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  1. Article ; Online: The Influence of Surface Processing on the Surface Plasmonic Enhancement of an Al-Nanoparticles-Enhanced ZnO UV Photodectector

    Gaoming Li / Qianwen Yan / Xiaolong Zhao / Yongning He

    Nanomaterials, Vol 13, Iss 1877, p

    2023  Volume 1877

    Abstract: Surface Plasmonic Resonance (SPR) induced by metallic nanoparticles can be exploited to enhance the response of photodetectors (PD) to a large degree. Since the interface between metallic nanoparticles and semiconductors plays an important role in SPR, ... ...

    Abstract Surface Plasmonic Resonance (SPR) induced by metallic nanoparticles can be exploited to enhance the response of photodetectors (PD) to a large degree. Since the interface between metallic nanoparticles and semiconductors plays an important role in SPR, the magnitude of the enhancement is highly dependent on the morphology and roughness of the surface where the nanoparticles are distributed. In this work, we used mechanical polishing to produce different surface roughnesses for the ZnO film. Then, we exploited sputtering to fabricate Al nanoparticles on the ZnO film. The size and spacing of the Al nanoparticles were adjusted by sputtering power and time. Finally, we made a comparison among the PD with surface processing only, the Al-nanoparticles-enhanced PD, and the Al-nanoparticles-enhanced PD with surface processing. The results showed that increasing the surface roughness could enhance the photo response due to the augmentation of light scattering. More interestingly, the SPR induced by the Al nanoparticles could be strengthened by increasing the roughness. The responsivity could be enlarged by three orders of magnitude after we introduced surface roughness to boost the SPR. This work revealed the mechanism behind how surface roughness influences SPR enhancement. This provides new means for improving the photo responses of SPR-enhanced photodetectors.
    Keywords surface processing ; localized surface plasmon ; Al nanoparticles ; ZnO UV photodetector ; Chemistry ; QD1-999
    Subject code 620
    Language English
    Publishing date 2023-06-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Glycometabolism regulates hepatitis C virus release.

    Tao Yu / Qiankun Yang / Fangling Tian / Haishuang Chang / Zhenzheng Hu / Bowen Yu / Lin Han / Yifan Xing / Yaming Jiu / Yongning He / Jin Zhong

    PLoS Pathogens, Vol 17, Iss 7, p e

    2021  Volume 1009746

    Abstract: HCV cell-culture system uses hepatoma-derived cell lines for efficient virus propagation. Tumor cells cultured in glucose undergo active aerobic glycolysis, but switch to oxidative phosphorylation for energy production when cultured in galactose. Here, ... ...

    Abstract HCV cell-culture system uses hepatoma-derived cell lines for efficient virus propagation. Tumor cells cultured in glucose undergo active aerobic glycolysis, but switch to oxidative phosphorylation for energy production when cultured in galactose. Here, we investigated whether modulation of glycolysis in hepatocytes affects HCV infection. We showed HCV release, but not entry, genome replication or virion assembly, is significantly blocked when cells are cultured in galactose, leading to accumulation of intracellular infectious virions within multivesicular body (MVB). Blockade of the MVB-lysosome fusion or treatment with pro-inflammatory cytokines promotes HCV release in galactose. Furthermore, we found this glycometabolic regulation of HCV release is mediated by MAPK-p38 phosphorylation. Finally, we showed HCV cell-to-cell transmission is not affected by glycometabolism, suggesting that HCV cell-to-supernatant release and cell-to-cell transmission are two mechanistically distinct pathways. In summary, we demonstrated glycometabolism regulates the efficiency and route of HCV release. We proposed HCV may exploit the metabolic state in hepatocytes to favor its spread through the cell-to-cell transmission in vivo to evade immune response.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2021-07-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Structure of human M-type phospholipase A2 receptor revealed by cryo-electron microscopy

    Dong, Yue / Hua Tang / Longxing Cao / Xiangyi Shi / Yongning He

    Journal of Molecular Biology. 2017,

    2017  

    Abstract: M-type phospholipase A2 receptor (M-PLA2R) is a member of the mannose receptor family and known as the receptor of secretory phospholipase A2s (sPLA2s). It has also been identified as the major autoantigen of idiopathic membranous nephropathy, one of the ...

