Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
about
Functional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionStructure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation † , ‡Structural Basis for HIV-1 Neutralization by 2F5-Like Antibodies m66 and m66.6Bioinformatic analysis of HIV-1 entry and pathogenesis.Functional bottlenecks for generation of HIV-1 intersubtype Env recombinants.C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.Recombinant expression, purification, and biophysical characterization of the transmembrane and membrane proximal domains of HIV-1 gp41.4E10-resistant HIV-1 isolated from four subjects with rare membrane-proximal external region polymorphismsAnalysis of primary resistance mutations to HIV-1 entry inhibitors in therapy naive subtype C HIV-1 infected mother-infant pairs from Zambia.HIV-1 gp41 and TCRalpha trans-membrane domains share a motif exploited by the HIV virus to modulate T-cell proliferationCharacterization of the water defect at the HIV-1 gp41 membrane spanning domain in bilayers with and without cholesterol using molecular simulations.In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1Residues in the membrane-spanning domain core modulate conformation and fusogenicity of the HIV-1 envelope glycoprotein.All-atom models of the membrane-spanning domain of HIV-1 gp41 from metadynamics.The membrane-spanning domain of gp41 plays a critical role in intracellular trafficking of the HIV envelope protein.Detailed topology mapping reveals substantial exposure of the "cytoplasmic" C-terminal tail (CTT) sequences in HIV-1 Env proteins at the cell surface.Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.Study of the HIV-2 Env cytoplasmic tail variability and its impact on Tat, Rev and Nef.Mutagenesis of tyrosine and di-leucine motifs in the HIV-1 envelope cytoplasmic domain results in a loss of Env-mediated fusion and infectivity.HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.Co-expression of foreign proteins tethered to HIV-1 envelope glycoprotein on the cell surface by introducing an intervening second membrane-spanning domain.Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelopeTargeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapyBiophysical Characterization of a Vaccine Candidate against HIV-1: The Transmembrane and Membrane Proximal Domains of HIV-1 gp41 as a Maltose Binding Protein FusionThe paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External RegionHIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization.Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.An immunomodulating motif of the HIV-1 fusion protein is chirality-independent: implications for its mode of action.Structural basis for membrane anchoring of HIV-1 envelope spikeTrimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.Truncation of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein defines elements required for fusion, incorporation, and infectivityRole of spike protein endodomains in regulating coronavirus entry.Evaluation of the contribution of the transmembrane region to the ectodomain conformation of the human immunodeficiency virus (HIV-1) envelope glycoprotein.A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.Conserved arginine residue in the membrane-spanning domain of HIV-1 gp41 is required for efficient membrane fusion
P2860
Q27489741-B9CD7273-3127-4B59-BDA7-F65ACC64C85FQ27653846-2307CE30-F553-435A-9A7A-A1B6F6718264Q27680872-27EB401B-2920-41EB-AEB8-A86F81392897Q27693321-2E11E36C-F5F1-47B5-8597-CFC28B177A68Q30374877-7ECB98D1-33EC-4CA2-8FD9-88900F32C4BFQ30422545-3AE7E540-EAA6-4E84-BB59-E7DCCE465199Q30601090-A86EA134-5241-4F1B-9132-20B400C58A83Q33547451-AC016F53-7C6B-4414-8D66-C3BB8C200052Q33597247-7C06611E-F87E-4A4E-B294-9108BF495C5EQ33686978-3F51E1C2-8CC3-4982-8E66-B035F7066B78Q33694260-D11F4F43-A2D6-436B-B2F2-26D589D279AAQ33725718-704A358C-E7B1-4EDB-B88E-EA21EA457925Q33987533-465892C5-E9FC-4342-8634-549D72998788Q34306895-9A966293-5E5B-4B5F-9275-CCE0ED7A475AQ34366384-77093C95-B0BA-41FD-B585-A1B80DD22A08Q34750051-02F09DA3-19EC-4FFE-89ED-73A38D8A0FE7Q34917410-2D389182-7257-45E1-AF49-6CBE8C435660Q35041167-506D2600-10EB-4751-8A22-FB4E36DC7986Q35052938-3FBD6154-9FD0-4A92-B87F-8BAD5BB95B8DQ35113720-3C6614E1-417E-4F2F-9455-A1C050212F7FQ35142768-14BB0939-CD04-42A5-BAAF-E5D0D994A442Q35144796-FAC1520C-F042-473A-8A40-7E323B3BB6CDQ35164416-E6BB192D-BCC6-4DFD-BDE6-9CF9FBDD4901Q35556337-5413C9D1-3301-4105-AF22-E47FD94767D1Q35615810-28F54C3E-307A-461E-9D47-1151C70EB607Q35752124-5A95A5FC-F841-423F-B7AB-AC3540D31F23Q35826179-6F8616D9-D456-42F9-8E8C-314B8873EDECQ35826196-F7A68796-50AF-4F56-B9F4-BBE0B0EC6300Q35860914-7DC14B0D-CE13-4D3B-9C3D-0F4924D434D7Q35909307-662095B2-CD5D-4C93-A0F7-0CBB8138B2E6Q36827883-F4652EF2-62DE-4FAB-86DF-998717403275Q37078294-3D1706FE-3D7B-4643-A73F-5A13CDFBB22FQ37311315-796CBF6A-275B-420B-8993-B15D3792922FQ37376640-BC48E7B0-D0DC-4543-9032-8DE8760730FCQ37388782-5DFE43B6-0D95-4635-A64E-B29590349B10Q37410656-2D4F65AF-BFF0-4234-A93E-0909D8C04495Q37432095-5FDF63C3-5154-4959-A42B-762411044168Q37649155-6D7358B1-52F5-4025-B42B-B676532274E5Q39300864-532B6358-6EAD-46C6-B8D4-0D410A5E40D0Q39525705-AF1906D6-40DB-4750-B582-F135BB7CDD20
P2860
Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Role of the membrane-spanning ...... ell fusion and virus infection
@ast
Role of the membrane-spanning ...... ell fusion and virus infection
@en
type
label
Role of the membrane-spanning ...... ell fusion and virus infection
@ast
Role of the membrane-spanning ...... ell fusion and virus infection
@en
prefLabel
Role of the membrane-spanning ...... ell fusion and virus infection
@ast
Role of the membrane-spanning ...... ell fusion and virus infection
@en
P2093
P2860
P356
P1433
P1476
Role of the membrane-spanning ...... ell fusion and virus infection
@en
P2093
Eric Hunter
Liang Shang
P2860
P304
P356
10.1128/JVI.02666-07
P407
P577
2008-03-19T00:00:00Z