The selective semi-hydrogenation of phenylacetylene(PA)to styrene(ST)represents a critical industrial reaction,essential for producing polymer-grade styrene.Yet,achieving high selectivity at high conversions remains f...The selective semi-hydrogenation of phenylacetylene(PA)to styrene(ST)represents a critical industrial reaction,essential for producing polymer-grade styrene.Yet,achieving high selectivity at high conversions remains fundamentally challenging due to competing overhydrogenation.Here we report an atomic-scale approach for encapsulating ultrafine PtCu(Platinum,Copper)bimetallic nanoclusters(NCs)within the microporous TS-1 zeolite matrix through a ligand-as sis ted hydrothermal strategy.Remarkably,the as-synthesized PtCu@TS-1 catalyst exhibited an unprecedented turnover frequency(TOF)of 2006.7 h^(-1)and a superior styrene yield of 87.7%,significantly surpassing conventional Pt-based catalysts.Advanced characterization and in situ spectroscopy revealed that electron-rich Pt sites,induced by electron transfer from Cu in confined PtCu ensembles,substantially lower the activation barrier for hydrogen dissociation,accelerating selective hydrogenation.Moreover,the atomic confinement effect within the zeolite structure effectively modulates intermediate adsorption and accelerates product desorption,thus overcoming the selectivity-activity tradeoff.This study introduces a generalizable atomic-level catalyst design principle,highlighting the immense potential of quantum-sized bimetallic clusters within porous materials for precisely tuning reaction selectivity and activity.展开更多
Protein phosphorylation is one of the most common post-translational modification processes that play an essential role in regulating protein functionality.The Helicoverpa armigera single nucleopolyhedrovirus (HearNPV...Protein phosphorylation is one of the most common post-translational modification processes that play an essential role in regulating protein functionality.The Helicoverpa armigera single nucleopolyhedrovirus (HearNPV) orf2-encoded nucleocapsid protein HA2 participates in orchestration of virus-induced actin polymerization through its WCA domain,in which phosphorylation status are supposed to be critical in respect to actin polymerization.In the present study,two putative phosphorylation sites (232Thr and 250Ser) and a highly conserved Serine (245Ser) on the WCA domain of HA2 were mutated,and their phenotypes were characterized by reintroducing the mutated HA2 into the HearNPV genome.Viral infectivity assays demonstrated that only the recombinant HearNPV bearing HA2 mutation at 245Ser can produce infectious virions,both 232Thr and 250Ser mutations were lethal to the virus.However,actin polymerization assay demonstrated that all the three viruses bearing HA2 mutations were still capable of initiating actin polymerization in the host nucleus,which indicated the putative phosphorylation sites on HA2 may contribute to HearNPV replication through another unidentified pathway.展开更多
Helicobacter pylori infection is characterized as progressive processes of bacterial persistence and chronic gastritis with features of infiltration of mononuclear cells more than granulocytes in gastric mucosa.Angiop...Helicobacter pylori infection is characterized as progressive processes of bacterial persistence and chronic gastritis with features of infiltration of mononuclear cells more than granulocytes in gastric mucosa.Angiopoietin-like 4(ANGPTL4)is considered a double-edged sword in inflammation-associated diseases,but its function and clinical relevance in H.pylori-associated pathology are unknown.Here,we demonstrate both pro-colonization and pro-inflammation roles of ANGPTL4 in H.pylori infection.Increased ANGPTL4 in the infected gastric mucosa was produced from gastric epithelial cells(GECs)synergistically induced by H.pylori and IL-17A in a cagA-dependent manner.Human gastric ANGPTL4 correlated with H.pylori colonization and the severity of gastritis,and mouse ANGPTL4 from non-bone marrow-derived cells promoted bacteria colonization and inflammation.Importantly,H.pylori colonization and inflammation were attenuated in Il17a-/-,Angptl4-/-,and Il17a-/-Angptl4-/-mice.Mechanistically,ANGPTL4 bound to integrinαV(ITGAV)on GECs to suppress CXCL1 production by inhibiting ERK,leading to decreased gastric influx of neutrophils,thereby promoting H.pylori colonization;ANGPTL4 also bound to ITGAV on monocytes to promote CCL5 production by activating PI3K-AKT-NF-κB,resulting in increased gastric influx of regulatory CD4+T cells(Tregs)via CCL5-CCR4-dependent migration.In turn,ANGPTL4 induced Treg proliferation by binding to ITGAV to activate PI3K-AKT-NF-κB,promoting H.pylori-associated gastritis.Overall,we propose a model in which ANGPTL4 collectively ensures H.pylori persistence and promotes gastritis.Efforts to inhibit ANGPTL4-associated pathway may prove valuable strategies in treating H.pylori infection.展开更多
基金financially supported by the Taishan Scholar Program of Shandong Province(No.tsqn202408211)China Postdoctoral Science Foundation(No.2024M761141)+3 种基金Postdoctoral Fellowship Program of CPSF(No.GZC20250785)Postdoctoral Innovation Program of Shandong Province(No.SDCX-ZG-202503085)Shandong Excellent YoungScientists Fund Program(No.2022HWYQ-082)National Natural Science Foundation of China(Nos.22278174,21808079,and 22378159)
文摘The selective semi-hydrogenation of phenylacetylene(PA)to styrene(ST)represents a critical industrial reaction,essential for producing polymer-grade styrene.Yet,achieving high selectivity at high conversions remains fundamentally challenging due to competing overhydrogenation.Here we report an atomic-scale approach for encapsulating ultrafine PtCu(Platinum,Copper)bimetallic nanoclusters(NCs)within the microporous TS-1 zeolite matrix through a ligand-as sis ted hydrothermal strategy.Remarkably,the as-synthesized PtCu@TS-1 catalyst exhibited an unprecedented turnover frequency(TOF)of 2006.7 h^(-1)and a superior styrene yield of 87.7%,significantly surpassing conventional Pt-based catalysts.Advanced characterization and in situ spectroscopy revealed that electron-rich Pt sites,induced by electron transfer from Cu in confined PtCu ensembles,substantially lower the activation barrier for hydrogen dissociation,accelerating selective hydrogenation.Moreover,the atomic confinement effect within the zeolite structure effectively modulates intermediate adsorption and accelerates product desorption,thus overcoming the selectivity-activity tradeoff.This study introduces a generalizable atomic-level catalyst design principle,highlighting the immense potential of quantum-sized bimetallic clusters within porous materials for precisely tuning reaction selectivity and activity.
