Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold
about
NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display librariesPutative bioactive motif of tritrpticin revealed by an antibody with biological receptor-like propertiesOrientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.Structure of the antimicrobial, cationic hexapeptide cyclo(RRWWRF) and its analogues in solution and bound to detergent micelles.Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMRSolution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activityRelative free energy of binding between antimicrobial peptides and SDS or DPC micelles.Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides.Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules.Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defensesDeconstructing the DGAT1 enzyme: membrane interactions at substrate binding sites.Length effects in antimicrobial peptides of the (RW)n seriesStructure-function analyses involving palindromic analogs of tritrypticin suggest autonomy of anti-endotoxin and antibacterial activities.Using O2 to probe membrane immersion depth by 19F NMR.The π Configuration of the WWW Motif of a Short Trp-Rich Peptide Is Critical for Targeting Bacterial Membranes, Disrupting Preformed Biofilms, and Killing Methicillin-Resistant Staphylococcus aureus.The proteome targets of intracellular targeting antimicrobial peptides.Archetypal tryptophan-rich antimicrobial peptides: properties and applications.Sequential and Structural Aspects of Antifungal Peptides from Animals, Bacteria and Fungi Based on Bioinformatics Tools.Position-Dependent Influence of the Three Trp Residues on the Membrane Activity of the Antimicrobial Peptide, Tritrpticin.Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.In vitro activities of tritrpticin alone and in combination with other antimicrobial agents against Pseudomonas aeruginosa.The addressing fragment of mitogaligin: first insights into functional and structural properties.Relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determine their cytotoxicity.Structural Elucidation of the Cell-Penetrating Penetratin Peptide in Model Membranes at the Atomic Level: Probing Hydrophobic Interactions in the Blood-Brain BarrierConformation of a bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide.Functional gold nanoparticle-based antibacterial agents for nosocomial and antibiotic-resistant bacteria.De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activityStaphylokinase has distinct modes of interaction with antimicrobial peptides, modulating its plasminogen-activation properties.The optimization of polymalic acid peptide copolymers for endosomolytic drug delivery.Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular-dynamics simulations.Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures.The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide.Structures and mode of membrane interaction of a short alpha helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy.Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4.Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions.Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure.Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5.Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide.Hydrocarbon-stapled lipopeptides exhibit selective antimicrobial activity.
P2860
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P2860
Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@ast
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@en
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@nl
type
label
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@ast
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@en
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@nl
prefLabel
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@ast
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@en
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@nl
P2093
P3181
P356
P1433
P1476
Structure of the antimicrobial ...... ct membrane-bound peptide fold
@en
P2093
P304
P3181
P356
10.1021/BI990701C
P407
P577
1999-12-21T00:00:00Z