Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin.
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Binding Dynamics of Hepatitis C Virus' NS5A Amphipathic Peptide to Cell and Model MembranesStructural basis of membrane-induced cardiotoxin A3 oligomerizationBarrel-stave model or toroidal model? A case study on melittin pores.Structure, location, and lipid perturbations of melittin at the membrane interfaceInsertion and pore formation driven by adsorption of proteins onto lipid bilayer membrane-water interfaces.Interactions of mouse Paneth cell alpha-defensins and alpha-defensin precursors with membranes. Prosegment inhibition of peptide association with biomimetic membranesCapsid protein VP4 of human rhinovirus induces membrane permeability by the formation of a size-selective multimeric poreProcess of inducing pores in membranes by melittinKinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopyThe lipid dependence of melittin action investigated by dual-color fluorescence burst analysis.Recombinant antimicrobial peptide hPAB-β expressed in Pichia pastoris, a potential agent active against methicillin-resistant Staphylococcus aureus.Non-viral peptide-based approaches to gene delivery.Antimicrobial peptides in toroidal and cylindrical pores.Antimicrobial peptides bind more strongly to membrane poresReconstitution of holin activity with a synthetic peptide containing the 1-32 sequence region of EJh, the EJ-1 phage holin.Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis.Effect of phospholipid composition on an amphipathic peptide-mediated pore formation in bilayer vesiclesStructure of (KIAGKIA)3 aggregates in phospholipid bilayers by solid-state NMR.Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores.High-risk human papillomavirus E5 oncoprotein displays channel-forming activity sensitive to small-molecule inhibitors.Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aureinpH-dependent disruption of Escherichia coli ATCC 25922 and model membranes by the human antimicrobial peptides hepcidin 20 and 25.Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin.A chimeric peptide composed of a dermaseptin derivative and an RNA III-inhibiting peptide prevents graft-associated infections by antibiotic-resistant staphylococciThe structure of a melittin-stabilized poreThe molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulumCorrelating antimicrobial activity and model membrane leakage induced by nylon-3 polymers and detergentsDetermination of pore sizes and relative porosity in porous nanoshell architectures using dextran retention with single monomer resolution and proton permeationStructure of the alamethicin pore reconstructed by x-ray diffraction analysis.The roles of antimicrobial peptides in innate host defense.Kinetic Defects Induced by Melittin in Model Lipid Membranes: A Solution Atomic Force Microscopy Study.Antimicrobial peptides: successes, challenges and unanswered questions.Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides.Bee venom in cancer therapy.Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins.Computational studies of peptide-induced membrane pore formation.Highly efficient macromolecule-sized poration of lipid bilayers by a synthetically evolved peptideSelective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain.The electrical response of bilayers to the bee venom toxin melittin: evidence for transient bilayer permeabilization.Role of Vif in stability of the human immunodeficiency virus type 1 core
P2860
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P2860
Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: pore formation by melittin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@ast
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@en
type
label
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@ast
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@en
prefLabel
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@ast
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@en
P2093
P2860
P1433
P1476
Sizing membrane pores in lipid ...... s: pore formation by melittin.
@en
P2093
A S Ladokhin
M E Selsted
P2860
P304
P356
10.1016/S0006-3495(97)78822-2
P407
P577
1997-04-01T00:00:00Z