Cecropins

Known as: Cecropins [Chemical/Ingredient], cecropin 
Antimicrobial peptides that form channels in membranes that are more permeable to anions than cations. They resemble MAGAININS, with their N-terminal… (More)
National Institutes of Health

Papers overview

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Review
2003
Review
2003
Antibacterial peptides are the effector molecules of innate immunity. Generally they contain 15-45 amino acid residues and the… (More)
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1996
1996
The lytic peptides, cecropins, were originally isolated from the haemolymph of the giant silk moth, Hyalophora cecropia and… (More)
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Highly Cited
1995
Highly Cited
1995
Cecropins are positively charged antibacterial polypeptides that were originally isolated from insects. Later on a mammalian… (More)
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Highly Cited
1994
Highly Cited
1994
The cecropins are a group of peptides that were first isolated from the hemolymph of the giant silk moth, Hyalophora cecropia. In… (More)
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Review
1992
Review
1992
The outer membrane of gram-negative bacteria provides the cell with an effective permeability barrier against external noxious… (More)
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1989
1989
Magainins and cecropins are families of peptides with broad antimicrobial and antiparasitic activities derived respectively from… (More)
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Highly Cited
1989
Highly Cited
1989
Solid phase synthesis was used to produce 5 hybrid peptides containing sequences from the antibacterial peptide, cecropin A, and… (More)
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Highly Cited
1988
Highly Cited
1988
Cecropins, positively charged antibacterial peptides found in the cecropia moth, and synthetic peptide analogs form large time… (More)
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Highly Cited
1988
Highly Cited
1988
The mechanism of action of cecropin was studied by using liposomes as a model system. The bilayer was efficiently destroyed if… (More)
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Highly Cited
1982
Highly Cited
1982
We have investigated low molecular weight antibacterial proteins from the Cecropia moth. Hyalophora cecropia. In addition to the… (More)
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