Atomic-resolution simulations predict a transition state for vesicle fusion defined by contact of a few lipid tails.
about
Structure and Mechanism of the Saposin-like Domain of a Plant Aspartic ProteaseEmergent ultra-long-range interactions between active particles in hybrid active-inactive systemsGROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit.Coupled diffusion in lipid bilayers upon close approach.Membrane Fusion and Infection of the Influenza Hemagglutinin.Characterization of a potent antimicrobial lipopeptide via coarse-grained molecular dynamics.Molecular-level simulation of pandemic influenza glycoproteins.Dynamic heterogeneity controls diffusion and viscosity near biological interfaces.Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational modelsSimulation of fusion-mediated nanoemulsion interactions with model lipid bilayers.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionVisualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Dynamic protein conformations preferentially drive energy transfer along the active chain of the photosystem II reaction centre.Caught in the act: visualization of SNARE-mediated fusion events in molecular detail.Line-tension controlled mechanism for influenza fusion.Activation thermodynamics of poly(ethylene glycol)-mediated model membrane fusion support mechanistic models of stalk and pore formation.A Coiled-Coil Peptide Shaping Lipid Bilayers upon Fusion.Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.A comparison of coarse-grained and continuum models for membrane bending in lipid bilayer fusion pores.Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptideIndividual vesicle fusion events mediated by lipid-anchored DNA.Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.Continuum descriptions of membranes and their interaction with proteins: Towards chemically accurate models.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Phosphatidylserine inhibits and calcium promotes model membrane fusion.Sequence-dependent backbone dynamics of a viral fusogen transmembrane helix.Phosphatidylserine-Dependent Catalysis of Stalk and Pore Formation by Synaptobrevin JMR-TMD Peptide.Adhesion energy can regulate vesicle fusion and stabilize partially fused states.pH Alters PEG-mediated fusion of phosphatidylethanolamine-containing vesiclesThe transmembrane domain peptide of vesicular stomatitis virus promotes both intermediate and pore formation during PEG-mediated vesicle fusion.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.v-SNARE transmembrane domains function as catalysts for vesicle fusionPulling force and surface tension drive membrane fusion.v-SNARE function in chromaffin cells.Pathway for insertion of amphiphilic nanoparticles into defect-free lipid bilayers from atomistic molecular dynamics simulations.Permeability and ammonia selectivity in aquaporin TIP2;1: linking structure to function.
P2860
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P2860
Atomic-resolution simulations predict a transition state for vesicle fusion defined by contact of a few lipid tails.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Atomic-resolution simulations ...... contact of a few lipid tails.
@ast
Atomic-resolution simulations ...... contact of a few lipid tails.
@en
type
label
Atomic-resolution simulations ...... contact of a few lipid tails.
@ast
Atomic-resolution simulations ...... contact of a few lipid tails.
@en
prefLabel
Atomic-resolution simulations ...... contact of a few lipid tails.
@ast
Atomic-resolution simulations ...... contact of a few lipid tails.
@en
P2860
P1476
Atomic-resolution simulations ...... contact of a few lipid tails.
@en
P2093
Vijay S Pande
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000829
P577
2010-06-24T00:00:00Z