Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37.
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Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2Gram-positive anaerobic cocci--commensals and opportunistic pathogensStrategies 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 resistanceEnteric bacterial proteases in inflammatory bowel disease- pathophysiology and clinical implicationsHost defense peptides of thrombin modulate inflammation and coagulation in endotoxin-mediated shock and Pseudomonas aeruginosa sepsisStructural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37A cactus-derived toxin-like cystine knot Peptide with selective antimicrobial activityAntimicrobial Activity of Cationic Antimicrobial Peptides against Gram-Positives: Current Progress Made in Understanding the Mode of Action and the Response of BacteriaExtracellular Bacterial Proteases in Chronic Wounds: A Potential Therapeutic Target?Protein C inhibitor--a novel antimicrobial agentComplicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilisAlpha-defensins in enteric innate immunity: functional Paneth cell alpha-defensins in mouse colonic lumen.Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptidesalpha2-Macroglobulin-proteinase complexes protect Streptococcus pyogenes from killing by the antimicrobial peptide LL-37.EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activitySpeB of Streptococcus pyogenes differentially modulates antibacterial and receptor activating properties of human chemokines.End-tagging of ultra-short antimicrobial peptides by W/F stretches to facilitate bacterial killing.The anticancer activity of lytic peptides is inhibited by heparan sulfate on the surface of the tumor cells.Human salivary mucin MUC7 12-mer-L and 12-mer-D peptides: antifungal activity in saliva, enhancement of activity with protease inhibitor cocktail or EDTA, and cytotoxicity to human cells.Small lytic peptides escape the inhibitory effect of heparan sulfate on the surface of cancer cells.Streptococcus pyogenes polymyxin B-resistant mutants display enhanced ExPortal integrity.Hydrophobicity and helicity regulate the antifungal activity of 14-helical β-peptides.Growth characteristics of and virulence factor production by group A Streptococcus during cultivation in human salivaActin enables the antimicrobial action of LL-37 peptide in the presence of microbial proteasesEvaluation of the ability of LL-37 to neutralise LPS in vitro and ex vivo.Pseudomonas aeruginosa elastase provides an escape from phagocytosis by degrading the pulmonary surfactant protein-A.The ability of Proteus mirabilis to sense surfaces and regulate virulence gene expression involves FliL, a flagellar basal body protein.Deciphering the magainin resistance process of Escherichia coli strains in light of the cytosolic proteomeProteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythiaProtease-armed bacteria in the skin.Gelatinase contributes to the pathogenesis of endocarditis caused by Enterococcus faecalis.Macrophage-pathogen interactions in infectious diseases: new therapeutic insights from the zebrafish host modelIsomerization of an antimicrobial peptide broadens antimicrobial spectrum to gram-positive bacterial pathogensAntimicrobial Peptide Resistance Mechanisms of Gram-Positive Bacteria.Full activation of Enterococcus faecalis gelatinase by a C-terminal proteolytic cleavage.The endothelin system has a significant role in the pathogenesis and progression of Mycobacterium tuberculosis infection.New insights into the antimicrobial effect of mast cells against Enterococcus faecalisThe human antimicrobial peptide LL-37 binds directly to CsrS, a sensor histidine kinase of group A Streptococcus, to activate expression of virulence factors.Evolution of antimicrobial peptides to self-assembled peptides for biomaterial applications
P2860
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P2860
Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Proteinases of common pathogen ...... e antibacterial peptide LL-37.
@en
type
label
Proteinases of common pathogen ...... e antibacterial peptide LL-37.
@en
prefLabel
Proteinases of common pathogen ...... e antibacterial peptide LL-37.
@en
P2093
P2860
P1476
Proteinases of common pathogen ...... e antibacterial peptide LL-37.
@en
P2093
Artur Schmidtchen
Emma Andersson
Hans Tapper
Inga-Maria Frick
Lars Björck
P2860
P304
P356
10.1046/J.1365-2958.2002.03146.X
P407
P577
2002-10-01T00:00:00Z