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International Journal of Antimicrobial Agents|July 15, 2010
The antimicrobial peptide Ci-MAM-A24 is highly active against multidrug-resistant and anaerobic bacteria pathogenic for humansHenning Fedders, Rainer Podschun, Matthias Leippe
Developmental and Comparative Immunology|February 20, 2003
Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranesJörg Andrä, Rosa Herbst, Matthias Leippe
FEBS Letters|April 20, 2004
Membrane lipid composition protects Entamoeba histolytica from self-destruction by its pore-forming toxinsJörg Andrä, Otto Berninghausen, Matthias Leippe
The Journal of Biological Chemistry|April 13, 2004
Antimicrobial and pore-forming peptides of free-living and potentially highly pathogenic Naegleria fowleri are released from the same precursor moleculeRosa Herbst, Francine Marciano-Cabral, Matthias Leippe
Bioscience Reports|May 10, 2023
A guided tour through α-helical peptide antibiotics and their targetsNils Preußke, Frank Dieter Sönnichsen, Matthias Leippe
The Biochemical Journal|July 5, 2008
An exceptional salt-tolerant antimicrobial peptide derived from a novel gene family of haemocytes of the marine invertebrate Ciona intestinalisHenning Fedders, Matthias Michalek, Joachim Grötzinger, et al.
Trends in Parasitology|January 11, 2005
Ancient weapons: the three-dimensional structure of amoebapore AMatthias Leippe, Heike Bruhn, Oliver Hecht, et al.
Biological Chemistry|October 11, 2008
An efficient fluorimetric method to measure the viability of intraerythrocytic Plasmodium falciparumAstrid Evers, Saskia Heppner, Matthias Leippe, et al.
Biological Chemistry|June 2, 2005
Blocking effect of a biotinylated protease inhibitor on the egress of Plasmodium falciparum merozoites from infected red blood cellsChristoph Gelhaus, Radim Vicik, Tanja Schirmeister, et al.
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