Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.
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HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich lipid domains.Fusion of Enveloped Viruses in Endosomes.Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scalesAllosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivityThe role of cholesterol in membrane fusionThe Roles of Histidines and Charged Residues as Potential Triggers of a Conformational Change in the Fusion Loop of Ebola Virus Glycoprotein.Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational modelsMembrane-dependent conformation, dynamics, and lipid interactions of the fusion peptide of the paramyxovirus PIV5 from solid-state NMRDrug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.The three lives of viral fusion peptidesHIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation.HIV entry and envelope glycoprotein-mediated fusionConditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureHIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Membrane attachment and structure models of lipid storage droplet protein 1Structure 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.Cholesterol and host cell surface proteins contribute to cell-cell fusion induced by the Burkholderia type VI secretion system 5.Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle statepH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.Structure-function dissection of the Pseudorabies virus glycoprotein B fusion loops.Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.
P2860
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P2860
Fusion activity of HIV gp41 fusion domain is related to its secondary structure and depth of membrane insertion in a cholesterol-dependent fashion.
description
2012 nî lūn-bûn
@nan
2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
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
@wuu
name
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@ast
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@en
type
label
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@ast
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@en
prefLabel
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@ast
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@en
P2093
P2860
P1476
Fusion activity of HIV gp41 fu ...... cholesterol-dependent fashion.
@en
P2093
Alex L Lai
Anna Eswara Moorthy
Lukas K Tamm
Yinling Li
P2860
P356
10.1016/J.JMB.2012.02.010
P407
P577
2012-02-17T00:00:00Z