About: A molecular model of membrane excitability

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scientific article published on 01 January 1974

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1974 (uk) articolo scientifico (pubblicato il 1974) (it) article scientifique publié en 1974 (fr) գիտական հոդված հրատարակված 1974 թվականի հունվարի 1-ին (hy) artículu científicu espublizáu en xineru de 1974 (ast) im Jahr 1974 veröffentlichter wissenschaftlicher Artikel (de) artikull shkencor i botuar më 01 janar 1974 (sq) scientific article published on 01 January 1974 (en)
publication date	wds:Q68900312-57514096-DFF3-42F8-B359-3722CDD56C51
publication date	1974-01-01 00:00:00Z (xsd:dateTime)
author name string	wds:Q68900312-21B71BF8-6930-4DE4-BA0F-061DEEC9D2EF wds:Q68900312-A75E7142-2C71-432F-A495-B084092F52A2
author name string	Baumann G Mueller P
rdfs:label	A molecular model of membrane excitability (en) A molecular model of membrane excitability (nl) A molecular model of membrane excitability (sq)
skos:prefLabel	A molecular model of membrane excitability (en) A molecular model of membrane excitability (nl) A molecular model of membrane excitability (sq)
name	A molecular model of membrane excitability (en) A molecular model of membrane excitability (nl) A molecular model of membrane excitability (sq)
title	wds:Q68900312-7969121D-9104-4A8C-AF4C-5483B00C43E2
title	A molecular model of membrane excitability (en)
page(s)	wds:Q68900312-C00E71EC-6610-47A7-9F0E-3314E679CEBE
page(s)	538-557
instance of	wds:Q68900312-69DB488B-C3DA-49CC-87C6-DB6288368FB6
instance of	scholarly article
PubMed ID	wds:Q68900312-EFA3995F-27F7-4993-AF55-C966BECF5DCA
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4461846
PubMed ID	4461846
published in	wds:Q68900312-7F4E0C2A-A060-45D4-AD3C-CFA5070D042C
published in	Journal of supramolecular structure
issue	wds:Q68900312-DF08A198-DB11-42E4-9DE0-3ED99D2BFCB7
volume	wds:Q68900312-53E6547D-673A-4E89-9809-D13786AF7D9C
issue	5-6
volume	2
DOI	wds:Q68900312-3C4C929E-A665-4D8D-BDA5-7B1609C99216
DOI	http://dx.doi.org/10.1002/JSS.400020504
DOI	10.1002/JSS.400020504
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q68900312
is cites work of	Ionophoric activity of the antibiotic peptaibol trichorzin PA VI: a 23Na- and 35Cl-NMR study Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes Implication of segment S45 in the permeation pathway of voltage-dependent sodium channels A novel horse alpha-defensin: gene transcription, recombinant expression and characterization of the structure and function Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico. Electrically gated ionic channels in lipid bilayers Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMR Model ion channels: gramicidin and alamethicin An alamethicin channel in a lipid bilayer: molecular dynamics simulations Simulation studies of alamethicin-bilayer interactions Lipid-alamethicin interactions influence alamethicin orientation Lateral diffusion and conductance properties of a fluorescein-labelled alamethicin in planar lipid bilayers Alamethicin-like behaviour of new 18-residue peptaibols, trichorzins PA. Role of the C-terminal amino-alcohol in the ion channel forming activity Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy. Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR. Mode of action of the staphylococcinlike peptide Pep 5: voltage-dependent depolarization of bacterial and artificial membranes The biophysics of peptide models of ion channels Anti-tuberculosis activity of α-helical antimicrobial peptides: de novo designed L- and D-enantiomers versus L- and D-LL-37. Determination of molecular motion in membranes using periodic pattern photobleaching Voltage-gated cation conductance channel from fragmented sarcoplasmic reticulum: steady-state electrical properties. ATP induces nucleotide permeability in rat mast cells Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide Potassium current and the effect of cesium on this current during anomalous rectification of the egg cell membrane of a starfish Hydrogen bond stabilities in membrane-reconstituted alamethicin from amide-resolved hydrogen-exchange measurements Structure and function of channel-forming peptaibols Antiamoebin can function as a carrier or as a pore-forming peptaibol Signal transduction across alamethicin ion channels in the presence of noise Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states Dipole moment of alamethicin as related to voltage-dependent conductance in lipid bilayers Inactivation of monazomycin-induced voltage-dependent conductance in thin lipid membranes. I. Inactivation produced by long chain quaternary ammonium ions Properties of the conductance induced in lecithin bilayer membranes by alamethicin The role of the mitochondrial apoptosis induced channel MAC in cytochrome c release Structure, location, and lipid perturbations of melittin at the membrane interface Alamethicin. A rich model for channel behavior The lowest conductance state of the alamethicin pore Focal Targeting of the Bacterial Envelope by Antimicrobial Peptides Pressure effects on alamethicin conductance in bilayer membranes Experimental evidence consistent with aggregation kinetics in the sodium current of Myxicola giant axons Structural and dipolar properties of the voltage-dependent pore former alamethicin in octanol/dioxane Alamethicin-induced current-voltage curve asymmetry in lipid bilayers Markov process characterization of a single membrane gating site Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. A geometric sequence that accurately describes allowed multiple conductance levels of ion channels: the "three-halves (3/2) rule". Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation Effect of cholesterol and charge on pore formation in bilayer vesicles by a pH-sensitive peptide Ion channel subconductance states Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes Barrel-stave model or toroidal model? A case study on melittin pores. Transduction of membrane tension by the ion channel alamethicin Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formation

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