CD317/tetherin is enriched in the HIV-1 envelope and downregulated from the plasma membrane upon virus infection.
about
The great escape: viral strategies to counter BST-2/tetherinStructural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomainHIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanismsDifferential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/tetherinBST-2/tetherin: a new component of the innate immune response to enveloped virusesAntiviral inhibition of enveloped virus release by tetherin/BST-2: action and counteractionThe role of BST-2/Tetherin in host protection and disease manifestationMapping the distributions and quantifying the labelling intensities of cell compartments by immunoelectron microscopy: progress towards a coherent set of methodsThree-Dimensional Structural Characterization of HIV-1 Tethered to Human Cells.Structural insight into the mechanisms of enveloped virus tethering by tetherinStructural and Biophysical Analysis of BST-2/Tetherin Ectodomains Reveals an Evolutionary Conserved Design to Inhibit Virus ReleaseQuantitative multicolor super-resolution microscopy reveals tetherin HIV-1 interaction.Bone marrow stromal cell antigen 2 (BST-2) restricts mouse mammary tumor virus (MMTV) replication in vivoCounteraction of the multifunctional restriction factor tetherinThe HIV-1 Vpu viroporin inhibitor BIT225 does not affect Vpu-mediated tetherin antagonismModulation of HIV-1-host interaction: role of the Vpu accessory proteinUltra structural characterisation of tetherin - a protein capable of preventing viral release from the plasma membraneCharacterization of E3 ligases involved in lysosomal sorting of the HIV-1 restriction factor BST2.The ESCRT-0 component HRS is required for HIV-1 Vpu-mediated BST-2/tetherin down-regulation.Multiple-labelling immunoEM using different sizes of colloidal gold: alternative approaches to test for differential distribution and colocalization in subcellular structures.HIV-1 Vpu antagonism of tetherin inhibits antibody-dependent cellular cytotoxic responses by natural killer cells.A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction.Determinants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu proteinThe interferon-inducible host factor bone marrow stromal antigen 2/tetherin restricts virion release, but is it actually a viral restriction factor?Tetherin/BST-2 antagonism by Nef depends on a direct physical interaction between Nef and tetherin, and on clathrin-mediated endocytosis.Identification of Residues in the BST-2 TM Domain Important for Antagonism by HIV-1 Vpu Using a Gain-of-Function Approach.Viral miniproteinsIn vivo expression profile of the antiviral restriction factor and tumor-targeting antigen CD317/BST-2/HM1.24/tetherin in humans.In COS cells Vpu can both stabilize tetherin expression and counteract its antiviral activity.Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane.Role of the endocytic pathway in the counteraction of BST-2 by human lentiviral pathogensAntibody-mediated enhancement of HIV-1 and HIV-2 production from BST-2/tetherin-positive cells.C-terminal hydrophobic region in human bone marrow stromal cell antigen 2 (BST-2)/tetherin protein functions as second transmembrane motif.Structural Basis for the Antiviral Activity of BST-2/Tetherin and Its Viral AntagonismInfluenza virus partially counteracts restriction