In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37 (original) (raw)

Therapeutic Action of Antimicrobial Cathelicidin Peptide LL-37 on a Murine Sepsis Model

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Development of novel LL-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application

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Human cathelicidin antimicrobial peptide LL-37

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Effect of antibacterial cathelicidin peptide CAP18/LL-37 on sepsis in neonatal rats

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In vitro and in vivo antimicrobial activity of two α-helical cathelicidin peptides and of their synthetic analogs

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Human anti-microbial cathelicidin peptide LL-37 suppresses the LPS-induced apoptosis of endothelial cells

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LL-37 Protects Rats against Lethal Sepsis Caused by Gram-Negative Bacteria

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The human cathelicidin LL-37 — A pore-forming antibacterial peptide and host-cell modulator

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Antimicrobial cathelicidin peptide LL-37 inhibits the pyroptosis of macrophages and improves the survival of polybacterial septic mice

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Antimicrobial Cathelicidin Peptide LL-37 Inhibits the LPS/ATP-Induced Pyroptosis of Macrophages by Dual Mechanism

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Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity

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Cationic amphipathic peptide analogs of cathelicidin LL‐37 as a probe in the development of antimicrobial/anticancer agents

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Biological Characterization of Two Novel Cathelicidin-derived Peptides and Identification of Structural Requirements for Their Antimicrobial and Cell Lytic Activities

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Anti-inflammatory Properties of Antimicrobial Peptides and Peptidomimetics: LPS and LTA Neutralization

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Lipid Segregation Explains Selective Toxicity of a Series of Fragments Derived from the Human Cathelicidin LL-37

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A stable cyclized antimicrobial peptide derived from LL-37 with host immunomodulatory effects and activity against uropathogens

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Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37

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Lysine substitutions convert a bacterial-agglutinating peptide into a bactericidal peptide that retains anti-lipopolysaccharide activity and low hemolytic activity

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Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37

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Cathelicidin Peptide Sheep Myeloid Antimicrobial Peptide-29 Prevents Endotoxin-induced Mortality in Rat Models of Septic Shock

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Human Host Defense Cathelicidin Peptide LL-37 Enhances the Lipopolysaccharide Uptake by Liver Sinusoidal Endothelial Cells without Cell Activation

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Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure

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