Proteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythia
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Host response mechanisms in periodontal diseasesThe structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinasesStructure of the catalytic domain of theTannerella forsythiamatrix metallopeptidase karilysin in complex with a tetrapeptidic inhibitorA phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme Karilysin can be truncated to Ser-Trp-Phe-ProDiagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis.Actin enables the antimicrobial action of LL-37 peptide in the presence of microbial proteasesDichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins.LL-37 in periodontal health and disease and its susceptibility to degradation by proteinases present in gingival crevicular fluid.KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structureInactivation of the antifungal and immunomodulatory properties of human cathelicidin LL-37 by aspartic proteases produced by the pathogenic yeast Candida albicans.A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system.Influence of saliva on the oral microbiota.Outer membrane vesicles of Tannerella forsythia: biogenesis, composition, and virulenceMirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.Human neutrophils and oral microbiota: a constant tug-of-war between a harmonious and a discordant coexistence.Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen Porphyromonas gingivalis during invasion.A novel mechanism of latency in matrix metalloproteinases.Mammalian antimicrobial peptide influences control of cutaneous Leishmania infection.The antibacterial activity of LL-37 against Treponema denticola is dentilisin protease independent and facilitated by the major outer sheath protein virulence factor.In vivo expression of proteases and protease inhibitor, a serpin, by periodontal pathogens at teeth and implants.Trefoil factors in saliva and gingival tissues of patients with chronic periodontitis.
P2860
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P2860
Proteolytic inactivation of LL-37 by karilysin, a novel virulence mechanism of Tannerella forsythia
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@ast
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@en
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@nl
type
label
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@ast
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@en
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@nl
prefLabel
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@ast
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@en
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@nl
P2093
P2860
P50
P356
P1476
Proteolytic inactivation of LL ...... hanism of Tannerella forsythia
@en
P2093
Joanna Koziel
Kornelia Przybyszewska
Maria Rapala-Kozik
Miroslaw Ksiazek
P2860
P304
P356
10.1159/000281881
P577
2010-02-04T00:00:00Z