HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin. - Wikidata - wikimedia - TriplyDB

HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin.

HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin.

http://www.wikidata.org/entity/Q37257389

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The great escape: viral strategies to counter BST-2/tetherin MYADM 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 activity Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1 Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain HIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanisms Differential effects of human immunodeficiency virus type 1 Vpu on the stability of BST-2/tetherin Antiviral inhibition of enveloped virus release by tetherin/BST-2: action and counteraction HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes The role of BST-2/Tetherin in host protection and disease manifestation Targeted therapy for HM1.24 (CD317) on multiple myeloma cells Quantitative 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 degradation Counteraction of the multifunctional restriction factor tetherin Positioning 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 protein Tetherin 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 membrane Tetherin 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-2 HIV-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 cells Serine-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 restriction Identification of alternatively translated Tetherin isoforms with differing antiviral and signaling activities Identification 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 infection 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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P2860

HM1.24 is internalized from lipid rafts by clathrin-mediated endocytosis through interaction with alpha-adaptin.

http://www.wikidata.org/entity/Q37257389

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 08 April 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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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

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JBC.M109.005124

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Journal of Biological Chemistry

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HM1.24 is internalized from li ...... nteraction with alpha-adaptin.

@en

P2093

Azusa Takigawa

http://www.w3.org/2001/XMLSchema#string

Hideaki Fujita

http://www.w3.org/2001/XMLSchema#string

Jun Amano

http://www.w3.org/2001/XMLSchema#string

Naoko Masuyama

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Rika Tanaka

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Tomonori Muto

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Toshio Kuronita

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Yoshinori Aso

http://www.w3.org/2001/XMLSchema#string

Yoshitaka Tanaka

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Yuko Hirota

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P2860

Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly

Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis

Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference

Molecular cloning and chromosomal mapping of a bone marrow stromal cell surface gene, BST2, that may be involved in pre-B-cell growth

Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit

Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis

VIP21/caveolin is a cholesterol-binding protein

Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles

Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process

AP-2/Eps15 interaction is required for receptor-mediated endocytosis

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15927-15941

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scholarly article

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10.1074/JBC.M109.005124

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P407

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23

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284

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2009-04-08T00:00:00Z

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19359243

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2708888

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