HIV-1 Accessory Protein Vpu Internalizes Cell-surface BST-2/Tetherin through Transmembrane Interactions Leading to Lysosomes
出版年份 2009 全文链接
标题
HIV-1 Accessory Protein Vpu Internalizes Cell-surface BST-2/Tetherin through Transmembrane Interactions Leading to Lysosomes
作者
关键词
-
出版物
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 50, Pages 35060-35072
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2009-10-17
DOI
10.1074/jbc.m109.058305
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- HIV-1 Antagonism of CD317 Is Species Specific and Involves Vpu-Mediated Proteasomal Degradation of the Restriction Factor
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- HM1.24 Is Internalized from Lipid Rafts by Clathrin-mediated Endocytosis through Interaction with α-Adaptin
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- Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion
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- Vpu Antagonizes BST-2–Mediated Restriction of HIV-1 Release via β-TrCP and Endo-Lysosomal Trafficking
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- The Interferon-Induced Protein BST-2 Restricts HIV-1 Release and Is Downregulated from the Cell Surface by the Viral Vpu Protein
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- Inhibition of Lassa and Marburg Virus Production by Tetherin
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- Broad-Spectrum Inhibition of Retroviral and Filoviral Particle Release by Tetherin
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- Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
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- Identification of calcium-modulating cyclophilin ligand as a human host restriction to HIV-1 release overcome by Vpu
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