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Stiff interlocked nanoclay aerogels for synergistic detection and removal of organic contaminants in water
The Dendritic Cell-based Vaccine PROTEXI leverages Antiviral CD4 T cell Memory to boost anti-tumor immune responses in mice
Host-derived lactic acid disrupts IFN efficacy via antiviral inhibition and proinflammatory amplification
Direct electrosynthesis of acetamide from CO2 and nitrate via an atomically engineered dual-site catalyst
Personalized Phage Therapy in an ICU Patient with Polymicrobial Pulmonary Infections: a case from a single-arm trial
β-cell FMO3-produced TMAO prevents NF-κB-mediated senescence and inflammation in ageing and diabetic conditions
CmDREBa regulates the perennial growth habit of chrysanthemum in response to prolonged chilling
Immunological maladaptation preceding spontaneous preterm birth in human pregnancies
Abstract The majority of spontaneous preterm births (sPTB) occurs without identifiable clinical indications or apparent risk factors. A dysregulated maternal immune adaptation at delivery has been associated with sPTB. Yet, a precise understanding of maternal immune dynamics preceding sPTB remains lacking. Here we show, in a nested case-control study within a low-risk, population-based pregnancy cohort, that an abnormal immune adaptation in mothers’ blood precedes sPTB by weeks to months and discriminates sPTB cases from term controls (AUROC: 0.7). Prominent features include enhanced immune cell responses to an adrenergic stimulus during the first and second trimesters, followed by increased production of pro-inflammatory cytokines in the third trimester in sPTB vs. term pregnancies. Transcriptome analysis of second trimester single-cell CD4 + T cells reveals a Th17-skewed, neuroactive-protein responsive phenotype in sPTB pregnancies. Our study provides a multi-omics resource and a conceptual framework for early identification of individuals at increased risk for sPTB with broad translational implications for advancing targeted preventive measures.
Nematic and chiral superconductivity emerging within the loop-current phase in kagome metals
Abstract The kagome metals A V 3 Sb 5 ( A = Cs, Rb, K) host multiple symmetry-breaking phases, including charge-density-wave and loop-current orders, and exhibit highly exotic superconductivity with pronounced nematicity and chirality. Remarkably, even dilute impurities transform this exotic superconducting state into an isotropic s -wave state. These observations pose a challenge to existing theoretical scenarios. We show that loop-current order induces nematic chiral d -wave superconductivity in kagome metals. The loop-current-induced orbital magnetization (OM) stabilizes one chiral superconducting channels. This OM-chirality coupling mechanism is generic and applies to pairing driven by either attractive or repulsive interactions. Furthermore, coexisting loop-current and bond orders give rise to pronounced nematic chiral superconductivity even for an almost C 6 -symmetric Fermi surface. For attractive pairing, dilute impurities suppress the chiral state and restore a conventional s -wave phase, as observed experimentally. The theory further predicts a robust 2 × 2 pair-density modulation. This study provides key insights into time-reversal-symmetry-breaking exotic superconductivity in kagome metals.
Luminescence meets physical unclonability in fracture engineered porous polymer skeletons for anticounterfeiting
Microbial drought resistance is achieved at the expense of soil carbon loss
SLC26A11 is an atypical solute carrier with dual transport-channel function mediating lysosomal sulfate transport
Abstract Membrane transporters and channels are generally assumed to be based on distinct structural and functional principles. SLC26A11, a solute carrier with high expression levels in the brain, has been proposed to function as either an anion transporter or a channel. Here, we resolve this apparent discrepancy by demonstrating that SLC26A11 is a dual-function protein capable of operating as both a sulfate transporter and a chloride channel. By resolving its structure and combining biochemical studies and molecular dynamics simulations, we show that SLC26A11 exhibits all the hallmarks of a secondary transporter. The mechanistic basis for its selective ion transport identifies the protein as the elusive lysosomal sulfate exporter. Additionally, we demonstrate that SLC26A11 exhibits an uncoupled, channel-like chloride conductance gated by proton:sulfate symport. Our finding that the chloride-conducting state arises from the transport cycle may contribute to the development of therapeutic strategies for treating brain edema, and the identification of its role in lysosome sulfate efflux may provide new approaches to study and treat lysosomal storage diseases.