HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.
about
Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusionFusion of Enveloped Viruses in Endosomes.The three lives of viral fusion peptidesSinglet oxygen effects on lipid membranes: implications for the mechanism of action of broad-spectrum viral fusion inhibitors.Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionEfficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid bindingBiophysical Characterization of a Vaccine Candidate against HIV-1: The Transmembrane and Membrane Proximal Domains of HIV-1 gp41 as a Maltose Binding Protein FusionThe Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External RegionStructural and Functional Studies on the Marburg Virus GP2 Fusion LoopThe Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureIdentification of the Fusion Peptide-Containing Region in Betacoronavirus Spike GlycoproteinsConformational properties of peptides corresponding to the ebolavirus GP2 membrane-proximal external region in the presence of micelle-forming surfactants and lipids.Trimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Mutational scanning reveals the determinants of protein insertion and association energetics in the plasma membrane.Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.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.Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.Structural Study of a New HIV-1 Entry Inhibitor and Interaction with the HIV-1 Fusion Peptide in Dodecylphosphocholine Micelles.Sequence-dependent backbone dynamics of a viral fusogen transmembrane helix.Stability and Water Accessibility of the Trimeric Membrane Anchors of the HIV-1 Envelope Spikes.
P2860
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P2860
HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.
description
2012 nî lūn-bûn
@nan
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
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2012年论文
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2012年论文
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name
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@ast
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@en
type
label
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@ast
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@en
prefLabel
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@ast
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@en
P2093
P2860
P356
P1433
P1476
HIV-1 gp41 transmembrane domai ...... hibition of virus-cell fusion.
@en
P2093
Eliran Moshe Reuven
Mathias Viard
Nurit Manukovsky
Robert Blumenthal
Yakir Dadon
Yechiel Shai
P2860
P304
P356
10.1021/BI201721R
P407
P577
2012-03-23T00:00:00Z