Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
about
On the role of NMR spectroscopy for characterization of antimicrobial peptidesHydrogen-bond energetics drive helix formation in membrane interfaces.Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X.Membrane-active peptides: binding, translocation, and flux in lipid vesicles.Lipid membrane editing with peptide cargo linkers in cells and synthetic nanostructures.The nociceptive and anti-nociceptive effects of bee venom injection and therapy: a double-edged swordGain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Post-formulation peptide drug loading of nanostructures for metered control of NF-κB signalingMelittin-glutathione S-transferase fusion protein exhibits anti-inflammatory properties and minimal toxicity.Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptideMembrane curvature sensing by amphipathic helices: a single liposome study using α-synuclein and annexin B12Hydrogen Exchange Mass Spectrometry of Proteins at Langmuir MonolayersProgrammable nanoparticle functionalization for in vivo targeting.Conformational Heterogeneity of Bax Helix 9 Dimer for Apoptotic Pore FormationMechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Structure-function relationships of membrane-associated GT-B glycosyltransferases.Cationic amphiphiles, a new generation of antimicrobials inspired by the natural antimicrobial peptide scaffoldSurvey of the year 2009: applications of isothermal titration calorimetry.Melittin, the Major Pain-Producing Substance of Bee VenomThe electrical response of bilayers to the bee venom toxin melittin: evidence for transient bilayer permeabilization.Thermodynamic profiling of peptide membrane interactions by isothermal titration calorimetry: a search for pores and micelles.Selective membrane disruption: mode of action of C16G2, a specifically targeted antimicrobial peptide.Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides.Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes.Conformational changes, from β-strand to α-helix, of the fatty acid-binding protein ReP1-NCXSQ in anionic lipid membranes: dependence with the vesicle curvature.Exploring homo-FRET to quantify the oligomer stoichiometry of membrane-bound proteins involved in a cooperative partition equilibrium.pH-Dependent membrane lysis by using melittin-inspired designed peptides.Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.
P2860
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P2860
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@en
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@nl
type
label
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@en
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@nl
prefLabel
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@en
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@nl
P2093
P356
P1433
P1476
Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation.
@en
P2093
Gabriela Klocek
Joachim Seelig
Therese Schulthess
Yechiel Shai
P304
P356
10.1021/BI802127H
P407
P577
2009-03-01T00:00:00Z