Antimicrobial Action and Cell Agglutination by the Eosinophil Cationic Protein Are Modulated by the Cell Wall Lipopolysaccharide Structure

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Molecular basis for endotoxin neutralization by amphipathic peptides derived from the α-helical cationic core-region of NK-lysin

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NMR Structural Determinants of Eosinophil Cationic Protein Binding to Membrane and Heparin Mimetics

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Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall

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Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site

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Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment

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Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7

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The1H,13C,15N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopy

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Genome Sequences of Escherichia coli B strains REL606 and BL21(DE3)

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Eosinophil Cationic Protein High-Affinity Binding to Bacteria-Wall Lipopolysaccharides and Peptidoglycans†

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Outer membrane permeability and antibiotic resistance

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The Antipathogen Activities of Eosinophil Cationic Protein

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