Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
about
β-Microseminoprotein endows post coital seminal plasma with potent candidacidal activity by a calcium- and pH-dependent mechanismKeratinocyte production of cathelicidin provides direct activity against bacterial skin pathogensCell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epitheliumAntimicrobial proteins and polypeptides in pulmonary innate defenceAntimicrobial polypeptides in host defense of the respiratory tractA cleavage-potentiated fragment of tear lacritin is bactericidal.Vitamin D and the anti-viral stateThe vitamin D-antimicrobial peptide pathway and its role in protection against infectionStudies on anticancer activities of antimicrobial peptidesMultiple Functions of the New Cytokine-Based Antimicrobial Peptide Thymic Stromal Lymphopoietin (TSLP)Inhibitors of Serine Proteases in Regulating the Production and Function of Neutrophil Extracellular TrapsThe role of antimicrobial peptides in chronic inflammatory skin diseasesPotential Use of Antimicrobial Peptides as Vaginal Spermicides/MicrobicidesAntiviral potential of cathelicidinsThe new insight into the role of antimicrobial proteins-alarmins in the immunopathogenesis of psoriasisAnti-Inflammatory and Antimicrobial Actions of Vitamin D in Combating TB/HIVExtrarenal expression of the 25-hydroxyvitamin D-1-hydroxylaseCationic antimicrobial peptides promote microbial mutagenesis and pathoadaptation in chronic infectionsStructural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37Proteomic analysis of human neutrophil granulesProtein C inhibitor--a novel antimicrobial agentCathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1LInteractions between neutrophil-derived antimicrobial peptides and airway epithelial cellsLow plasma level of cathelicidin antimicrobial peptide (hCAP18) predicts increased infectious disease mortality in patients undergoing hemodialysisSnake cathelicidin from Bungarus fasciatus is a potent peptide antibioticsAntiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37Analysis and prediction of the critical regions of antimicrobial peptides based on conditional random fieldsThe lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils.Opa+ Neisseria gonorrhoeae exhibits reduced survival in human neutrophils via Src family kinase-mediated bacterial trafficking into mature phagolysosomesNeisseria gonorrhoeae phagosomes delay fusion with primary granules to enhance bacterial survival inside human neutrophils.Resistance of Neisseria gonorrhoeae to neutrophils.The pro-inflammatory peptide LL-37 promotes ovarian tumor progression through recruitment of multipotent mesenchymal stromal cells.A theoretical approach to spot active regions in antimicrobial proteins.Human antimicrobial peptide LL-37 is present in atherosclerotic plaques and induces death of vascular smooth muscle cells: a laboratory study.Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin.Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses.Bactericidal activities of the cationic steroid CSA-13 and the cathelicidin peptide LL-37 against Helicobacter pylori in simulated gastric juiceGeneric and specific adaptive responses of Streptococcus pneumoniae to challenge with three distinct antimicrobial peptides, bacitracin, LL-37, and nisin.Uropathogenic Escherichia coli modulates immune responses and its curli fimbriae interact with the antimicrobial peptide LL-37.Circulating cathelicidin levels correlate with mucosal disease activity in ulcerative colitis, risk of intestinal stricture in Crohn's disease, and clinical prognosis in inflammatory bowel disease.
P2860
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P2860
Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
description
2001 nî lūn-bûn
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2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
name
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@ast
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@en
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@nl
type
label
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@ast
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@en
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@nl
prefLabel
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@ast
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@en
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@nl
P2093
P3181
P1433
P1476
Human cathelicidin, hCAP-18, i ...... lar cleavage with proteinase 3
@en
P2093
A H Johnsen
G S Tjabringa
N Borregaard
P S Hiemstra
P304
P3181
P356
10.1182/BLOOD.V97.12.3951
P407
P577
2001-06-01T00:00:00Z