Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein
about
Non-metabolic membrane tubulation and permeability induced by bioactive peptidesControls and constrains of the membrane disrupting action of Aurein 1.2.Posing for a picture: vesicle immobilization in agarose gel.Structural features of peptoid-peptide hybrids in lipid-water interfacesβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHSpecific and selective peptide-membrane interactions revealed using quartz crystal microbalance.Phosphatidylethanolamine binding is a conserved feature of cyclotide-membrane interactions.NH125 kills methicillin-resistant Staphylococcus aureus persisters by lipid bilayer disruption.Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Absence of fluid-ordered/fluid-disordered phase coexistence in ceramide/POPC mixtures containing cholesterolThe lipid dependence of melittin action investigated by dual-color fluorescence burst analysis.How to address CPP and AMP translocation? Methods to detect and quantify peptide internalization in vitro and in vivo (Review).Direct visualization of lipid domains in human skin stratum corneum's lipid membranes: effect of pH and temperature.Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruptionImportance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2.Effect of proline position on the antimicrobial mechanism of buforin II.The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action.Giant unilamellar vesicles electroformed from native membranes and organic lipid mixtures under physiological conditionsInfectious Disease: Connecting Innate Immunity to Biocidal Polymers.Proline facilitates membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disorderingSynthetic, biologically active amphiphilic peptidesAmyloid beta oligomers induce neuronal elasticity changes in age-dependent manner: a force spectroscopy study on living hippocampal neurons.Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogsSpontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide.Recent developments in fluorescence correlation spectroscopy for diffusion measurements in planar lipid membranes.Toward understanding protocell mechanosensation.New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysisStructure and functional dynamics characterization of the ion channel of the human respiratory syncytial virus (hRSV) small hydrophobic protein (SH) transmembrane domain by combining molecular dynamics with excited normal modes.Selective and vertical microfabrication of lipid tubule arrays on glass substrates using template-guided gentle hydration.Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.Membrane changes under oxidative stress: the impact of oxidized lipids.Bacterial Spheroplasts as a Model for Visualizing Membrane Translocation of Antimicrobial Peptides.Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistenceQCM-D fingerprinting of membrane-active peptides.Mode of Action of a Designed Antimicrobial Peptide: High Potency against Cryptococcus neoformans.Antimicrobial Peptides from the Aurein Family Form Ion-Selective Pores in Bacillus subtilis.All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization.Coarse-grained simulations of the membrane-active antimicrobial Peptide maculatin 1.1.Pores formed by Baxα5 relax to a smaller size and keep at equilibriumRetro analog concept: comparative study on physico-chemical and biological properties of selected antimicrobial peptides.
P2860
Q27303093-1F7AE982-D1BA-48DF-8A76-989DC1D92D79Q27306846-6B2E2BAF-5FD0-43A5-9921-E6FBA46AFFD0Q27318036-E2D01CEB-FE50-4F68-AA2E-294D9C717F12Q27694626-DB6613F6-6421-431B-9513-592B327C1D25Q28541669-87E098F0-BB95-4C99-AB5E-0A98FB736C32Q30480700-A27419D3-782B-4550-95C6-9C9C9E0F4D8BQ30525336-D4B3C844-97EA-40BB-A9E7-02FECB7D8F5FQ30795809-CDAF8D1F-0C87-4487-95CA-F2B7D3DE1E12Q30843749-2F94C385-E28B-427C-B959-464D15457325Q33237656-FCE991BA-882F-4A09-9C99-BFE478A4EFB7Q33282119-E887CFB6-C637-4BCD-A2E5-5F15A961324DQ33285497-13719BBE-E2D1-490C-A8E9-798BC8CB4CE4Q33290862-4CE5F1BB-8997-4ED6-B924-114D80BB7445Q33531584-4C3C3999-200E-4361-9A66-62A8B4537E91Q34250487-5A4C8EAE-9180-40A1-8570-79BD6C5B66A2Q34699473-ED08E846-51C0-4267-8490-34A231332B01Q34757081-A667A129-0B49-4451-AA81-6CFA6D5D29AFQ36129099-86C46C05-1FE6-46C5-83DE-77B0A53C003DQ36298207-D4EAFF07-CF04-494C-BF19-6F2FFFBBD540Q36742771-876A73D8-6E06-46E4-A8B4-9BC4A0C186D7Q36859083-40872604-C868-40BD-B58D-5DDACD84BA7EQ36898056-84F8AF7A-F357-4DB8-85C1-221D3D4FFE28Q37277016-7D7C3481-4634-42DE-B792-541DE44ADE1EQ37434421-2FF28F79-36CC-459F-96DD-01E2D7DF221EQ37729842-EB36B58E-DD5D-4E95-BCBA-C54984888FCDQ37809771-D2B8CAAA-8FE3-4DC3-BB74-6CD634154601Q38661134-74569707-6B1E-42DA-98D1-AC1613B57B12Q38798163-F0BBA39F-724D-4C5E-9886-27FD78E4C787Q38798585-9312F3B5-0AD4-44A0-8DB0-A2843B2F89BAQ39183260-A9089AE5-6FF6-44BD-91F3-4A823C3E82CFQ39310069-43EF2181-5DB4-46FC-A5E5-46AC1EAA8C29Q39588074-6AFE5E62-F492-4CFD-B295-5481E108135CQ39595002-7FDE5569-1CD7-4084-8D9B-8A6B8D5B4BBDQ39805047-2E8336B2-D2F9-499D-8934-B53B08B61A28Q40497992-DD13BB53-47BD-407E-A640-21829754CAD9Q41142894-9F9E460A-DA0F-43EB-BB13-93CCE2970777Q41152752-4A6B9D0F-2C3B-4A0E-A136-37AC53AADEA7Q41999493-5541BBEE-B8BD-4F85-9AD4-21100A603353Q42183300-11B0F251-9024-4288-80D9-C0E8F106DDDEQ42359917-7CD60F02-30EA-493A-99D4-F47BDB648A8C
P2860
Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein
description
2005 nî lūn-bûn
@nan
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Direct visualization of membra ...... aculatin, citropin, and aurein
@ast
Direct visualization of membra ...... aculatin, citropin, and aurein
@en
Direct visualization of membra ...... aculatin, citropin, and aurein
@nl
type
label
Direct visualization of membra ...... aculatin, citropin, and aurein
@ast
Direct visualization of membra ...... aculatin, citropin, and aurein
@en
Direct visualization of membra ...... aculatin, citropin, and aurein
@nl
prefLabel
Direct visualization of membra ...... aculatin, citropin, and aurein
@ast
Direct visualization of membra ...... aculatin, citropin, and aurein
@en
Direct visualization of membra ...... aculatin, citropin, and aurein
@nl
P2093
P2860
P1433
P1476
Direct visualization of membra ...... aculatin, citropin, and aurein
@en
P2093
Ernesto E Ambroggio
Gerardo D Fidelio
John H Bowie
Luis A Bagatolli
P2860
P304
P356
10.1529/BIOPHYSJ.105.066589
P407
P577
2005-07-01T00:00:00Z