2019 2018 2017 2016 2015 2014 2013 2012 2011 2010 

2009 2008 2007 2006 2005 2004 2003 before 2003




Lamrabet, O., Jauslin, T., Lima, W. C., Leippe, M., Cosson, P. (2020) The multifarious lysozyme arsenal of Dictyostelium discoideum
Dev. Comp. Immunol., in press  PubMed Abstract

Zimmermann, J., Obeng, N., Yang, W., Pees, B., Petersen, C., Washina, S., Kissoyan, K. A., Aidley, J., Hoeppner, M. P., Bunk, B., Spröer, C., Leippe, M., Dierking, K., Kaleta, C., Schulenburg, H. (2020). The functional repertoire encoded within the native microbiota of the model nematode Caenorhabditis elegans.
ISME J. 14, 26-38. PubMed Abstract




Yang, W., Petersen, C., Pees, B., Zimmermann, J., Waschina, S., Dirksen, P., Rosenstiel, P., Tholey, A., Leippe, M., Dierking, K., Kaleta, C., Schulenburg, H. (2019). The inducible response of the nematode Caenorhabditis elegans to members of its natural microbiota across development and adult life.
Front. Microbiol. 10:1793. PubMed Abstract

Lee H. G., Stumpp M., Yan J. J., Tseng Y. C., Heinzel S., Hu M. Y. (2019). Tipping points of gastric pH regulation and energetics in the sea urchin larva exposed to CO2-induced seawater acidification.
Comp. Biochem. Physiol. A Mol. Integr. Physiol. 234, 87-97. PubMed Abstract

Stumpp M., Dupont S., Hu M. Y. (2019). Measurement of feeding rates, respiration, and pH regulatory processes in the light of ocean acidification research.
Methods Cell. Biol. 150, 391-409.  PubMed Abstract

Lettau, M., Dietz, M., Dohmen, K., Leippe, M., Kabelitz, D., Janssen, O. (2019). Granulysin species segregate to different lysosome-related effector vesicles (LREV) and get mobilized by either classical or non-classical degranulation. 
Mol. Immunol. 107, 44–53. PubMed Abstract




Hu, M. Y., Yan, J. J., Petersen, I., Himmerkus, N., Bleich, M., Stumpp, M. (2018). A SLC4 family bicarbonate transporter is critical for intracellular pH regulation and biomineralization in sea urchin embryos. 
eLife 2018 7, e36600. PubMed Abstract

Hu, M. Y., Lein, E., Bleich, M., Melzner, F., Stumpp, M. (2018). Trans-life cycle acclimation to experimental ocean acidification affects gastric pH homeostasis and larval recruitment in the sea star Asterias rubens. 
Acta Physiologica 224(2), e13075. PubMed Abstract

Dhakshinamoorthy, R., Bitzhenner, M., Cosson, P., Soldati, T., Leippe, M. (2018). The saposin-like protein AplD displays pore-forming activity and participates in defence against bacterial infection during a multicellular stage of Dictyostelium discoideum.
Front. Cell. Infect. Microbiol. 8, 73.  PubMed Abstract

Cassidy, L., Petersen, C., Treitz, C., Dierking, K., Schulenburg, H., Leippe, M., Tholey, A. (2018). The C. elegans proteome response to naturally associated microbiome members of the genus Ochrobactrum.
Proteomics 18(8), e1700426. PubMed Abstract

Leipert, J., Bobis, I., Schubert, S., Fickenscher, H., Leippe, M., Tholey, A. (2018). Miniaturized dispersive liquid-liquid microextraction and MALDI MS using ionic liquid matrices for the detection of bacterial communication molecules and virulence factors.
Anal. Bioanal. Chem. 410, 4737-4748. PubMed Abstract




Hu, M., Tseng, Y.-C., Su, Y.-H., Lein, E., Lee, H.-G., Lee, J.-R., Dupont, S., Stumpp, M. (2017). Variability in larval gut pH regulation defines sensitivity to ocean acidification in six species of the Ambulacraria superphylum.
Proc. R. Soc. B 284, 20171066. PubMed Abstract

Leipert, J., Treitz, C., Leippe, M., Tholey, A. (2017). Identification and quantification of N-Acyl homoserine lactones involved in bacterial communication by small-scale synthesis of internal standards and matrix-assisted laser desorption/ionization mass spectrometry. 
J. Am. Soc. Mass Spectrom. 28, 2538-2547. PubMed Abstract

Huth, S., Reverey, J. F., Leippe, M., Selhuber-Unkel, C. (2017). Adhesion forces and mechanics in mannose-mediated Acanthamoeba interactions. 
PLOS ONE 12(5), e0176207. PubMed Abstract




Cauchard, S., Van Reet, N., Büscher, P., Goux, D., Grötzinger, J., Leippe, M., Cattoir, V., Laugier, C., Cauchard, J. (2016). Killing of Trypanozoon parasites by the equine cathelicidin eCATH1. 
Antimicrob. Agents Chemother. 60, 2610-2619. PubMed Abstract




Reverey, J., Jeon, J.-H., Bao, H., Leippe, M., Metzler, R., Selhuber-Unkel, C. (2015). Superdiffusion dominates intracellular particle motion in the supercrowded space of pathogenic Acanthamoeba castellanii. 
Scientific Reports 5, 11690. PubMed Abstract

Michalek, M., Leippe, M. (2015).  Mechanistic insights into the lipid interaction of an ancient saposin-like protein.
Biochemistry 54, 1778-1786. PubMed Abstract

