The co-evolution of host cationic antimicrobial peptides and microbial resistance.
about
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37Adaptation of the bacterial membrane to changing environments using aminoacylated phospholipidsThe human intestinal microbiome: a new frontier of human biologyComparative metagenomics revealed commonly enriched gene sets in human gut microbiomesFocal Targeting of the Bacterial Envelope by Antimicrobial PeptidesAntimicrobial Peptides as Potential Alternatives to Antibiotics in Food Animal IndustryRegulation of the Intestinal Barrier Function by Host Defense PeptidesMycobacterium tuberculosis: success through dormancyStrategies and molecular tools to fight antimicrobial resistance: resistome, transcriptome, and antimicrobial peptidesAntibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistanceMidkine in host defenceRole of Net Charge on Catalytic Domain and Influence of Cell Wall Binding Domain on Bactericidal Activity, Specificity, and Host Range of Phage LysinsCrystal structure and functional mechanism of a human antimicrobial membrane channelDermatophytic defensin with antiinfective potentialThe intramolecular disulfide-stapled structure of laterosporulin, a class IId bacteriocin, conceals a human defensin-like structural moduleSurvival strategies of yeast and filamentous fungi against the antifungal protein AFP.Beyond Traditional Antimicrobials: A Caenorhabditis elegans Model for Discovery of Novel Anti-infectivesAntimicrobial Activity of Cationic Antimicrobial Peptides against Gram-Positives: Current Progress Made in Understanding the Mode of Action and the Response of BacteriaCationic antimicrobial peptide LL-37 is effective against both extra- and intracellular Staphylococcus aureusHighly selective end-tagged antimicrobial peptides derived from PRELPInsect Antimicrobial Peptide Complexes Prevent Resistance Development in BacteriaL-Rhamnosylation of Listeria monocytogenes Wall Teichoic Acids Promotes Resistance to Antimicrobial Peptides by Delaying Interaction with the MembraneNovel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational ModificationsIn Vivo, In Vitro, and In Silico Characterization of Peptoids as Antimicrobial AgentsOligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.Discovery and characterization of a disulfide-locked C(2)-symmetric defensin peptide.Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membraneStructural and enzymatic analysis of TarM glycosyltransferase from Staphylococcus aureus reveals an oligomeric protein specific for the glycosylation of wall teichoic acid.Dermcidin-derived peptides show a different mode of action than the cathelicidin LL-37 against Staphylococcus aureus.The PDB database is a rich source of alpha-helical anti-microbial peptides to combat disease causing pathogens.Art-175 is a highly efficient antibacterial against multidrug-resistant strains and persisters of Pseudomonas aeruginosaKilling of Trypanozoon Parasites by the Equine Cathelicidin eCATH1.Single-Molecule Sequencing (PacBio) of the Staphylococcus capitis NRCS-A Clone Reveals the Basis of Multidrug Resistance and Adaptation to the Neonatal Intensive Care Unit Environment.The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion.Antimycobacterial activity of Pichia pastoris-derived mature bovine neutrophil β-defensins 5.Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides.Highly active and selective endopeptidases with programmed substrate specificitiesThe GraRS regulatory system controls Staphylococcus aureus susceptibility to antimicrobial host defenses.Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses.Transcriptome analysis of the responses of Staphylococcus aureus to antimicrobial peptides and characterization of the roles of vraDE and vraSR in antimicrobial resistance.
P2860
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P2860
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@ast
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@en
type
label
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@ast
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@en
prefLabel
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@ast
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@en
P356
P1476
The co-evolution of host cationic antimicrobial peptides and microbial resistance.
@en
P2093
Andreas Peschel
Hans-Georg Sahl
P2860
P2888
P304
P356
10.1038/NRMICRO1441
P407
P577
2006-06-12T00:00:00Z