Due to overcoming the limitation of aggregation caused quenching (ACQ) on solid-state emitter, aggregation-induced emission (AIE) organic luminogens have becoming a promising candidate in aqueous electrochemiluminescence (ECL). However, restricted by...

It is still a big challenge to develop active, stable, and easy-to-make bifunctional non-noble electrocatalysts for upshifting overall urea-assisted water splitting toward practical environmental applications at large current densities with lower cell voltages. In response, here we report a competitive bifunctional electrocatalyst that can catalyze both the urea oxidation reaction (UOR) and hydrogen evolution reaction (HER) by fabricating the in situ grown Ni phosphate (shell)-anchored Ni12P5 nanorod (core) arrays on the 3D Ni foam skeleton (named as Ni12P5/Ni-Pi/NF). Benefiting from the unique hierarchical core–shell nanorod architecture with abundant exposed active sites and improved electron and mass transfer efficiency, such elaborate binder-free arrays could act as a robust 3D UOR anode and can achieve 900 mA cm–2 only at potentials of 1.378 V in 1.0 M KOH with 0.5 M urea. Additionally, this electrode also shows remarkable cathodic HER catalytic activities. Moreover, when constructing an alkaline electrolyzer using the bifunctional electrodes, the integrated system is capable of delivering the current density of 500 mA cm–2 stably for over 6 h at a cell voltage as low as 1.662 V, which is 287 mV less than that for pure water splitting. As such, our result may become a significant step in developing an industrial electrolyzer for meaningful massive electrocatalytic hydrogen (H2) production by urea-assisted water splitting.

Metallic selenides have been widely investigated as promising electrode materials for metal‐ion batteries based on their relatively high theoretical capacity. However, rapid capacity decay and structural collapse resulting from the larger‐sized Na+/K+ greatly hamper their application. Herein, a bimetallic selenide (MoSe2/CoSe2) encapsulated in nitrogen, sulfur‐codoped hollow carbon nanospheres interconnected reduced graphene oxide nanosheets (rGO@MCSe) are successfully designed as advanced anode materials for Na/K‐ion batteries. As expected, the significant pseudocapacitive charge storage behavior substantially contributes to superior rate capability. Specifically, it achieves a high reversible specific capacity of 311 mAh g−1 at 10 A g−1 in NIBs and 310 mAh g−1 at 5 A g−1 in KIBs. A combination of ex situ X‐ray diffraction, Raman spectroscopy, and transmission electron microscopy tests reveals the phase transition of rGO@MCSe in NIBs/KIBs. Unexpectedly, they show quite different Na+/K+ insertion/extraction reaction mechanisms for both cells, maybe due to more sluggish K+ diffusion kinetics than that of Na+. More significantly, it shows excellent energy storage properties in Na/K‐ion full cells when coupled with Na3V2(PO4)2O2F and PTCDA@450 °C cathodes. This work offers an advanced electrode construction guidance for the development of high‐performance energy storage devices.

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The molecular mechanisms associated with rabies virus (RV) virulence are not fully understood. In this study, the RV Flury low-egg-passage (LEP) and high-egg-passage (HEP) strains were used as models to explore the attenuation mechanism of RV. The results of our studies confirmed that the R333Q mutation in the glycoprotein (G R333Q ) is crucial for the attenuation of Flury RV in mice. The R333Q mutation is stably maintained in the HEP genome background but not in the LEP genome background during replication in mouse brain tissue or cell culture. Further investigation using chimeric viruses revealed that the polymerase L gene determines the genetic stability of the G R333Q mutation during replication. Moreover, a recombinant RV containing the LEP G protein with the R333Q mutation and the HEP L gene showed significant attenuation, genetic stability, enhancement of apoptosis, and immunogenicity. These results indicate that attenuation of the RV Flury strain results from the coevolution of G and L elements and provide important information for the generation of safer and more effective modified live rabies vaccine.Rabies virus (RV) belongs to the genus Lyssavirus of the family Rhabdoviridae and causes a fatal neurological disease in humans and animals (6). The RV genome is a nonsegmented negative-strand (NNS) RNA encoding five structural proteins: nucleoprotein (N), phosphoprotein (P), matrix protein (M), glycoprotein (G), and large polymerase (L). Among these, the G protein is a major contributor to RV pathogenicity (7,31,33). The G protein facilitates fast virus entry and transsynaptic spread and regulates the rate of virus replication, together with other viral elements (8,30,39). The G protein of nonpathogenic RV strains can trigger apoptosis, while the RV G of pathogenic strains induces less or no apoptosis (35, 59). The amino acid residue at position 333 of the G protein (G333) of some fixed strains has been shown to be an important determinant of virulence in adult mice (5). Strains that have arginine or lysine at position G333 kill adult mice, whereas mutants with other amino acids at this site cause a nonlethal infection (1,5,25,36,49,53). However, the pathogenicity of RV strains is not solely determined by substitutions at the G333 position. Other substitutions in the G protein, such as N194K, have also been shown to affect viral pathogenicity in mice (10, 21, 50). In addition, other viral elements, such as the N, P, M, and L genes, the trailer sequence in the noncoding region, and the pseudogene, were also reported to modulate RV pathogenicity (12,46,57,58). How these viral elements regulate the pathogenicity of RV remains to be fully explored, and further investigation is needed to understand the molecular basis of RV pathogenicity.Attenuated Flury RV low-egg-passage (LEP) and high-eggpassage (HEP) strains were established through serial passage in chicken brain, chicken embryos, and culture cells using a Flury RV isolated from a girl who died of rabies (23,24). LEP has Arg at position G333 and kills adu...