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SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3- TBK1 complex
by
Chen, Xiaojuan
, Zheng, Yang
, Yang, Xingxing
, Xing, Yaling
, Yang, Yudong
, Chen, Zhongbin
in
Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ deubiquitinase
/ Developmental Biology
/ Dimerization
/ HEK293 Cells
/ Human Genetics
/ Humans
/ I-kappa B Kinase - metabolism
/ interferon
/ Interferon Regulatory Factor-3 - metabolism
/ Interferon Type I - antagonists & inhibitors
/ Interferon Type I - metabolism
/ Life Sciences
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Papain - metabolism
/ papain-like protease
/ Peptide Hydrolases - chemistry
/ Peptide Hydrolases - metabolism
/ Phosphorylation
/ Protein Binding
/ Protein Science
/ Protein Structure, Tertiary
/ Protein-Serine-Threonine Kinases - metabolism
/ Research Article
/ SARS coronavirus
/ SARS Virus - enzymology
/ SARS-CoV
/ SARS冠状病毒
/ Signal Transduction
/ Stem Cells
/ STING-TRAF3-TBK1 complex
/ TNF Receptor-Associated Factor 3 - metabolism
/ Ubiquitination
/ 信号转导通路
/ 干扰素
/ 木瓜
/ 类型
/ 蛋白酶
/ 酶抑制
2014
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SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3- TBK1 complex
by
Chen, Xiaojuan
, Zheng, Yang
, Yang, Xingxing
, Xing, Yaling
, Yang, Yudong
, Chen, Zhongbin
in
Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ deubiquitinase
/ Developmental Biology
/ Dimerization
/ HEK293 Cells
/ Human Genetics
/ Humans
/ I-kappa B Kinase - metabolism
/ interferon
/ Interferon Regulatory Factor-3 - metabolism
/ Interferon Type I - antagonists & inhibitors
/ Interferon Type I - metabolism
/ Life Sciences
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Papain - metabolism
/ papain-like protease
/ Peptide Hydrolases - chemistry
/ Peptide Hydrolases - metabolism
/ Phosphorylation
/ Protein Binding
/ Protein Science
/ Protein Structure, Tertiary
/ Protein-Serine-Threonine Kinases - metabolism
/ Research Article
/ SARS coronavirus
/ SARS Virus - enzymology
/ SARS-CoV
/ SARS冠状病毒
/ Signal Transduction
/ Stem Cells
/ STING-TRAF3-TBK1 complex
/ TNF Receptor-Associated Factor 3 - metabolism
/ Ubiquitination
/ 信号转导通路
/ 干扰素
/ 木瓜
/ 类型
/ 蛋白酶
/ 酶抑制
2014
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SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3- TBK1 complex
by
Chen, Xiaojuan
, Zheng, Yang
, Yang, Xingxing
, Xing, Yaling
, Yang, Yudong
, Chen, Zhongbin
in
Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ deubiquitinase
/ Developmental Biology
/ Dimerization
/ HEK293 Cells
/ Human Genetics
/ Humans
/ I-kappa B Kinase - metabolism
/ interferon
/ Interferon Regulatory Factor-3 - metabolism
/ Interferon Type I - antagonists & inhibitors
/ Interferon Type I - metabolism
/ Life Sciences
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Papain - metabolism
/ papain-like protease
/ Peptide Hydrolases - chemistry
/ Peptide Hydrolases - metabolism
/ Phosphorylation
/ Protein Binding
/ Protein Science
/ Protein Structure, Tertiary
/ Protein-Serine-Threonine Kinases - metabolism
/ Research Article
/ SARS coronavirus
/ SARS Virus - enzymology
/ SARS-CoV
/ SARS冠状病毒
/ Signal Transduction
/ Stem Cells
/ STING-TRAF3-TBK1 complex
/ TNF Receptor-Associated Factor 3 - metabolism
/ Ubiquitination
/ 信号转导通路
/ 干扰素
/ 木瓜
/ 类型
/ 蛋白酶
/ 酶抑制
2014
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SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3- TBK1 complex
Journal Article
SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3- TBK1 complex
2014
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Overview
SARS coronavirus (SARS-CoV) develops an antagonis- tic mechanism by which to evade the antiviral activities of interferon (IFN). Previous studies suggested that SARS-CoV papain-like protease (PLpro) inhibits activa- tion of the IRF3 pathway, which would normally elicit a robust IFN response, but the mechanism(s) used by SARS PLpro to inhibit activation of the IRF3 pathway is not fully known. In this study, we uncovered a novel mechanism that may explain how SARS PLpro effi- ciently inhibits activation of the IRF3 pathway. We found that expression of the membrane-anchored PLpro domain (PLpro-TM) from SARS-CoV inhibits STING/ TBKl/IKKE-mediated activation of type I IFNs and dis- rupts the phosphorylation and dimerization of IRF3, which are activated by STING and TBKI. Meanwhile, we showed that PLpro-TM physically interacts with TRAF3, TBK1, IKK~, STING, and IRF3, the key components that assemble the STING-TRAF3-TBK1 complex for activa- tion of IFN expression. However, the interaction between the components in STING-TRAF3-TBK1 complex is dis- rupted by PLpro-TM. Furthermore, SARS PLpro-TM reduces the levels of ubiquitinated forms of RIG-I, STING, TRAF3, TBK1, and IRF3 in the STING-TRAF3- TBK1 complex. These results collectively point to a new mechanism used by SARS-CoV through which PLpro negatively regulates IRF3 activation by interaction withSTING-TRAF3-TBK1 complex, yielding a SARS-CoV countermeasure against host innate immunity.
Publisher
Higher Education Press,Springer Nature B.V
Subject
/ Biomedical and Life Sciences
/ Humans
/ I-kappa B Kinase - metabolism
/ Interferon Regulatory Factor-3 - metabolism
/ Interferon Type I - antagonists & inhibitors
/ Interferon Type I - metabolism
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Peptide Hydrolases - chemistry
/ Peptide Hydrolases - metabolism
/ Protein-Serine-Threonine Kinases - metabolism
/ SARS-CoV
/ SARS冠状病毒
/ TNF Receptor-Associated Factor 3 - metabolism
/ 信号转导通路
/ 干扰素
/ 木瓜
/ 类型
/ 蛋白酶
/ 酶抑制
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