Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
about
Studies on anticancer activities of antimicrobial peptidesIon channel-forming alamethicin is a potent elicitor of volatile biosynthesis and tendril coiling. Cross talk between jasmonate and salicylate signaling in lima beanConformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces.Analysis and evaluation of channel models: simulations of alamethicin.Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects.Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesiclesMembrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMRMolecular flexibility demonstrated by paramagnetic enhancements of nuclear relaxation. Application to alamethicin: a voltage-gated peptide channel.Single ion channel recordings with CMOS-anchored lipid membranes.Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers, and transbilayer bundles.Peptide aggregation and pore formation in a lipid bilayer: a combined coarse-grained and all atom molecular dynamics study.Biological effects of Trichoderma harzianum peptaibols on mammalian cellsRegulation of callose synthase activity in situ in alamethicin-permeabilized Arabidopsis and tobacco suspension cells.Alamethicin aggregation in lipid membranes.Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situTrichoderma viride cellulase induces resistance to the antibiotic pore-forming peptide alamethicin associated with changes in the plasma membrane lipid composition of tobacco BY-2 cells.Common structural features in gramicidin and other ion channels.Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Fractional polymerization of a suspended planar bilayer creates a fluid, highly stable membrane for ion channel recordings.Signal transduction across alamethicin ion channels in the presence of noiseMeet me on the other side: trans-bilayer modulation of a model voltage-gated ion channel activity by membrane electrostatics asymmetryOrientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay.Partitioning of differently sized poly(ethylene glycol)s into OmpF porinThe implementation of slab geometry for membrane-channel molecular dynamics simulationsEnlargement and contracture of C2-ceramide channels.Conformational changes in alamethicin associated with substitution of its alpha-methylalanines with leucines: a FTIR spectroscopic analysis and correlation with channel kineticsGain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.Substantiation in Enterococcus faecalis of dose-dependent resistance and cross-resistance to pore-forming antimicrobial peptides by use of a polydiacetylene-based colorimetric assay.Length-Dependent Formation of Transmembrane Pores by 310-Helical α-Aminoisobutyric Acid Foldamers.Observing a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change.Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formersThe modulatory effect of calcium ions upon alamethicin monomers uptake on artificial phospholipid membranes.Yeast viral killer toxins: lethality and self-protection.Heart failure drug digitoxin induces calcium uptake into cells by forming transmembrane calcium channelsInclusion of lateral pressure/curvature stress effects in implicit membrane modelsDependence of Alamethicin Membrane Orientation on the Solution Concentration.Synthetic, biologically active amphiphilic peptidesAlamethicin in lipid bilayers: combined use of X-ray scattering and MD simulations.
P2860
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P2860
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@ast
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@en
type
label
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@ast
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@en
prefLabel
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@ast
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@en
P1476
Alamethicin: a peptide model for voltage gating and protein-membrane interactions.
@en
P2093
P304
P356
10.1146/ANNUREV.BB.23.060194.001041
P577
1994-01-01T00:00:00Z