University of Modena and Reggio Emilia

About: University of Modena and Reggio Emilia is a education organization based out in Modena, Italy. It is known for research contribution in the topics: Population & Medicine. The organization has 8179 authors who have published 22418 publications receiving 671337 citations. The organization is also known as: Università degli Studi di Modena e Reggio Emilia & Universita degli Studi di Modena e Reggio Emilia.

Waveguiding mechanism in tube lattice fibers

Abstract: Waveguiding mechanism and modal characteristics of hollow core fibers consisting of a single or a regular arrangement of dielectric tubes are investigated. These fibers have been recently proposed as low loss, broadband THz waveguides. By starting from a description in terms of coupling between air and dielectric modes in a single tube waveguide, a simple and useful model is proposed and numerically validated. It is able to predict dispersion curves, high and low loss spectral regions, and the conditions to ensure the existence of low loss regions. In addition, it allows a better understanding of the role of the geometrical parameters and of the dielectric refractive index. The model is then applied to improve the tradeoff between low loss and effectively single mode propagation, showing that the best results are obtained with a heptagonal arrangement of the tubes.

Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast

Abstract: Mammary epithelial stem cells are fundamental to maintain tissue integrity. Cancer stem cells (CSCs) are implicated in both treatment resistance and disease relapse, and the molecular bases of their malignant properties are still poorly understood. Here we show that both normal stem cells and CSCs of the breast are controlled by the prolyl-isomerase Pin1. Mechanistically, following interaction with Pin1, Notch1 and Notch4, key regulators of cell fate, escape from proteasomal degradation by their major ubiquitin-ligase Fbxw7α. Functionally, we show that Fbxw7α acts as an essential negative regulator of breast CSCs' expansion by restraining Notch activity, but the establishment of a Notch/Pin1 active circuitry opposes this effect, thus promoting breast CSCs self-renewal, tumor growth and metastasis in vivo. In human breast cancers, despite Fbxw7α expression, high levels of Pin1 sustain Notch signaling, which correlates with poor prognosis. Suppression of Pin1 holds promise in reverting aggressive phenotypes, through CSC exhaustion as well as recovered drug sensitivity carrying relevant implications for therapy of breast cancers.

Buffer Traps in Fe-Doped AlGaN/GaN HEMTs: Investigation of the Physical Properties Based on Pulsed and Transient Measurements

Abstract: This paper presents an extensive investigation of the properties of the trap with activation energy equal to 0.6 eV, which has been demonstrated to be responsible for current collapse (CC) in AlGaN/GaN HEMTs. The study was carried out on AlGaN/GaN HEMTs with increasing concentration of iron doping in the buffer. Based on pulsed characterization and drain current transient measurements, we demonstrate that for the samples under investigation: 1) increasing concentrations of Fe-doping in the buffer may induce a strong CC, which is related to the existence of a trap level located 0.63 eV below the conduction band energy and 2) this trap is physically located in the buffer layer, and is not related to the iron atoms but—more likely—to an intrinsic defect whose concentration depends on buffer doping. Moreover, we demonstrate that this level can be filled both under OFF-state conditions (by gate-leakage current) and under ON-state operation (when hot electrons can be injected to the buffer): for these reasons, it can significantly affect the switching properties of AlGaN/GaN HEMTs.

BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta: implications for a proteasome-to-autophagy switch.

Abstract: Eukaryotic cells use autophagy and the ubiquitin-proteasome system as their major protein degradation pathways. Upon proteasomal impairment, cells switch to autophagy to ensure proper clearance of clients (the proteasome-to-autophagy switch). The HSPA8 and HSPA1A cochaperone BAG3 has been suggested to be involved in this switch. However, at present it is still unknown whether and to what extent BAG3 can indeed reroute proteasomal clients to the autophagosomal pathway. Here, we show that BAG3 induces the sequestration of ubiquitinated clients into cytoplasmic puncta colabeled with canonical autophagy linkers and markers. Following proteasome inhibition, BAG3 upregulation significantly contributes to the compensatory activation of autophagy and to the degradation of the (poly)ubiquitinated proteins. BAG3 binding to the ubiquitinated clients occurs through the BAG domain, in competition with BAG1, another BAG family member, that normally directs ubiquitinated clients to the proteasome. Therefore, we propose that following proteasome impairment, increasing the BAG3/BAG1 ratio ensures the "BAG-instructed proteasomal to autophagosomal switch and sorting" (BIPASS).