Structure and orientation of pardaxin determined by NMR experiments in model membranes.
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Studies on anticancer activities of antimicrobial peptidesFocal Targeting of the Bacterial Envelope by Antimicrobial PeptidesOn the role of NMR spectroscopy for characterization of antimicrobial peptidesThe magic of bicelles lights up membrane protein structureNMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATIONA kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environmentsDisulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)Pardaxin, a fish antimicrobial peptide, exhibits antitumor activity toward murine fibrosarcoma in vitro and in vivoDeletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective bindingNMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.Modular determinants of antimicrobial activity in platelet factor-4 family kinocidins.Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruptionAntimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation.Lipid polymorphism induced by surfactant peptide SP-B(1-25)Snake venoms: attractive antimicrobial proteinaceous compounds for therapeutic purposes.Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers.Probing membrane topology of the antimicrobial peptide distinctin by solid-state NMR spectroscopy in zwitterionic and charged lipid bilayers.Human cannabinoid 1 GPCR C-terminal domain interacts with bilayer phospholipids to modulate the structure of its membrane environment.Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin.Membrane orientation of MSI-78 measured by sum frequency generation vibrational spectroscopy.Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR.Synthesis and characterization of the 47-residue heterodimeric antimicrobial peptide distinctin, featuring directed disulfide bridge formationProline facilitates membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disorderingStructure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studiesHigh-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands.When detergent meets bilayer: birth and coming of age of lipid bicelles.Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation.Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights.Lipid composition-dependent membrane fragmentation and pore-forming mechanisms of membrane disruption by pexiganan (MSI-78)Penetration depth of surfactant peptide KL4 into membranes is determined by fatty acid saturation.Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.Dynamic conformational responses of a human cannabinoid receptor-1 helix domain to its membrane environment.Retinal dynamics during light activation of rhodopsin revealed by solid-state NMR spectroscopy.Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Membrane proteins structure and dynamics by nuclear magnetic resonance.Studying the structure and dynamics of biomolecules by using soluble paramagnetic probesMolecular understanding of a potential functional link between antimicrobial and amyloid peptides.Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells.Solution NMR studies on Helicobacter pylori proteins for antibiotic target discovery.
P2860
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P2860
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@ast
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@en
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@nl
type
label
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@ast
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@en
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@nl
prefLabel
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@ast
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@en
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@nl
P2093
P2860
P356
P1476
Structure and orientation of pardaxin determined by NMR experiments in model membranes.
@en
P2093
Ayyalusamy Ramamoorthy
Bethany Buck
Dong-Kuk Lee
Fernando Porcelli
Gianluigi Veglia
Kevin J Hallock
P2860
P304
45815-45823
P356
10.1074/JBC.M405454200
P407
P577
2004-07-29T00:00:00Z