NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION - Wikidata - wikimedia - TriplyDB

NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION

NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION

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Inhibitory Effects of Antimicrobial Peptides on Lipopolysaccharide-Induced Inflammation On the role of NMR spectroscopy for characterization of antimicrobial peptides NMR Structures of the Histidine-Rich Peptide LAH4 in Micellar Environments: Membrane Insertion, pH-Dependent Mode of Antimicrobial Action, and DNA Transfection Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)Sequence context induced antimicrobial activity: insight into lipopolysaccharide permeabilization Pardaxin, a fish antimicrobial peptide, exhibits antitumor activity toward murine fibrosarcoma in vitro and in vivo In Vivo, In Vitro, and In Silico Characterization of Peptoids as Antimicrobial Agents New amphiphilic neamine derivatives active against resistant Pseudomonas aeruginosa and their interactions with lipopolysaccharides Mapping residue-specific contacts of polymyxin B with lipopolysaccharide by saturation transfer difference NMR: insights into outer-membrane disruption and endotoxin neutralization.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Snake venoms: attractive antimicrobial proteinaceous compounds for therapeutic purposes.Cobra cytotoxins: structural organization and antibacterial activity.Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance.Functional divergence in shrimp anti-lipopolysaccharide factors (ALFs): from recognition of cell wall components to antimicrobial activity.NMR structure of temporin-1 ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane.Membrane disruptive antimicrobial activities of human β-defensin-3 analogs.NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus.Immunomodulatory and Anti-Inflammatory Activities of Chicken Cathelicidin-2 Derived Peptides.Lipopolysaccharide-bound structure of the antimicrobial peptide cecropin P1 determined by nuclear magnetic resonance spectroscopy.Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.Combined Systems Approaches Reveal a Multistage Mode of Action of a Marine Antimicrobial Peptide against Pathogenic Escherichia coli and Its Protective Effect against Bacterial Peritonitis and Endotoxemia Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activities Use of the antimicrobial peptide pardaxin (GE33) to protect against methicillin-resistant Staphylococcus aureus infection in mice with skin injuries The role of biophysical parameters in the antilipopolysaccharide activities of antimicrobial peptides from marine fish.Application of NMR methods to the study of the interaction of natural products with biomolecular receptors.Lipopolysaccharide neutralization by antimicrobial peptides: a gambit in the innate host defense strategy.Molecular understanding of a potential functional link between antimicrobial and amyloid peptides.Antimicrobial peptide resistance in Neisseria meningitidis.Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control.Antimicrobial Peptides Share a Common Interaction Driven by Membrane Line Tension Reduction.Design of short membrane selective antimicrobial peptides containing tryptophan and arginine residues for improved activity, salt-resistance, and biocompatibility.Resurrecting inactive antimicrobial peptides from the lipopolysaccharide trap.Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control Multivalent gold nanoparticle-peptide conjugates for targeting intracellular bacterial infections.Synthetic Antimicrobial Peptides Exhibit Two Different Binding Mechanisms to the Lipopolysaccharides Isolated from Pseudomonas aeruginosa and Klebsiella pneumoniae.Does cholesterol play a role in the bacterial selectivity of antimicrobial peptides?Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs.The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids.Insight into the interactions, residue snorkeling, and membrane disordering potency of a single antimicrobial peptide into different lipid bilayers.

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P2860

NMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATION

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2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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NMR Structure of Pardaxin, a P ...... UTER MEMBRANE PERMEABILIZATION

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P2860

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

Antimicrobial peptides of multicellular organisms

LL-37, the only human member of the cathelicidin family of antimicrobial peptides

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

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Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies

The immunopathogenesis of sepsis

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