Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational models
about
Membranotropic Cell Penetrating Peptides: The Outstanding JourneyEthical alternatives to experiments with novel potential pandemic pathogens.Membrane Fusion and Infection of the Influenza Hemagglutinin.The three lives of viral fusion peptidesTransferring the PRIMO Coarse-Grained Force Field to the Membrane Environment: Simulations of Membrane Proteins and Helix-Helix Association.Synaptotagmin's role in neurotransmitter release likely involves Ca(2+)-induced conformational transition.Cholesterol-dependent membrane fusion induced by the gp41 membrane-proximal external region-transmembrane domain connection suggests a mechanism for broad HIV-1 neutralization.REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.A Coiled-Coil Peptide Shaping Lipid Bilayers upon Fusion.Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptideCapturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.Influence of membrane composition on the binding and folding of a membrane lytic peptide from the non-enveloped flock house virus.Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The influenza fusion peptide promotes lipid polar head intrusion through hydrogen bonding with phosphates and N-terminal membrane insertion depth.Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: mechanistic implications.Influenza Hemifusion Phenotype Depends on Membrane Context: Differences in Cell-Cell and Virus-Cell Fusion.
P2860
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P2860
Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational models
description
2013 nî lūn-bûn
@nan
2013 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մարտին հրատարակված գիտական հոդված
@hy
2013年の論文
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2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Lipid tail protrusion in simul ...... ants and conformational models
@ast
Lipid tail protrusion in simul ...... ants and conformational models
@en
type
label
Lipid tail protrusion in simul ...... ants and conformational models
@ast
Lipid tail protrusion in simul ...... ants and conformational models
@en
prefLabel
Lipid tail protrusion in simul ...... ants and conformational models
@ast
Lipid tail protrusion in simul ...... ants and conformational models
@en
P2860
P1476
Lipid tail protrusion in simul ...... ants and conformational models
@en
P2093
Per Larsson
P2860
P304
P356
10.1371/JOURNAL.PCBI.1002950
P577
2013-03-07T00:00:00Z