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The catalytic conversion of biomass platform chemicals using abundant non-noble metal nanocatalysts is a challenging topic. Here, high-density cobalt oxide nanoparticles loaded on biomass-derived porous N-doped carbon (NC) was fabricated by a tandem hydrothermal pyrolysis and mild nitrate decomposition process, which is a green and cheap preparation method. The Co3O4 nanoparticles with the average size of 12 nm were uniformly distributed on the porous NC. The nanocomposites also possessed large surface area, high N content, good dispersibility in isopropanol, and furfural absorbability. Due to these characteristics, the novel cobalt nanocatalyst exhibited high catalytic activity for producing furfuryl alcohol, yielding 98.7% of the conversion and 97.1% of the selectivity at 160 °C for 6 h under 1 bar H2. The control experiments implied that both direct hydrogenation and transfer hydrogenation pathways co-existed in the hydrogenation reaction. The excellent catalytic activity of Co3O4@NC was attributed to the cooperative effects of porous NC and Co3O4 nanoparticles. This approach provides a new idea to design effective high-density nonnoble metal oxide nanocatalysts for hydrogenation reactions, which can make full use of sustainable natural biomass. [ABSTRACT FROM AUTHOR]

A new complex, bis[2-(1 H-benzimidazol-2-yl)benzoato]nickel(II) (NiL), has been synthesized and characterized. It was used as catalyst for synthesis of dimethyl carbonate (DMC) from methanol and CO in the presence of dicyclohexyl carbodiimide (DCC) as promoter. The effects of temperature, reaction time, and amount of catalyst on the reaction, and the reusability of the catalyst, were investigated. A catalytic mechanism is proposed. The results revealed that NiL + DCC had excellent catalytic activity, because this catalytic system promoted facile formation of DMC, with acceptable yield, in the presence of a small amount of NiL and under moderate conditions (80 °C, 1.0 MPa). Moreover, the catalyst has been consecutively used five times without significant loss of activity. [ABSTRACT FROM AUTHOR]

Understanding how biophysical and biochemical microenvironmental cues together influence the regenerative activities of muscle stem cells and their progeny is crucial in strategizing remedies for pathological dysregulation of these cues in aging and disease. In this study, we investigated the cell-level influences of extracellular matrix (ECM) ligands and culture substrate stiffness on primary human myoblast contractility and proliferation within 16 h of plating and found that tethered fibronectin led to stronger stiffness-dependent responses compared to laminin and collagen. A proteome-wide analysis further uncovered cell metabolism, cytoskeletal and nuclear component regulation distinctions between cells cultured on soft and stiff substrates. Interestingly, we found that softer substrates increased the incidence of myoblasts with a wrinkled nucleus, and that the extent of wrinkling could predict Ki67 (also known as MKI67) expression. Nuclear wrinkling and Ki67 expression could be controlled by pharmacological manipulation of cellular contractility, offering a potential cellular mechanism. These results provide new insights into the regulation of human myoblast stiffness-dependent contractility response by ECM ligands and highlight a link between myoblast contractility and proliferation., Competing Interests: Competing interests The authors declare no competing or financial interests., (© 2024. Published by The Company of Biologists Ltd.)

Protein phosphorylation plays an important role in various life processes, such as signaling, metabolism, and growth. In addition to the well-known O -phosphorylation, which occurs on serine, threonine and tyrosine side chains, N -phosphorylation, occurring on histidine, arginine and lysine side chains, has attracted much attention. However, due to the chemical instability of N -phosphorylation, the studies on it are still in the nascent stage. In this review, enrichment and detection methods for protein N -phosphorylation are reviewed, and future research in this field is prospected.

Protein persulfidation is an important oxidative translational modification which plays vital roles in many important processes including cellular senescence, endoplasmic reticulum stress, vasorelaxation, and apoptosis. The proteome-wide analysis of persulfidation is of great importance; therefore, this study combines filter-aided sample preparation with an iodoacetic acid functionalized polyamidoamine dendrimer to enrich persulfidated peptides (denoted as filter-aided dendrimer enrichment strategy, FADE). To evaluate the performance of this strategy, the synthetic persulfidated standard peptide was spiked into bovine serum albumin (BSA) digests at a mass ratio of 1:100, and was successfully identified by FADE. Moreover, in combination with stable isotope labelling by amino acids in cell culture technology, the FADE strategy was applied to enrich persulfidated peptides from NaHS-stimulated SHSY5Y cells over a concentration gradient, resulting in the identification of 163 persulfidated peptides. Bioinformatic analysis indicated that persulfidation might play important roles in the central nervous system.