about
Activity of protegrins against yeast-phase Candida albicansSusceptibility of Neisseria gonorrhoeae to protegrinsCathelicidins: family of antimicrobial peptides. A reviewStructural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micellesAntimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR studyStructural organization of the bovine cathelicidin gene family and identification of a novel member.Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection.Antimicrobial peptides as mediators of epithelial host defense.Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils.Haemophilus ducreyi is susceptible to protegrin.Protegrins: new antibiotics of mammalian origin.Sensitivity of periodontal pathogens to the bactericidal activity of synthetic protegrins, antibiotic peptides derived from porcine leukocytes.Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity.Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins.Synthesis and solution structure of the antimicrobial peptide protegrin-1.The porcine lung as a potential model for cystic fibrosisStructures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39.Cathelicidin gene expression in porcine tissues: roles in ontogeny and tissue specificity.Effect of glucocorticoids on the synthesis of antimicrobial peptides in amphibian skin.Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides.Defining the genetic relationship of protegrin-related sequences and the in vivo expression of protegrins.Enhanced resistance to bacterial infection in protegrin-1 transgenic mice.Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and atlantic salmon (Salmo salar).Antimicrobial and conformational studies of the active and inactive analogues of the protegrin-1 peptide.The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils.Molecular cloning of a bombinin gene from Bombina orientalis: detection of NF-kappaB and NF-IL6 binding sites in its promoter.Gene-encoded peptide antibiotics and innate immunity. Do 'animalcules' have defence budgets?Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide.Transcriptional regulation of cathelicidin genes in chicken bone marrow cells.
P2860
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P2860
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
The structure of porcine protegrin genes.
@ast
The structure of porcine protegrin genes.
@en
The structure of porcine protegrin genes.
@nl
type
label
The structure of porcine protegrin genes.
@ast
The structure of porcine protegrin genes.
@en
The structure of porcine protegrin genes.
@nl
prefLabel
The structure of porcine protegrin genes.
@ast
The structure of porcine protegrin genes.
@en
The structure of porcine protegrin genes.
@nl
P2860
P1433
P1476
The structure of porcine protegrin genes.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(95)00633-K
P407
P50
P577
1995-07-01T00:00:00Z