Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein.
about
HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradationMultilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting stepsThe formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to VpuFunctional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family.HIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanismsDifferential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartmentsHIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomesThe human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factorsThe human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradationThe Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channelsVpu Protein: The Viroporin Encoded by HIV-1Cytopathic Mechanisms of HIV-1Structural studies of the HIV-1 accessory protein Vpu in langmuir monolayers: synchrotron X-ray reflectivity.Atomistic detailed mechanism and weak cation-conducting activity of HIV-1 Vpu revealed by free energy calculationsTetherin-driven adaptation of Vpu and Nef function and the evolution of pandemic and nonpandemic HIV-1 strains.Tetherin Antagonism by HIV-1 Group M Nef Proteins.Modulation of HIV-1-host interaction: role of the Vpu accessory proteinTetherin restricts direct cell-to-cell infection of HIV-1.Antiviral efficacy of the novel compound BIT225 against HIV-1 release from human macrophages.Vpu matchmakers as a therapeutic strategy for HIV infection.BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction.Vpu increases susceptibility of human immunodeficiency virus type 1-infected cells to fas killing.Regulation of virus release by the macrophage-tropic human immunodeficiency virus type 1 AD8 isolate is redundant and can be controlled by either Vpu or Env.HIV-1-based defective lentiviral vectors efficiently transduce human monocytes-derived macrophages and suppress replication of wild-type HIV-1Tetherin antagonism by Vpu protects HIV-infected cells from antibody-dependent cell-mediated cytotoxicity.Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production.CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathwayRequirements of the membrane proximal tyrosine and dileucine-based sorting signals for efficient transport of the subtype C Vpu protein to the plasma membrane and in virus release.Polarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity.Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein.Mapping the energy surface of transmembrane helix-helix interactionsComparative structural studies of Vpu peptides in phospholipid monolayers by x-ray scattering.A cytoplasmic tail determinant in HIV-1 Vpu mediates targeting of tetherin for endosomal degradation and counteracts interferon-induced restriction.Cell-cell spread of human immunodeficiency virus type 1 overcomes tetherin/BST-2-mediated restriction in T cells.Epitope tags beside the N-terminal cytoplasmic tail of human BST-2 alter its intracellular trafficking and HIV-1 restrictionDeterminants of tetherin antagonism in the transmembrane domain of the human immunodeficiency virus type 1 Vpu proteinIdentification of amino acids in the human tetherin transmembrane domain responsible for HIV-1 Vpu interaction and susceptibility.Evidence that Vpu modulates HIV-1 Gag-envelope interaction towards envelope incorporation and infectivity in a cell type dependent manner.Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum.Identification of Residues in the BST-2 TM Domain Important for Antagonism by HIV-1 Vpu Using a Gain-of-Function Approach.
P2860
Q21089617-62986091-0911-4CA1-AFCA-F650D8B237D5Q21131559-EF81DA00-28D7-4F75-A570-112ACCC96E2BQ21245050-656284BC-372B-4649-8FF5-FB0B4AF24293Q24523647-BF488614-7DBC-436C-A877-98A4B6813DA8Q24619066-A3EDF297-9BE7-4D09-8350-C3D82C55AC6CQ24646897-57E8149B-622E-465D-9985-247EAD13DB93Q24646984-BA571A51-5D71-4995-9BD0-1A304CE1EC14Q24670601-5F82DEFD-3379-429A-997A-D0E477ABF6FBQ24676509-E3D4797C-8E49-4937-A156-A1057E2768F5Q24680307-58E12EA9-0E97-4651-B194-A0476E53C007Q26801489-A42884F2-1D45-47FB-AC08-4A0F01A54FC0Q27485043-20375269-4F42-4E3B-A60A-5D2799F114F5Q28360964-E4AA18F7-56A9-4770-B981-53A9E958A34EQ28544943-AB7595D2-F125-400F-AD75-13812A2E383DQ30382590-49F3FB4F-D99D-4C18-A2A5-555BFCD3D729Q30393226-45161D2C-220A-4EAD-8C1B-BEB731CB463BQ30397761-F6705C49-840F-4BAE-BE4A-09920712E2D4Q30497822-320BE371-3BB6-4F8D-8297-F9A032F99B68Q30968332-3DE15848-8657-441D-A01A-9C9993C05960Q33455532-EB3C9065-1D5C-4965-9AB3-8628D99B7882Q33519521-46CC3FD4-6B26-42EA-9695-5F25B54D57A2Q33638829-53B236CC-CB59-46BF-829E-EC493B76CFA8Q33640055-65E99BB7-5117-417E-A611-5A44F929C9F0Q33671675-70B265AF-9C59-4938-9195-FF86E9B319F8Q33674461-EB9E9436-13BC-4BBB-8F10-2C1554956320Q33737672-590F1EB2-859B-4CB8-9DB5-8EE53289912EQ33782459-7FF666CC-FFC3-4369-B180-55C2EFB058C3Q33926185-249814E2-7215-4ABF-9B16-B89A5E7EDD72Q33933111-4523BF41-F408-4C80-B2D6-D1CD3B3DB974Q34062105-B8C3689D-1800-4512-91DD-BA872031C6DAQ34176789-78EE7044-AF03-4546-B424-D2A8355921B5Q34180848-93470F8D-6D6A-4256-9336-E0F6DE93F59DQ34220959-EEB7E16F-ECAF-4A48-85F7-8F542CDE1CD7Q34291056-F638DBBF-8832-4A56-ABA0-6DF8362F4163Q34408687-39880D47-9924-4B53-AC34-730AEEBA3750Q34416492-C36FE03B-6A6F-4256-BDB2-A8BC0BD81FA8Q34485169-0B24C841-3C80-4BB8-B9BD-C879453246EEQ34684340-06EE616E-AE16-4FD9-B933-1D62339225EFQ34701164-E91BF3A2-9B1B-4B62-9D28-F8FA37528D1BQ35028829-7665A801-AECB-49F3-8EF2-C6313107B3E8
P2860
Human immunodeficiency virus type 1 Vpu protein is an oligomeric type I integral membrane protein.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Human immunodeficiency virus t ...... e I integral membrane protein.
@ast
Human immunodeficiency virus t ...... e I integral membrane protein.
@en
type
label
Human immunodeficiency virus t ...... e I integral membrane protein.
@ast
Human immunodeficiency virus t ...... e I integral membrane protein.
@en
prefLabel
Human immunodeficiency virus t ...... e I integral membrane protein.
@ast
Human immunodeficiency virus t ...... e I integral membrane protein.
@en
P2093
P2860
P1433
P1476
Human immunodeficiency virus t ...... e I integral membrane protein.
@en
P2093
P2860
P304
P407
P577
1993-08-01T00:00:00Z