HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin.
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The great escape: viral strategies to counter BST-2/tetherinMYADM regulates Rac1 targeting to ordered membranes required for cell spreading and migration.BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activityStructural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1Structural 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/tetherinAntiviral inhibition of enveloped virus release by tetherin/BST-2: action and counteractionHIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomesThe role of BST-2/Tetherin in host protection and disease manifestationTargeted therapy for HM1.24 (CD317) on multiple myeloma cellsQuantitative multicolor super-resolution microscopy reveals tetherin HIV-1 interaction.Expression of HIV-1 Vpu leads to loss of the viral restriction factor CD317/Tetherin from lipid rafts and its enhanced lysosomal degradationCounteraction of the multifunctional restriction factor tetherinPositioning of cysteine residues within the N-terminal portion of the BST-2/tetherin ectodomain is important for functional dimerization of BST-2.Tetherin/BST-2: Restriction Factor or Immunomodulator?Efficient Vpu-Mediated Tetherin Antagonism by an HIV-1 Group O Strain.Modulation of HIV-1-host interaction: role of the Vpu accessory proteinTetherin restricts direct cell-to-cell infection of HIV-1.A cholesterol recognition amino acid consensus domain in GP64 fusion protein facilitates anchoring of baculovirus to mammalian cells.Ultra structural characterisation of tetherin - a protein capable of preventing viral release from the plasma membraneTetherin can restrict cell-free and cell-cell transmission of HIV from primary macrophages to T cells.Characterization of E3 ligases involved in lysosomal sorting of the HIV-1 restriction factor BST2.Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.The ESCRT-0 component HRS is required for HIV-1 Vpu-mediated BST-2/tetherin down-regulation.CD317/tetherin is enriched in the HIV-1 envelope and downregulated from the plasma membrane upon virus infection.The novel immunotoxin HM1.24-ETA' induces apoptosis in multiple myeloma cells.Cloning and characterization of the antiviral activity of feline Tetherin/BST-2HIV-1 Vpu antagonism of tetherin inhibits antibody-dependent cellular cytotoxic responses by natural killer cells.SIV Nef proteins recruit the AP-2 complex to antagonize Tetherin and facilitate virion release.Signaling and ligand interaction of ILT7: receptor-mediated regulatory mechanisms for plasmacytoid dendritic cellsSerine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu.A single nucleotide polymorphism in tetherin promotes retrovirus restriction in vivo.A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction.Epitope tags beside the N-terminal cytoplasmic tail of human BST-2 alter its intracellular trafficking and HIV-1 restrictionIdentification of alternatively translated Tetherin isoforms with differing antiviral and signaling activitiesIdentification of amino acids in the human tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility.The interferon-inducible host factor bone marrow stromal antigen 2/tetherin restricts virion release, but is it actually a viral restriction factor?The role of BST2/tetherin in feline retrovirus infectionBST-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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HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 08 April 2009
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
@cs
name
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@en
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@nl
type
label
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@en
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@nl
prefLabel
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@en
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@nl
P2093
P2860
P356
P1476
HM1.24 is internalized from li ...... nteraction with alpha-adaptin.
@en
P2093
Azusa Takigawa
Hideaki Fujita
Naoko Masuyama
Rika Tanaka
Tomonori Muto
Toshio Kuronita
Yoshinori Aso
Yoshitaka Tanaka
Yuko Hirota
P2860
P304
15927-15941
P356
10.1074/JBC.M109.005124
P407
P577
2009-04-08T00:00:00Z