[Sequence analysis of melittin from tryptic and peptic degradation products]
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Studies on anticancer activities of antimicrobial peptidesBarrel-stave model or toroidal model? A case study on melittin pores.Structure-function relationship of antibacterial synthetic peptides homologous to a helical surface region on human lactoferrin against Escherichia coli serotype O111.The structure of melittin in the form I crystals and its implication for melittin's lytic and surface activities.Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared studyUltrasonic study of melittin effects on phospholipid model membranes.Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.Conformation and dynamics of melittin bound to magnetically oriented lipid bilayers by solid-state (31)P and (13)C NMR spectroscopy.Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane.Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature.All-D amino acid-containing channel-forming antibiotic peptides.Amino acid sequence of honeybee prepromelittin synthesized in vitroAction of melittin on the DPPC-cholesterol liquid-ordered phase: a solid state 2H-and 31P-NMR studyDynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR.Structural studies of bee melittinThe sting. Melittin forms channels in lipid bilayers.Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formationRetro and retroenantio analogs of cecropin-melittin hybrids.Translation of melittin messenger RNA in vitro yields a product terminating with glutaminylglycine rather than with glutaminamideModulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cationsGenetically Engineered Yeast Expressing a Lytic Peptide from Bee Venom (Melittin) Kills Symbiotic Protozoa in the Gut of Formosan Subterranean Termites.Antimicrobial Peptide CMA3 Derived from the CA-MA Hybrid Peptide: Antibacterial and Anti-inflammatory Activities with Low Cytotoxicity and Mechanism of Action in Escherichia coliPeptide antimicrobial agents.Three neurotoxins from the venom of a sea snake Astrotia stokesii, including two long-chain neurotoxic proteins with amidated C-termini.Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum.Design of an α-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activityProteolytically activated anti-bacterial hydrogel microspheresActive, soluble recombinant melittin purified by extracting insoluble lysate of Escherichia coli without denaturation.Membrane-active host defense peptides--challenges and perspectives for the development of novel anticancer drugs.Therapeutic approaches using host defence peptides to tackle herpes virus infections.Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity.Determination of toxin-induced leakage of different-size nucleotides through the plasma membrane of human diploid fibroblasts.Improvement of outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification.The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein H.Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding.The structure of melittin in membranes.Phospholipid flip-flop modulated by transmembrane peptides WALP and melittin.Melittin and the 8-26 fragment. Differences in ionophoric properties as measured by monolayer methodCleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues.Determination of the secondary structure of selected melittin analogues with different haemolytic activities.
P2860
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P2860
[Sequence analysis of melittin from tryptic and peptic degradation products]
description
1967 nî lūn-bûn
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1967年の論文
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1967年学术文章
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1967年学术文章
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1967年学术文章
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1967年学术文章
@zh-hans
1967年学术文章
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1967年学术文章
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1967年學術文章
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1967年學術文章
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name
[Sequence analysis of melittin from tryptic and peptic degradation products]
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[Sequence analysis of melittin from tryptic and peptic degradation products]
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type
label
[Sequence analysis of melittin from tryptic and peptic degradation products]
@en
[Sequence analysis of melittin from tryptic and peptic degradation products]
@nl
prefLabel
[Sequence analysis of melittin from tryptic and peptic degradation products]
@en
[Sequence analysis of melittin from tryptic and peptic degradation products]
@nl
P1476
[Sequence analysis of melittin from tryptic and peptic degradation products]
@en
P2093
Habermann E
P577
1967-01-01T00:00:00Z