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unfolded protein response

  • N-Linked Glycosylation Plays an Important Role in Budding of Neuraminidase Protein and Virulence of Influenza Viruses
    Structure and Assembly
    N-Linked Glycosylation Plays an Important Role in Budding of Neuraminidase Protein and Virulence of Influenza Viruses

    NA is a highly glycosylated protein. Nevertheless, how the NLG affects the function of NA protein remains largely unclear.

    Danqi Bao, Ruixue Xue, Min Zhang, Chenyang Lu, Tianxin Ma, Chaochao Ren, Ting Zhang, Jianmei Yang, Qiaoyang Teng, Xuesong Li, Zejun Li, Qinfang Liu
  • Pharmacologic Activation of Lytic Epstein-Barr Virus Gene Expression without Virion Production
    Genome Replication and Regulation of Viral Gene Expression
    Pharmacologic Activation of Lytic Epstein-Barr Virus Gene Expression without Virion Production

    Epstein-Barr virus is associated with many different cancers. In these cancers the viral genome is predominantly latent; i.e., most viral genes are not expressed, most viral proteins are not synthesized, and new virions are not produced. Some strategies for treating these cancers involve activation of lytic viral gene expression. We identify an antibacterial antibiotic, clofoctol, that is an activator of EBV lytic RNA and protein...

    Jaeyeun Lee, John G. Kosowicz, S. Diane Hayward, Prashant Desai, Jennifer Stone, Jae Myun Lee, Jun O. Liu, Richard F. Ambinder
  • The Human Cytomegalovirus Endoplasmic Reticulum-Resident Glycoprotein UL148 Activates the Unfolded Protein Response
    Cellular Response to Infection
    The Human Cytomegalovirus Endoplasmic Reticulum-Resident Glycoprotein UL148 Activates the Unfolded Protein Response

    The unfolded protein response (UPR) is an ancient cellular response to ER stress that is of broad importance to viruses. Certain consequences of the UPR, including mRNA degradation and translational shutoff, would presumably be disadvantageous to viruses, while other attributes of the UPR, such as ER expansion and upregulation of protein folding chaperones, might enhance viral replication. Although HCMV is estimated to express well over...

    Mohammed N. A. Siddiquey, Hongbo Zhang, Christopher C. Nguyen, Anthony J. Domma, Jeremy P. Kamil
  • Cellular Response to Infection
    The PERK Arm of the Unfolded Protein Response Negatively Regulates Transmissible Gastroenteritis Virus Replication by Suppressing Protein Translation and Promoting Type I Interferon Production

    The induction of ER stress is a common outcome in cells infected with coronaviruses. The UPR initiated by ER stress is actively involved in viral replication and modulates the host innate responses to the invading viruses, but these underlying mechanisms remain incompletely understood. We show here that infection with the alphacoronavirus TGEV elicited ER stress in vitro and in vivo, and the UPR PERK-eIF2α branch was...

    Mei Xue, Fang Fu, Yanlong Ma, Xin Zhang, Liang Li, Li Feng, Pinghuang Liu
  • Virus-Cell Interactions
    Deficiency of the IRE1α-Autophagy Axis Enhances the Antitumor Effects of the Oncolytic Virus M1
    Kai Li, Cheng Hu, Fan Xing, Mingshi Gao, Jiankai Liang, Xiao Xiao, Jing Cai, Yaqian Tan, Jun Hu, Wenbo Zhu, Wei Yin, Yuan Li, Wenli Chen, Bingzheng Lu, Jialuo Mai, Pengxin Qiu, Xingwen Su, Guangmei Yan, Haipeng Zhang, Yuan Lin
  • Free
    Virus-Cell Interactions | Spotlight
    Zika Virus Hijacks Stress Granule Proteins and Modulates the Host Stress Response
    Shangmei Hou, Anil Kumar, Zaikun Xu, Adriana M. Airo, Iryna Stryapunina, Cheung Pang Wong, William Branton, Egor Tchesnokov, Matthias Götte, Christopher Power, Tom C. Hobman
  • Virus-Cell Interactions
    Herpes Simplex Virus 1 UL41 Protein Suppresses the IRE1/XBP1 Signal Pathway of the Unfolded Protein Response via Its RNase Activity
    Pengchao Zhang, Chenhe Su, Zhangtao Jiang, Chunfu Zheng
  • Virus-Cell Interactions
    Coxsackievirus B3 Infection Activates the Unfolded Protein Response and Induces Apoptosis through Downregulation of p58IPK and Activation of CHOP and SREBP1
    Huifang M. Zhang, Xin Ye, Yue Su, Ji Yuan, Zhen Liu, David A. Stein, Decheng Yang
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