    Abstract M-type phospholipase A2 receptor (M-PLA2R) is a member of the mannose receptor family and known as the receptor of secretory phospholipase A2s (sPLA2s). It has also been identified as the major autoantigen of idiopathic membranous nephropathy, one of the most common causes for nephrotic syndrome in adults. Here we determine the structure of human M-PLA2R ectodomain by cryo-electron microscopy. The results show that the ectodomain has high internal flexibility and forms a compact dual-ring shaped conformation at acidic pH, and adopts extended conformations at basic pH. The inter-domain interactions of human M-PLA2R are explored by the binding studies with individual domains, showing the mechanism of the conformational change. In addition, the biochemical data suggests that mouse M-PLA2R recognizes mouse sPLA2-G1B only at physiological or basic pH, rather than at acidic pH. These results suggest that the pH-dependent conformational change might play important roles in the functional activities of M-PLA2R such as ligand binding and release, and may also be relevant to the immunogenicity in membranous nephropathy.
    Keywords adults ; cryo-electron microscopy ; humans ; immune response ; ligands ; mannose ; mice ; nephrotic syndrome ; pH ; phospholipase A2 ; phospholipases
    Language English
    Size p. .
    Publishing place Elsevier Ltd
    Document type Article
    Note Pre-press version
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2017.10.019
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Structural basis for the multi-activity factor Rad5 in replication stress tolerance

    Miaomiao Shen / Nalini Dhingra / Quan Wang / Chen Cheng / Songbiao Zhu / Xiaolin Tian / Jun Yu / Xiaoxin Gong / Xuzhichao Li / Hongwei Zhang / Xin Xu / Liting Zhai / Min Xie / Ying Gao / Haiteng Deng / Yongning He / Hengyao Niu / Xiaolan Zhao / Song Xiang

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Volume 12

    Abstract: Rad5 is a hub connecting three replication stress tolerance pathways. Here, the authors present the 3.3 Å crystal structure of a N-terminal truncated K.lactis Rad5 construct that reveals the spatial arrangement of the HIRAN, Snf2 and RING domains and ... ...

    Abstract Rad5 is a hub connecting three replication stress tolerance pathways. Here, the authors present the 3.3 Å crystal structure of a N-terminal truncated K.lactis Rad5 construct that reveals the spatial arrangement of the HIRAN, Snf2 and RING domains and structure-guided in vitro and in vivo experiments reveal multiple activities of the yeast Rad5 HIRAN domain among them a role in binding PCNA and supporting its ubiquitination.
    Keywords Science ; Q
    Language English
    Publishing date 2021-01-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Cbln1 and Cbln4 Are Structurally Similar but Differ in GluD2 Binding Interactions

    Chen Zhong / Jinlong Shen / Huibing Zhang / Guangyi Li / Senlin Shen / Fang Wang / Kuan Hu / Longxing Cao / Yongning He / Jianping Ding

    Cell Reports, Vol 20, Iss 10, Pp 2328-

    2017  Volume 2340

    Abstract: Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and δ-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing ∼70% sequence identity with Cbln1. Here, we ... ...

    Abstract Unlike cerebellin 1 (Cbln1), which bridges neurexin (Nrxn) receptors and δ-type glutamate receptors in a trans-synaptic triad, Cbln4 was reported to have no or weak binding for the receptors despite sharing ∼70% sequence identity with Cbln1. Here, we report crystal structures of the homotrimers of the C1q domain of Cbln1 and Cbln4 at 2.2 and 2.3 Å resolution, respectively. Comparison of the structures suggests that the difference between Cbln1 and Cbln4 in GluD2 binding might be because of their sequence and structural divergence in loop CD. Surprisingly, we show that Cbln4 binds to Nrxn1β and forms a stable complex with the laminin, nectin, sex-hormone binding globulin (LNS) domain of Nrxn1β. Furthermore, the negative-stain electron microscopy reconstruction of hexameric full-length Cbln1 at 13 Å resolution and that of the Cbln4/Nrxn1β complex at 19 Å resolution suggest that Nrxn1β binds to the N-terminal region of Cbln4, probably through strand β10 of the S4 insert.
    Keywords Cbln1 ; Cbln4 ; C1q domain ; C1q/TNF superfamily ; neurexin ; receptor specificity ; synaptogenesis ; Nrxn1β ; synapse ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2017-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Human immunoglobulin G hinge regulates agonistic anti-CD40 immunostimulatory and antitumour activities through biophysical flexibility

