BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action
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HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactionsAntiviral inhibition of enveloped virus release by tetherin/BST-2: action and counteractionMechanism of HIV-1 virion entrapment by tetherinHSV-2 glycoprotein gD targets the CC domain of tetherin and promotes tetherin degradation via lysosomal pathwayIntrinsic cellular defenses against human immunodeficiency virusesCounteraction of the multifunctional restriction factor tetherinAnalysis of the human immunodeficiency virus type 1 M group Vpu domains involved in antagonizing tetherin.Lack of adaptation to human tetherin in HIV-1 group O and P.Impact of histidine residues on the transmembrane helices of viroporins.Tetherin antagonism by Vpu protects HIV-infected cells from antibody-dependent cell-mediated cytotoxicity.Mechanisms of Virologic Control and Clinical Characteristics of HIV+ Elite/Viremic ControllersPolarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity.Vpu downmodulates two distinct targets, tetherin and gibbon ape leukemia virus envelope, through shared features in the Vpu cytoplasmic tail.Vpu binds directly to tetherin and displaces it from nascent virions.Misdirection of membrane trafficking by HIV-1 Vpu and Nef: Keys to viral virulence and persistence.Bacteria-based analysis of HIV-1 Vpu channel activity.Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogensSome human immunodeficiency virus type 1 Vpu proteins are able to antagonize macaque BST-2 in vitro and in vivo: Vpu-negative simian-human immunodeficiency viruses are attenuated in vivo.Separable determinants of subcellular localization and interaction account for the inability of group O HIV-1 Vpu to counteract tetherinDifferential regulation of NF-κB-mediated proviral and antiviral host gene expression by primate lentiviral Nef and Vpu proteins.Structural Basis for the Antiviral Activity of BST-2/Tetherin and Its Viral AntagonismTransmembrane domain determinants of CD4 Downregulation by HIV-1 Vpu.Antiretroviral restriction factors.Role of retroviral restriction factors in the interferon-α-mediated suppression of HIV-1 in vivo.Ubiquitination of BST-2 protein by HIV-1 Vpu protein does not require lysine, serine, or threonine residues within the BST-2 cytoplasmic domain.A small molecule compound IMB-LA inhibits HIV-1 infection by preventing viral Vpu from antagonizing the host restriction factor BST-2.HIV-1 Adapts To Replicate in Cells Expressing Common Marmoset APOBEC3G and BST2Host restriction factors in retroviral infection: promises in virus-host interaction.HIV-1 Vpu - an ion channel in search of a job.HIV-1 Vpu antagonizes BST-2 by interfering mainly with the trafficking of newly synthesized BST-2 to the cell surface.Identification of novel key amino acids at the interface of the transmembrane domains of human BST-2 and HIV-1 VpuHIV-1 Vpu affects the anterograde transport and the glycosylation pattern of NTB-A.HIV-1 Vpu mediated downregulation of CD155 requires alanine residues 10, 14 and 18 of the transmembrane domain
P2860
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P2860
BST-2 is rapidly down-regulated from the cell surface by the HIV-1 protein Vpu: evidence for a post-ER mechanism of Vpu-action
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2011 nî lūn-bûn
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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年論文
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2011年論文
@zh-hant
2011年論文
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2011年論文
@zh-mo
2011年論文
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2011年论文
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name
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@ast
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@en
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@nl
type
label
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@ast
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@en
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@nl
prefLabel
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@ast
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@en
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@nl
P2093
P2860
P1433
P1476
BST-2 is rapidly down-regulate ...... ost-ER mechanism of Vpu-action
@en
P2093
Andrey Tokarev
Cheng-Chang Chen
John Guatelli
Mark Skasko
P2860
P356
10.1016/J.VIROL.2010.12.038
P407
P577
2011-01-14T00:00:00Z