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Showing 1–13 of 13 results
Advanced filters: Author: "Yong Xiong" Clear advanced filters

  • Despite effective vaccines against SARS-CoV-2, therapeutic options such as anti-virals and neutralizing antibodies are critical in treating disease, especially given the breakthrough infections of emerging VOCs. Here, Peng et al. generate two potent monoclonal antibodies and a bispecific antibody with two antigenrecognition variable regions targeting SARS-CoV-2 spike, provide CryoEM structures and show in vitro and in vivo efficacy of a humanized antibody against wildtype virus and delta variant.

    • Lei Peng
    • Yingxia Hu
    • Sidi Chen
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • By using nuclear pore complex mimics, the authors demonstrate that the cytoplasm-facing Nup358 provides a dock for the HIV-1 capsid, and the nucleoplasm-facing Nup153 positions the capsid for NPC entry. Nup358 and Nup153 thus create an affinity gradient which regulates capsid penetration, whereas Nup62 constitutes a final NPC gatekeeper against HIV-1 capsid entry.

    • Qi Shen
    • Qingzhou Feng
    • Yong Xiong
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 425-435

  • The HIV-1 Nef protein associates with the cytoplasmic domain of class I MHC and with the μ1 subunit of clathin adaptor protein complex I, rerouting MHC I to the endolysosomal degradation pathway. The molecular mechanism for this effect is now revealed by the crystal structure of Nef together with MHC I and a domain from μ1.

    • Xiaofei Jia
    • Rajendra Singh
    • Yong Xiong
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 701-706

  • FAN1 is a structure-specific nuclease that plays a major role in eliminating highly cytotoxic interstrand DNA crosslinks. Here, Zhao et al. present several crystal structures of FAN1 in complex with DNA substrates and biochemical analyses that establish how FAN1 functions to resolve interstrand DNA crosslinks.

    • Qi Zhao
    • Xiaoyu Xue
    • Yong Xiong
    Research
    Nature Communications
    Volume: 5, P: 1-9

  • Many pathogens manipulate ubiquitin-mediated signaling to evade host cell defense. Here, the authors characterize the structure and enzymatic activity of a deubiquitylase domain from the causative pathogen of scrub typhus, providing evidence for a distinct mechanism of ubiquitin chain selectivity.

    • Jason M. Berk
    • Christopher Lim
    • Mark Hochstrasser
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-17

  • Cryo-EM structure of the C-terminal domain of human APOBEC3F in complex with HIV-1 Vif and CFBβ, along with functional analyses, reveals how Vif targets a host restriction protein.

    • Yingxia Hu
    • Belete A. Desimmie
    • Yong Xiong
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 1176-1183

  • The sterile alpha-motif and histidine-aspartate domain-containing protein 1 (SAMHD1) is a dNTP phosphohydrolase that blocks HIV-1 infection by depleting cellular dNTPs. Here the authors present the structures of full-length mouse SAMHD1 in different nucleotide bound states and give insights into SAMHD1 activity regulation.

    • Olga Buzovetsky
    • Chenxiang Tang
    • Yong Xiong
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-9

  • Recent studies offer new insight on the mechanisms of IP6-mediated HIV-1 capsid assembly. The immature Gag lattice enables enrichment of IP6 into virions, aiding capsid maturation. Structures of capsid protein (CA) assemblies reveal motifs serving as switches modulating the conformations of CA pentamers/hexamers and affect co-factor accessibility.

    • Chunxiang Wu
    • Yong Xiong
    News & Views
    Nature Structural & Molecular Biology
    Volume: 30, P: 239-241

  • The conserved MHF1/MHF2 DNA-processing complex is essential for DNA repair in response to genotoxic stress. Here, Zhao et al.report the crystal structure of a human MHF–DNA complex that provides insight into how MHF recognizes branched DNA—a feature important for cellular resistance to DNA damage.

    • Qi Zhao
    • Dorina Saro
    • Yong Xiong
    Research
    Nature Communications
    Volume: 5, P: 1-12

  • The dNTPase SAMHD1 inhibits infection by HIV-1 and other retroviruses. In the presence of dGTP, the enzyme forms tetramers and becomes active, a process that is now elucidated by structural, biochemical and cellular analyses of human SAMHD1. Binding of dGTP to four allosteric sites promotes tetramerization and induces a conformational change in the substrate-binding pocket to activate the enzyme.

    • Xiaoyun Ji
    • Ying Wu
    • Yong Xiong
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1304-1309