    Xiaobo Liu / Yingjie Zhao / Huan Shi / Yan Zhang / Xueying Yin / Mingdong Liu / Huihui Zhang / Yongning He / Boxun Lu / Tengchuan Jin / Fubin Li

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 15

    Abstract: Conserved regions of the antibody molecule impact its downstream biological effects. Here the authors show that a rigid hinge conformation increases the agonistic activity of CD40 and DR5 antibodies, distinctly from FcγR-binding, suggesting that the ... ...

    Abstract Conserved regions of the antibody molecule impact its downstream biological effects. Here the authors show that a rigid hinge conformation increases the agonistic activity of CD40 and DR5 antibodies, distinctly from FcγR-binding, suggesting that the hinge and FcR binding regions can be separately modified to optimize therapies.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Human immunoglobulin G hinge regulates agonistic anti-CD40 immunostimulatory and antitumour activities through biophysical flexibility

    Xiaobo Liu / Yingjie Zhao / Huan Shi / Yan Zhang / Xueying Yin / Mingdong Liu / Huihui Zhang / Yongning He / Boxun Lu / Tengchuan Jin / Fubin Li

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 15

    Abstract: Conserved regions of the antibody molecule impact its downstream biological effects. Here the authors show that a rigid hinge conformation increases the agonistic activity of CD40 and DR5 antibodies, distinctly from FcγR-binding, suggesting that the ... ...

    Abstract Conserved regions of the antibody molecule impact its downstream biological effects. Here the authors show that a rigid hinge conformation increases the agonistic activity of CD40 and DR5 antibodies, distinctly from FcγR-binding, suggesting that the hinge and FcR binding regions can be separately modified to optimize therapies.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Functional expression and characterization of the envelope glycoprotein E1E2 heterodimer of hepatitis C virus.

    Longxing Cao / Bowen Yu / Dandan Kong / Qian Cong / Tao Yu / Zibo Chen / Zhenzheng Hu / Haishuang Chang / Jin Zhong / David Baker / Yongning He

    PLoS Pathogens, Vol 15, Iss 5, p e

    2019  Volume 1007759

    Abstract: Hepatitis C virus (HCV) is a member of Hepacivirus and belongs to the family of Flaviviridae. HCV infects millions of people worldwide and may lead to cirrhosis and hepatocellular carcinoma. HCV envelope proteins, E1 and E2, play critical roles in viral ... ...

    Abstract Hepatitis C virus (HCV) is a member of Hepacivirus and belongs to the family of Flaviviridae. HCV infects millions of people worldwide and may lead to cirrhosis and hepatocellular carcinoma. HCV envelope proteins, E1 and E2, play critical roles in viral cell entry and act as major epitopes for neutralizing antibodies. However, unlike other known flaviviruses, it has been challenging to study HCV envelope proteins E1E2 in the past decades as the in vitro expressed E1E2 heterodimers are usually of poor quality, making the structural and functional characterization difficult. Here we express the ectodomains of HCV E1E2 heterodimer with either an Fc-tag or a de novo designed heterodimeric tag and are able to isolate soluble E1E2 heterodimer suitable for functional and structural studies. Then we characterize the E1E2 heterodimer by electron microscopy and model the structure by the coevolution based modeling strategy with Rosetta, revealing the potential interactions between E1 and E2. Moreover, the E1E2 heterodimer is applied to examine the interactions with the known HCV receptors, neutralizing antibodies as well as the inhibition of HCV infection, confirming the functionality of the E1E2 heterodimer and the binding profiles of E1E2 with the cellular receptors. Therefore, the expressed E1E2 heterodimer would be a valuable target for both viral studies and vaccination against HCV.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2019-05-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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