基金National Nature Science Foundations of China (31030027,30770085 and 30800044)
文摘Protein phosphorylation is one of the most common post-translational modification processes that play an essential role in regulating protein functionality.The Helicoverpa armigera single nucleopolyhedrovirus (HearNPV) orf2-encoded nucleocapsid protein HA2 participates in orchestration of virus-induced actin polymerization through its WCA domain,in which phosphorylation status are supposed to be critical in respect to actin polymerization.In the present study,two putative phosphorylation sites (232Thr and 250Ser) and a highly conserved Serine (245Ser) on the WCA domain of HA2 were mutated,and their phenotypes were characterized by reintroducing the mutated HA2 into the HearNPV genome.Viral infectivity assays demonstrated that only the recombinant HearNPV bearing HA2 mutation at 245Ser can produce infectious virions,both 232Thr and 250Ser mutations were lethal to the virus.However,actin polymerization assay demonstrated that all the three viruses bearing HA2 mutations were still capable of initiating actin polymerization in the host nucleus,which indicated the putative phosphorylation sites on HA2 may contribute to HearNPV replication through another unidentified pathway.
基金supported by grants of the National Natural Science Foundation of China(82000530,82071744,82070578,81870394,32160208,and 82170628)Outstanding Scientific Youth Fund of Guizhou Province(Qiankehe platform talents 2021-5647,Qiankehe platform talents GCC[2023]040)+4 种基金Key Projects of Guizhou Provincial Basic Research Program(Qiankehe foundation-ZK 2021-major project 004)Collaborative Innovation Center of Chinese Ministry of Education(2020-39)Joint project of Chongqing Health Commission and Science and Technology Bureau(2023MSXM004)Sichuan Science and Technology Program(2022ZYD0071)The General Hospital of Western Theater Command(2021-XZYG-B24).
文摘Helicobacter pylori infection is characterized as progressive processes of bacterial persistence and chronic gastritis with features of infiltration of mononuclear cells more than granulocytes in gastric mucosa.Angiopoietin-like 4(ANGPTL4)is considered a double-edged sword in inflammation-associated diseases,but its function and clinical relevance in H.pylori-associated pathology are unknown.Here,we demonstrate both pro-colonization and pro-inflammation roles of ANGPTL4 in H.pylori infection.Increased ANGPTL4 in the infected gastric mucosa was produced from gastric epithelial cells(GECs)synergistically induced by H.pylori and IL-17A in a cagA-dependent manner.Human gastric ANGPTL4 correlated with H.pylori colonization and the severity of gastritis,and mouse ANGPTL4 from non-bone marrow-derived cells promoted bacteria colonization and inflammation.Importantly,H.pylori colonization and inflammation were attenuated in Il17a-/-,Angptl4-/-,and Il17a-/-Angptl4-/-mice.Mechanistically,ANGPTL4 bound to integrinαV(ITGAV)on GECs to suppress CXCL1 production by inhibiting ERK,leading to decreased gastric influx of neutrophils,thereby promoting H.pylori colonization;ANGPTL4 also bound to ITGAV on monocytes to promote CCL5 production by activating PI3K-AKT-NF-κB,resulting in increased gastric influx of regulatory CD4+T cells(Tregs)via CCL5-CCR4-dependent migration.In turn,ANGPTL4 induced Treg proliferation by binding to ITGAV to activate PI3K-AKT-NF-κB,promoting H.pylori-associated gastritis.Overall,we propose a model in which ANGPTL4 collectively ensures H.pylori persistence and promotes gastritis.Efforts to inhibit ANGPTL4-associated pathway may prove valuable strategies in treating H.pylori infection.
