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Numerous reported bioinspired osmotic energy conversion systems employing cation‐/anion‐selective membranes and solutions with different salinity are actually far from the biological counterpart. The iso‐osmotic power generator with the specific ionic permselective channels (e.g. K+ or Na+ channels) which just allow specific ions to get across and iso‐osmotic solutions still remain challenges. Inspired by nature, we report a bioinspired K+‐channel by employing a K+ selective ligand, 1,1,1‐tris{[(2′‐benzylaminoformyl)phenoxy]methyl}ethane (BMP) and graphene oxide membrane. Specifically, the K+ and Na+ selectivity of the prepared system could reach up to ≈17.8, and the molecular dynamics simulation revealed that the excellent permselectivity of K+ mainly stemmed from the formed suitable channel size. Thus, we assembled the K+‐selective iso‐osmotic power generator (KSIPG) with the power density up to ≈15.1 mW/m2 between equal concentration solutions, which is higher than traditional charge‐selective osmotic power generator (CSOPG). The proposed strategy has well shown the realizable approach to construct single‐ion selective channels‐based highly efficient iso‐osmotic energy conversion systems and would surely inspire new applications in other fields, including self‐powered systems and medical materials, etc. [ABSTRACT FROM AUTHOR]

Background: Aberrant activation of Wnt/β-catenin signaling by dysregulated post-translational protein modifications, especially ubiquitination is causally linked to cancer development and progression. Although Lys48-linked ubiquitination is known to regulate Wnt/β-catenin signaling, it remains largely obscure how other types of ubiquitination, such as linear ubiquitination governs its signaling activity. Methods: The expression and regulatory mechanism of linear ubiquitin chain assembly complex (LUBAC) on Wnt/β-catenin signaling was examined by immunoprecipitation, western blot and immunohistochemical staining. The ubiquitination status of β-catenin was detected by ubiquitination assay. The impacts of SHARPIN, a core component of LUBAC on malignant behaviors of gastric cancer cells were determined by various functional assays in vitro and in vivo. Results: Unlike a canonical role in promoting linear ubiquitination, SHARPIN specifically interacts with β-catenin to maintain its protein stability. Mechanistically, SHARPIN competes with the E3 ubiquitin ligase β-Trcp1 for β-catenin binding, thereby decreasing β-catenin ubiquitination levels to abolish its proteasomal degradation. Importantly, SHARPIN is required for invasiveness and malignant growth of gastric cancer cells in vitro and in vivo, a function that is largely dependent on its binding partner β-catenin. In line with these findings, elevated expression of SHARPIN in gastric cancer tissues is associated with disease malignancy and correlates with β-catenin expression levels. Conclusions: Our findings reveal a novel molecular link connecting linear ubiquitination machinery and Wnt/β-catenin signaling via SHARPIN-mediated stabilization of β-catenin. Targeting the linear ubiquitination-independent function of SHARPIN could be exploited to inhibit the hyperactive β-catenin signaling in a subset of human gastric cancers. [ABSTRACT FROM AUTHOR]

Three analogous lanthanide-containing complexes were isolated, with the molecular formula [Ln4(μ3-OH)2(tmhd)4L6]·2CH3CN (where Ln = Eu(1), Gd(2) and Dy(3); HL = 5-phenyl-8-hydroxylquinoline; and Htmhd = 2,2,6,6-tetramethyl-3,5-heptanedione). Single-crystal X-ray diffraction measurements performed on 1–3 revealed that they were all composed of [Ln4(μ3-OH)2] centers with butterfly-shaped arrangements. Investigations into the luminescence properties and lifetime of 1 showed characteristic emission peaks of the Eu3+ ion and an average luminescence lifetime of 9.26 μs. Detailed magnetic studies suggested that antiferromagnetic interactions existed in 2 and 3, and that there was a remarkable magnetocaloric effect with a −ΔSm value of 17.94 J K−1 kg−1 for 2, and a slow magnetic relaxation process with an energy barrier ΔE/kB of 35.8 K for 3. [ABSTRACT FROM AUTHOR]