imposed by tetherin/BST-2.The size and conservation of a coiled-coil structure in the ectodomain of human BST-2/tetherin is dispensable for inhibition of HIV-1 virion release.Filamin A Is Involved in HIV-1 Vpu-mediated Evasion of Host Restriction by Modulating Tetherin Expression.ATP1B3 Protein Modulates the Restriction of HIV-1 Production and Nuclear Factor κ Light Chain Enhancer of Activated B Cells (NF-κB) Activation by BST-2.Roles played by capsid-dependent induction of membrane curvature and Gag-ESCRT interactions in tetherin recruitment to HIV-1 assembly sites.Host Factors and HIV-1 Replication: Clinical Evidence and Potential Therapeutic Approaches
P2860
Q21090506-9FEDCD29-900C-46C7-9A3F-0F4358A5A382Q24306855-CC3A974C-A2CB-4981-B203-FCE2935610AFQ24619066-889A3149-3D68-45EA-A985-E0B3679144BEQ24629504-9618A958-9A99-4980-9C7E-267836BF9179Q24630382-E95DA740-6F42-41C6-BB67-19BBD2F57056Q24635271-0ED1092C-62FF-47BD-BCFB-77F5C34041ACQ26752737-A99EB24A-C8F9-41CA-AF8B-B97733A8E191Q27009362-19ABC7AB-C584-40F1-B232-A9912F5BE900Q27321247-8B2621AA-1AD9-4246-BF44-6145174DB869Q27664987-7C759C20-46D8-45BE-B4BC-3E8B5F0C3DACQ27665937-94299169-F1C6-4ABD-8161-E67084963453Q28478446-2EF3B490-AE90-4C24-9EF6-0E776BE0E14CQ28510187-E09015D9-42FD-4F9F-BCAC-B9855F93ECF8Q28659945-1828799D-1D13-4517-BB67-C5233C2E307BQ28742774-3E79F3C3-2E41-443D-B8C9-97D4871E555BQ30397761-21664481-70CB-4C56-BE4B-1213383FCEDEQ31034125-52C2E6AC-503F-455A-9E67-F23539E05ACEQ33743176-1A25694F-F81B-4816-A5D2-7F78EF0917FEQ33815533-863808EA-1600-4EC8-8684-4B3DB7BE1FF5Q33822569-68E428C9-E5D7-47C5-B5FE-997D78246CE2Q33887674-DC86D4CC-975E-4B5E-8895-BAA16FEE36D3Q34220959-24709E89-E025-4FED-B126-2CB19218000FQ34416492-466560BC-2A12-4891-AF42-6476B4815EFBQ34492477-783E2CD3-084B-4122-9E2D-C6665F6E83CEQ34819697-EAF1BFB5-F65B-412B-8C7B-BDBFB3D62363Q35028829-56D5B308-E29A-4547-8786-30AA46D63FB8Q35151120-3EDF5BA6-93EC-4ABE-8F2F-2997D948DE33Q35170879-C9650A7D-C43F-4E40-8806-BED8EE74FAAAQ35382088-33A8FB1C-2BE6-403C-96D3-B60011918EBBQ35382894-ECC28934-7E80-43E2-9A7B-2F11A5158C63Q35383008-E6ADE5DB-3AC6-41D6-A0D8-3262BE87BFFAQ35531194-AC3421AA-727B-4352-94E0-7B7C95E05D83Q35562726-9FECD4C0-625E-4165-AB87-8E11593DE616Q35607295-F16E75A1-D026-4A5A-B2FC-6C66E388A45FQ36052469-A4793BA5-2E6C-4F4C-B9A0-3BEC0CDC9970Q36492793-099198ED-DCC8-45E1-9263-9D908AF90B5DQ36594734-F87C9A1E-939C-452E-8012-D25E69B2A3FEQ36744586-A99643D1-BF62-4C77-B49C-7510A4EA6132Q36760105-01D5A770-F292-4279-960E-0A9546EB0654Q37252004-C67FFD4D-9ACB-4521-9948-05B4B7C53043
P2860
CD317/tetherin is enriched in the HIV-1 envelope and downregulated from the plasma membrane upon virus infection.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
CD317/tetherin is enriched in ...... membrane upon virus infection.
@ast
CD317/tetherin is enriched in ...... membrane upon virus infection.
@en
type
label
CD317/tetherin is enriched in ...... membrane upon virus infection.
@ast
CD317/tetherin is enriched in ...... membrane upon virus infection.
@en
prefLabel
CD317/tetherin is enriched in ...... membrane upon virus infection.
@ast
CD317/tetherin is enriched in ...... membrane upon virus infection.
@en
P2093
P2860
P50
P356
P1433
P1476
CD317/tetherin is enriched in ...... membrane upon virus infection.
@en
P2093
Amy Andrew
Heike Oberwinkler
Klaus Strebel
Manon Eckhardt
Stefanie Homann
P2860
P304
P356
10.1128/JVI.02421-09
P577
2010-02-10T00:00:00Z