It is of great significance to reveal the detailed mechanism of neighboring effects between monomers, as they could not only affect the intermediate bonding but also change the reaction pathway. This paper describes the electronic effect between neighboring Zn/Co monomers effectively promoting CO2 electroreduction to CO. Zn and Co atoms coordinated on N doped carbon (ZnCoNC) show a CO faradaic efficiency of 93.2 % at −0.5 V versus RHE during a 30‐hours test. Extended X‐ray absorption fine structure measurements (EXAFS) indicated no direct metal–metal bonding and X‐ray absorption near‐edge structure (XANES) showed the electronic effect between Zn/Co monomers. In situ attenuated total reflection‐infrared spectroscopy (ATR‐IR) and density functional theory (DFT) calculations further revealed that the electronic effect between Zn/Co enhanced the *COOH intermediate bonding on Zn sites and thus promoted CO production. This work could act as a promising way to reveal the mechanism of neighboring monomers and to influence catalysis.

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Heterogeneous MoS2/NiS is dimensionally constructed and selectively fine tuned to achieve different morphologies with multi-level interfaces.

With the goal to achieve highly efficacious MRI-monitored magnetic targeting, a novel drug carrier with dual nature of superior magnetophoretic mobility and superparamagnetism was synthesized. This carrier was specially designed in a core-shell structure. The core was achieved by utilizing a strategy of self-assembly of oppositely charged ultrafine superparamagnetic iron oxide nanoparticles previously prepared. The final particles were formed by coating such cores with carboxymethyldextran (CMD) polymer. By exclusion of non-magnetic materials from the interior part of the particles, this structure maximized the amount of magnetic material and thus yielded a superior magnetophoretic mobility. Such a strategy avoids the challenge of superparamagnetism loss, which would be caused by cores exceeding a critical domain size. Coating the self-assembled core enables the magnetic carrier to be stable upon usage and storage and to be readily linked with drug molecules for therapeutic applications. In vitro characterization showed that these nanoparticles displayed a 3-to 4-fold enhancement in magnetophoretic mobility, and a markedly improved stability when stored in 50% serum as a comparison of conventional iron oxide-based magnetic nanoparticles. Preliminary in vivo studies revealed that the nanoparticles alsofunction well as a contrast enhancer for MR imaging of brain glioma. This technology could lead to the development of a new paradigm of magnetic carriers that meet with the needs of various clinical applications.

Linear ubiquitination plays an important role in the regulation of the immune response by regulating nuclear factor κB (NF-κB). The linear ubiquitination-specific deubiquitinase ovarian tumor domain deubiquitinase with linear linkage specificity (OTULIN) can control the immune signaling transduction pathway by restricting the Met1-linked ubiquitination process. In our study, the porcine OTLLIN gene was cloned and deubiquitin functions were detected in a porcine reproductive and respiratory syndrome virus (PRRSV)-infected-cell model. PRRSV infection promotes the expression of the OTULIN gene; in turn, overexpression of OTULIN contributes to PRRSV proliferation. There is negative regulation of innate immunity with OTULIN during viral infection. The cooperative effects of swine OTULIN and PRRSV Nsp11 potentiate the ability to reduce levels of cellular protein ubiquitin associated with innate immunity. Importantly, PRRSV Nsp11 recruits OTULIN through a nonenzymatic combination to enhance its ability to remove linear ubiquitination targeting NEMO, resulting in a superimposed effect that inhibits the production of type I interferons (IFNs). Our report presents a new model of virus utilization of the ubiquitin-protease system from the perspective of the viral proteins that interact with cell deubiquitination enzymes, providing new ideas for prevention and control of PRRSV. Deubiquitination effects of swine OTULIN were identified. The interaction between porcine OTULIN and PRRSV Nsp11 is dependent on the OTU domain. PRRSV Nsp11 recruits OTULIN through a nonenzymatic combination to promote removal of linear ubiquitination targeting NEMO, resulting in a superimposed effect that inhibits the production of type I IFNs.

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