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Supramolecular Integration of 18-Crown-6 and an N-Capped Short Peptide Enables Multivalent Recognition and Modulation of Amyloid-β Proteotoxicity
Influence of molecular structure and size of cyclic and spherical carbon allotropes on high-order harmonic generation efficiency: a TDDFT study
Chromatin landscape and epigenetic heterogeneity of acute myeloid leukaemia
Revealing the Topological Analogy between End-Linked and Pendant Cross-Linked Polymer Networks for Mechanophore-Enabled Toughening
Public genomic surveillance of African Klebsiella pneumoniae species complex reveals uneven sampling and high ESBL gene carriage
Diet–microbiome synergy underlies obesity-associated immunotherapy efficacy
Revisiting Purported Solvothermal “Black Phosphorus”: Beyond Elemental Allotrope to Organic Ammonium Polyphosphides
l-Tartaric acid mitigates diabetic cardiac damage and is associated with changes in autophagy, apoptosis, and inflammatory markers
Intergenerational mobility fosters innovation in Europe
S-to-O Atom Swapping Unlocks a Promising Difuranphthalimide-Based Polymer Donor with Efficiency over 20%
Synergistic effect of carbon fabric metastructure and magnetic layers in a composite for electromagnetic radiation shielding
Abstract The widespread use of high-frequency electromagnetic radiation (EMR) in communication, defense, medical, and household technologies raises health and safety concerns, underscoring the demand for efficient shielding and absorption materials. This work presents flexible protective composites based on conductive carbon fabric coated with thin magnetic polymer films. Several multilayer configurations were prepared and characterized, consisting of carbon fabric coated with epoxy polymer layers containing Ni or Fe $$_2$$ O $$_3$$ fillers. The shielding performance, primarily governed by the fabric’s regular metastructure, exhibits strong polarization dependence in the $$90-330$$ GHz range. The combined interaction of conductive carbon fabric and magneto-responsive polymer layers enhances absorption, induces multiple resonances, and broadens the effective shielding bandwidth, resulting in significantly reduced reflection across a wide spectral range.
Architecture of the 8 MDa Hdr–Vhu–Fwd super-assembly in class I methanogens
Abstract Methanogens are central to global carbon cycling and among the largest biological sources of methane, a potent greenhouse gas 1 . At the heart of their energy metabolism lies the Hdr–Vhu–Fwd super-assembly, which couples H 2 oxidation with CO 2 reduction through flavin-based electron bifurcation. Here we present the cryogenic electron microscopy structure of the Hdr–Vhu–Fwd super-assembly from Methanococcus maripaludis , revealing an 8 MDa complex comprising 252 polypeptide chains and over 600 redox cofactors. Cryo-electron tomography further support that this super-assembly forms an intact structure within the cytoplasm of intact cells. This architecture comprises two hexameric HdrABC–Vhu rings linked by a tetrameric FwdF core, forming a continuous, circular electron chain. In this unique arrangement, 12 polyferredoxin subunits (VhuB) connect the Vhu–Hdr and Fwd complexes, thereby coupling electron bifurcation with CO 2 reduction and directly linking the last and the first step of methanogenesis. Moreover, we identify a modular variant of the complex in which the [NiFe]-hydrogenase Vhu is substituted by tungsten-containing formate dehydrogenase (FdhAB), indicating flexible integration of electron-input modules facilitating metabolic adaptation under diverse environmental conditions 2 . Analysis of the taxonomic distribution reveals that this architecture is specific to class I methanogens and is distinct from the smaller Hdr–Fmd complex of class II 3 . Together, our study reveals that the the Hdr–Vhu–Fwd super-assembly has a modular and adaptable bioenergetic assembly, suggesting a lineage-specific architecture to adapt to diverse anaerobic niches.
Correction to “Photoactive Iminobismuthanes for Catalytic C–H Amination”
PALLADIN regulates osteogenic differentiation of bone marrow mesenchymal stem cells and protects against bone loss in ovariectomized mice
Abstract Osteoporosis is a systemic skeletal disease associated with reduced bone density and impaired bone quality, which leading to a greater risk of fracture. The pathogenesis of osteoporosis is closely associated with compromised osteogenic differentiation of bone marrow mesenchymal stem cells (BMSCs). The actin-cytoskeleton associated protein PALLADIN has been reported to play a central role in the remodeling of the actin-cytoskeleton. However, no studies to date have established whether PALLADIN can influence osteogenic differentiation of BMSCs or the onset of osteoporosis. Here, PALLADIN knockdown was observed to reduce osteogenic differentiation of BMSCs, confirming the involvement of the gene in osteoporosis. Knockdown also altered the cytoskeletal organization and reduced Ras homolog family member A (RhoA) activity to inhibit osteogenic differentiation. The results of the in vivo experiments showed that overexpression of Palladin reversed bone loss and marrow adipose tissue (MAT) accumulation in OVX mice, while Palladin knockdown increased both bone loss and MAT accumulation in OVX mice. Together, these results suggest a model in which Palladin protects against bone loss induced by OVX through the promotion of BMSCs osteogenesis. In human osteoporotic BMSCs, PALLADIN expression is significantly downregulated, correlating with disease status. While functional validation in primary human osteoporotic BMSCs remains to be performed, these preclinical findings establish Palladin as a novel regulator of BMSCs osteogenic differentiation and provide a foundation for future efforts to characterize the pathogenesis of osteoporosis and identify new therapeutic targets.