The gas electron multiplier (GEM) used as single proportional counter or in a cascade of two or more elements, permits to attain high gains and to perform detection and localization of ionizing tracks at very high radiation rates. As in other micro-pattern detectors, however, the occasional occurrence of heavily ionizing trails may trigger a local breakdown, with possible harmful consequences on the device itself and on the readout electronics. This paper describes a systematic investigation of the discharge mechanisms in single and multiple GEM structures, and suggests various strategies to reduce both the energy and the probability of the discharges. r

Coexistence of threshold and memory switching characteristics of ALD HfO₂ memristor synaptic arrays for energy-efficient neuromorphic computing.

Carbon‐based electronic devices are suitable candidates for bioinspired electronics due to their low cost, eco‐friendliness, mechanical flexibility, and compatibility with complementary metal‐oxide‐semiconductor technology. New types of materials such as graphene quantum dots (GQDs) have attracted attention in the search for new applications beyond solar cells and energy harvesting due to their superior properties such as elevated photoluminescence, high chemical inertness, and excellent biocompatibility. In this paper, a biocompatible/organic electronic synapse based on nitrogen‐doped graphene oxide quantum dots (N‐GOQDs) is reported, which exhibits threshold resistive switching via silver cation (Ag+) migration dynamics. In analogy to the calcium (Ca2+) ion dynamics of biological synapses, important biological synapse functions such as short‐term potentiation (STP), paired‐pulse facilitation, and transition from STP to long‐term plasticity behaviors are replicated. Long‐term depression behavior is also evaluated and specific spike‐timing dependent plasticity is assessed. In addition, elaborated switching mechanism of biosimilar Ag+ migration dynamics provides the potential for using N‐GOQD‐based artificial synapse in future biocompatible neuromorphic systems.

A two terminal semiconducting device like a memristor is indispensable to emulate the function of synapse in the working memory. The analog switching characteristics of memristor play a vital role in the emulation of biological synapses. The application of consecutive voltage sweeps or pulses (action potentials) changes the conductivity of the memristor which is considered as the fundamental cause of the synaptic plasticity. In this study, a neuromorphic device using an in-situ growth of sub-tantalum oxide switching layer is fabricated, which exhibits the digital SET and analog RESET switching with an electroforming process without any compliance current (compliance free). The process of electroforming and SET is observed at the positive sweeps of +2.4 V and +0.86 V, respectively, while multilevel RESET is observed with the consecutive negative sweeps in the range of 0 V to −1.2 V. The movement of oxygen vacancies and gradual change in the anatomy of the filament is attributed to digital SET and analog RESET switching characteristics. For the Ti/Ta2O3−x/Pt neuromorphic device, the Ti top and Pt bottom electrodes are considered as counterparts of the pre-synaptic input terminal and a post-synaptic output terminal, respectively.

Interferon-β (IFN-β) is a pleiotropic cytokine used for therapy of multiple sclerosis, which is also effective in suppression of viral and bacterial infections and cancer. Recently, we reported a highly specific interaction between IFN-β and S100P lowering IFN-β cytotoxicity to cancer cells (Int J Biol Macromol. 2020; 143: 633–639). S100P is a member of large family of multifunctional Ca2+-binding proteins with cytokine-like activities. To probe selectivity of IFN-β—S100 interaction with respect to S100 proteins, we used surface plasmon resonance spectroscopy, chemical crosslinking, and crystal violet assay. Among the thirteen S100 proteins studied S100A1, S100A4, and S100A6 proteins exhibit strictly Ca2+-dependent binding to IFN-β with equilibrium dissociation constants, Kd, of 0.04–1.5 µM for their Ca2+-bound homodimeric forms. Calcium depletion abolishes the S100—IFN-β interactions. Monomerization of S100A1/A4/A6 decreases Kd values down to 0.11–1.0 nM. Interferon-α is unable of binding to the S100 proteins studied. S100A1/A4 proteins inhibit IFN-β-induced suppression of MCF-7 cells viability. The revealed direct influence of specific S100 proteins on IFN-β activity uncovers a novel regulatory role of particular S100 proteins, and opens up novel approaches to enhancement of therapeutic efficacy of IFN-β.