uni-axial stress control. In the formalisms, stressing a photo-excited quantum dot is equivalent creating a pseudo-magnetic field that is directly coupled to the pseudo-spin of the exciton doublet and tunable to tailor the polarized fine structure of exciton. The latter feature is associated with the valence-band-mixing of exciton that is especially sensitive to external stress in inherently unstrained droplet epitaxial GaAs/AlGaAs quantum dots and allows us to mechanically design and prepare any desired exciton states of QD photon sources prior to the photon generation.Comment: 7 figure

FAM129B, an antioxidative protein, reduces chemosensitivity by competing with Nrf2 for Keap1 binding.

BackgroundThe transcription factor Nrf2 is a master regulator of antioxidant response. While Nrf2 activation may counter increasing oxidative stress in aging, its activation in cancer can promote cancer progression and metastasis, and confer resistance to chemotherapy and radiotherapy. Thus, Nrf2 has been considered as a key pharmacological target. Unfortunately, there are no specific Nrf2 inhibitors for therapeutic application. Moreover, high Nrf2 activity in many tumors without Keap1 or Nrf2 mutations suggests that alternative mechanisms of Nrf2 regulation exist.MethodsInteraction of FAM129B with Keap1 is demonstrated by immunofluorescence, colocalization, co-immunoprecipitation and mammalian two-hybrid assay. Antioxidative function of FAM129B is analyzed by measuring ROS levels with DCF/flow cytometry, Nrf2 activation using luciferase reporter assay and determination of downstream gene expression by qPCR and wester blotting. Impact of FAM129B on in vivo chemosensitivity is examined in mice bearing breast and colon cancer xenografts. The clinical relevance of FAM129B is assessed by qPCR in breast cancer samples and data mining of publicly available databases.FindingsWe have demonstrated that FAM129B in cancer promotes Nrf2 activity by reducing its ubiquitination through competition with Nrf2 for Keap1 binding via its DLG and ETGE motifs. In addition, FAM129B reduces chemosensitivity by augmenting Nrf2 antioxidative signaling and confers poor prognosis in breast and lung cancer.InterpretationThese findings demonstrate the important role of FAM129B in Nrf2 activation and antioxidative response, and identify FMA129B as a potential therapeutic target. FUND: The Chang Gung Medical Foundation (Taiwan) and the Ministry of Science and Technology (Taiwan)

Vertical Integration in the Taiwan Aquaculture Industry

The study aims to improve the distribution channels in the Taiwan aquaculture industry through a better vertical integration. This study is derived from a need to improve the distribution performance of agricultural-based industries in response to increasing food demands in Asia and elsewhere. Based on a four-by-eight matrix derived from both a value chain and a service profit chain, thirty different strategies are developed. This development is based on key success factors and strategies for vertical integration interviewed and cited in the literatures. The findings are identified by applying the Gray Relational Analysis (GRA). For this study, the key success factors for aquaculture wholesale markets include the communication, integration and cohesion of opinion within the wholesale market; government support; andmutual trust between members of the vertical integration scheme. The suitable vertical integration strategies are an improved safety and hygiene inspection of aquaculture products, accuracy of aquaculture product categorization, and precision in product weighing.aquaculture industry, grey relational analysis (GRA), channels integration

Ventricular divergence correlates with epicardial wavebreaks and predicts ventricular arrhythmia in isolated rabbit hearts during therapeutic hypothermia

INTRODUCTION: High beat-to-beat morphological variation (divergence) on the ventricular electrogram during programmed ventricular stimulation (PVS) is associated with increased risk of ventricular fibrillation (VF), with unclear mechanisms. We hypothesized that ventricular divergence is associated with epicardial wavebreaks during PVS, and that it predicts VF occurrence. METHOD AND RESULTS: Langendorff-perfused rabbit hearts (n = 10) underwent 30-min therapeutic hypothermia (TH, 30°C), followed by a 20-min treatment with rotigaptide (300 nM), a gap junction modifier. VF inducibility was tested using burst ventricular pacing at the shortest pacing cycle length achieving 1:1 ventricular capture. Pseudo-ECG (p-ECG) and epicardial activation maps were simultaneously recorded for divergence and wavebreaks analysis, respectively. A total of 112 optical and p-ECG recordings (62 at TH, 50 at TH treated with rotigaptide) were analyzed. Adding rotigaptide reduced ventricular divergence, from 0.13±0.10 at TH to 0.09±0.07 (p = 0.018). Similarly, rotigaptide reduced the number of epicardial wavebreaks, from 0.59±0.73 at TH to 0.30±0.49 (p = 0.036). VF inducibility decreased, from 48±31% at TH to 22±32% after rotigaptide infusion (p = 0.032). Linear regression models showed that ventricular divergence correlated with epicardial wavebreaks during TH (p<0.001). CONCLUSION: Ventricular divergence correlated with, and might be predictive of epicardial wavebreaks during PVS at TH. Rotigaptide decreased both the ventricular divergence and epicardial wavebreaks, and reduced the probability of pacing-induced VF during TH

Influence of Y-doped induced defects on the optical and magnetic properties of ZnO nanorod arrays prepared by low-temperature hydrothermal process

One-dimensional pure zinc oxide (ZnO) and Y-doped ZnO nanorod arrays have been successfully fabricated on the silicon substrate for comparison by a simple hydrothermal process at the low temperature of 90°C. The Y-doped nanorods exhibit the same c-axis-oriented wurtzite hexagonal structure as pure ZnO nanorods. Based on the results of photoluminescence, an enhancement of defect-induced green-yellow visible emission is observed for the Y-doped ZnO nanorods. The decrease of E(2)(H) mode intensity and increase of E(1)(LO) mode intensity examined by the Raman spectrum also indicate the increase of defects for the Y-doped ZnO nanorods. As compared to pure ZnO nanorods, Y-doped ZnO nanorods show a remarked increase of saturation magnetization. The combination of visible photoluminescence and ferromagnetism measurement results indicates the increase of oxygen defects due to the Y doping which plays a crucial role in the optical and magnetic performances of the ZnO nanorods

Bifurcation of Arabidopsis NLR Immune Signaling via Ca2+-Dependent Protein Kinases

Nucleotide-binding domain leucine-rich repeat (NLR) protein complexes sense infections and trigger robust immune responses in plants and humans. Activation of plant NLR resistance (R) proteins by pathogen effectors launches convergent immune responses, including programmed cell death (PCD), reactive oxygen species (ROS) production and transcriptional reprogramming with elusive mechanisms. Functional genomic and biochemical genetic screens identified six closely related Arabidopsis Ca2+-dependent protein kinases (CPKs) in mediating bifurcate immune responses activated by NLR proteins, RPS2 and RPM1. The dynamics of differential CPK1/2 activation by pathogen effectors controls the onset of cell death. Sustained CPK4/5/6/11 activation directly phosphorylates a specific subgroup of WRKY transcription factors, WRKY8/28/48, to synergistically regulate transcriptional reprogramming crucial for NLR-dependent restriction of pathogen growth, whereas CPK1/2/4/11 phosphorylate plasma membrane-resident NADPH oxidases for ROS production. Our studies delineate bifurcation of complex signaling mechanisms downstream of NLR immune sensors mediated by the myriad action of CPKs with distinct substrate specificity and subcellular dynamics