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.

No abstract

We demonstrate inherent biorealistic synaptic plasticity functions in the Pt/n-ZnO/SiO 2-x /Pt heterostructures, where the n-ZnO semiconductor is geometrically cone-shaped in the size of a few nanometers. The synaptic functions were achieved within a two-terminal, electroforming-free, and low-power rectifying diode-like resistive switching device. The important rate-dependent synaptic functions, such as the nonlinear transient conduction behavior, short-and long-term plasticity, paired-pulse facilitation, spike-rate-dependent plasticity and sliding threshold effect, were investigated in a single device. These characteristics closely mimic the memory and learning functions of those in biosynapses, where frequency-dependent identical spiking operations are mostly taking place, and we emulate these characteristics in the "Learning-Forgetting-Relearning" synaptic behavior. The switching dynamics in the cone-shaped n-ZnO semiconductor are correlated with the transport mechanism along the grain boundaries of the charged ion species, namely, oxygen vacancies and charged oxygen. The diffusion and generation/recombination of these defects have specific time scales of self-decay by virtue of the asymmetric profile of the n-ZnO cone defects. Finally, the essential biorealistic synaptic plasticity functions were discovered for the perspectives of dynamic/adaptive electronic synapse implementations in hardware-based neuromorphic computing.

S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to four-helical cytokines, we have probed the interaction of Ca2+-bound recombinant human S100P with a panel of 32 four-helical human cytokines covering all structural families of this fold, using surface plasmon resonance spectroscopy. A total of 22 cytokines from all families of four-helical cytokines are S100P binders with the equilibrium dissociation constants, Kd, ranging from 1 nM to 3 µM (below the Kd value for the S100P complex with the V domain of its conventional receptor, receptor for advanced glycation end products, RAGE). Molecular docking and mutagenesis studies revealed the presence in the S100P molecule of a cytokine-binding site, which overlaps with the RAGE-binding site. Since S100 binding to four-helical cytokines inhibits their signaling in some cases, the revealed ability of the S100P protein to interact with ca. 71% of the four-helical cytokines indicates that S100P may serve as a poorly selective inhibitor of their action.