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Self-powered droplet manipulation for full human-droplet interaction in multiple mediums
Carbene-supported triphosphorus anion
Synthesis of crystalline two-dimensional conjugated polymers through irreversible chemistry under mild conditions
Subsurface ocean turbulent mixing enhances central Pacific ENSO
Enabling the synthesis of O3-type sodium anion-redox cathodes via atmosphere modulation
Observation of switchable polar skyrmion bubbles down to the atomic layers in van der Waals ferroelectric CuInP2S6
A multicenter cohort study of thyroidectomy-related decision regret in patients with low-risk papillary thyroid microcarcinoma
Mitochondrial damage in muscle specific PolG mutant mice activates the integrated stress response and disrupts the mitochondrial folate cycle
Deep learning network for NMR spectra reconstruction in time-frequency domain and quality assessment
Gout management using uricase and sodium citrate hollow mesoporous nanomotors
Electrochemical ohmic memristors for continual learning
Abstract Developing versatile and reliable memristive devices is crucial for advancing future memory and computing architectures. The years of intensive research have still not reached and demonstrated their full horizon of capabilities, and new concepts are essential for successfully using the complete spectra of memristive functionalities for industrial applications. Here, we introduce two-terminal ohmic memristor, characterized by a different type of switching defined as filament conductivity change mechanism (FCM). The operation is based entirely on localized electrochemical redox reactions, resulting in essential advantages such as ultra-stable binary and analog switching, broad voltage stability window, high temperature stability, high switching ratio and good endurance. The multifunctional properties enabled by the FCM can be effectively used to overcome the catastrophic forgetting problem in conventional deep neural networks. Our findings represent an important milestone in resistive switching fundamentals and provide an effective approach for designing memristive system, expanding the horizon of functionalities and neuroscience applications.
Modularity of Zorya defense systems during phage inhibition
Abstract Bacteria have evolved an extraordinary diversity of defense systems against bacteriophage (phage) predation. However, the molecular mechanisms underlying these anti-phage systems often remain elusive. Here, we provide mechanistic and structural insights into Zorya phage defense systems. Using cryo-EM structural analyses, we show that the Zorya type I and II core components, ZorA and ZorB, assemble in a 5:2 complex that is similar to inner-membrane ion-driven, rotary motors that power flagellar rotation, type 9 secretion, gliding and the Ton nutrient uptake systems. The ZorAB complex has an elongated cytoplasmic tail assembled by bundling the C-termini of the five ZorA subunits. Mutagenesis demonstrates that peptidoglycan binding by the periplasmic domains of ZorB, the structured cytoplasmic tail of ZorA, and ion flow through the motor is important for function in both type I and II systems. Furthermore, we identify ZorE as the effector module of the Zorya II system, possessing nickase activity. Our work reveals the molecular basis of the activity of Zorya systems and highlights the ZorE nickase as crucial for population-wide immunity in the type II system.
The ARCCRABP1 neurons play a crucial role in the regulation of energy homeostasis
Dilution-driven gel-sol-gel-sol transitions by the sequential evolution of surfactant micelles
Pseudomonas aeruginosa acyl-CoA dehydrogenases and structure-guided inversion of their substrate specificity
Abstract Fatty acids are a primary source of carbon for Pseudomonas aeruginosa (PA) in the airways of people with cystic fibrosis (CF). Here, we use tandem mass-tag proteomics to analyse the protein expression profile of a CF clinical isolate grown on different fatty acids. Two fatty acyl-CoA dehydrogenases (designated FadE1 and FadE2) are strongly induced during growth on fatty acids. FadE1 displays a strong preference for long-chain acyl-CoAs, whereas FadE2 exclusively utilizes medium-chain acyl-CoAs. Structural analysis of the enzymes enables us to identify residues comprising the substrate selectivity filter in each. Engineering these residues enables us to invert the substrate specificity of each enzyme. Mutants in fadE1 displayed impaired virulence in an infection model, and decreased growth on long chain fatty acids. The unique features of the substrate binding pocket enable us to identify an inhibitor that is differentially active against FadE1 and FadE2.