Yang, W., Dierking, K., Esser, D., Tholey, A., Leippe, M., Rosenstiel, P., Schulenburg, H. (2015). Overlapping and unique signatures in the proteomic and transcriptomic responses of the nematode Caenorhabditis elegans towards pathogenic Bacillus thuringiensis.
Dev. Comp. Immunol. 51, 1-9. PubMed Abstract

Schlusselhuber, M., Humblot, V., Casale, S., Métivier, C., Verdon, J., Leippe,  M., Berjeaud, J.-M. (2015). Potent antimicrobial peptides against Legionella pneumophila and its environmental host, Acanthamoeba castellanii
Appl. Microbiol. Biotechnol. 99, 4879-4891. PubMed Abstract

Treitz, C., Cassidy, L., Höckendorf, A., Leippe, M., Tholey, A. (2015). Quantitative proteome analysis of Caenorhabditis elegans upon exposure to nematicidal Bacillus thuringiensis.
J. Proteomics 113, 337-350. PubMed Abstract




Hung, C.-W., Jung, S., Grötzinger, J., Gelhaus, C., Leippe, M., Tholey, A. (2014). Determination of disulfide linkages in antimicrobial peptides of the macin family by combination of top-down and bottom-up proteomics. 
J. Proteomics 103, 216-226. 

Tasiemski, A., Jung, S., Boidin-Wichlacz, C., Jollivet, D., Cuvillier-Hot, V., Pradillon, F., Vetriani, C., Hecht, O., Sönnichsen, F. D., Gelhaus, C., Hung, C.-W., Tholey, A., Leippe, M., Grötzinger, J., Gaill, F. (2014). Characterization and function of the first antibiotic isolated from a vent organism: the extremophile metazoan Alvinella pompejana
PLOS ONE 9, e95737.  

Leippe, M. (2014). Pore-forming toxins from pathogenic amoebae.
Appl. Microbiol. Biotechnol. 98, 4347-4353 (Review). 

Haselmann, V., Kurz, A., Bertsch, U., Hübner, S., Olempska-Müller, M., Fritsch, J.,  Häsler, R., Pickl, A., Fritsche, H., Annewanter, F., Engler, C., Fleig, B., Bernt, A., Röder, C., Schmidt, H., Gelhaus, C., Hauser, C., Egberts, J.-H., Heneweer, C., Rohde, A. M., Böger, C., Knippschild, U., Röcken, C., Adam, D., Walczak, H., Schütze, S., Janssen, O., Wulczyn, F. G., Wajant, H.,  Kalthoff, H., Trauzold, A. (2014). Nuclear death receptor TRAIL-R2 inhibits maturation of let-7 and promotes tumor growth.
Gastroenterology 146, 278-290. 

Schlusselhuber, M., Guldbech, C., Sévin, C., Leippe, M., Petry, S., Grötzinger, J., Giguère, S., Cauchard, J. (2014). In vitro effectiveness of the antimicrobial peptide eCATH1 against antibiotic-resistant bacterial pathogens of horses.
FEMS Microbiol. Lett. 350, 216-222. 

Reverey, J. F., Fromme, R., Leippe, M., Selhuber-Unkel, S. (2014). In vitro adhesion of Acanthamoeba castellanii to soft contact lenses depends on water content and disinfection procedure.
Cont. Lens Anterior Eye 37, 262-266. 




Schlusselhuber, M., Torelli, R., Martini, C., Leippe, M., Cattoir, V., Leclercq, R., Laugier, C., Grötzinger, J., Sanguinetti , M., Cauchard, J. (2013). The equine antimicrobial peptide eCATH1 is effective against the facultative intracellular pathogen Rhodococcus equi in mice.
Antimicrob. Agents Chemother. 57, 4615-4621. 

Rahn, T., Leippe, M., Roeder, T., Fedders, H. (2013). EGFR signaling in the brain is necessary for olfactory learning in Drosophila larvae.
Learning & Memory 20, 194-200. 

Michalek, M., Sönnichsen, F. D., Wechselberger, R., Dingley, A. J., Hung, C.-W., Kopp, A., Wienk, H., Simanski, M., Herbst, R., Lorenzen, I., Marciano-Cabral, F., Gelhaus, C., Gutsmann, T., Tholey, A., Grötzinger, J., Leippe, M. (2013). Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.
Nature Chem. Biol. 9, 37-42. 
(The article has been selected for Faculty 1000 – F1000Prime. It was recommended as being of special significance in its field.)



Philipp, S., Oberg, H.-H., Janssen, O., Leippe, M., Gelhaus, C. (2012). Isolation of erythrocytes infected with viable early stages of Plasmodium falciparum by flow cytometry.
Cytometry Part A 81, 1048-1054. 

Polier, G., Neumann, J., Thuaud, F., Ribeiro, N., Gelhaus, C., Schmidt, H., Giaisi, M., Köhler, R., Müller, W.W., Proksch, P., Leippe, M., Janssen, O., Désaubry, L., Krammer, P.H., Li-Weber, M. (2012). The natural anti-cancer compounds rocaglamides inhibit the Raf-MEK-ERK pathway by targeting prohibitin 1 and 2.
Chem. Biol. 19, 1093–1104. 

De Colibus, L., Sonnen, A. F.-P., Morris, K. J., Siebert, C. A., Abrusci, P., Plitzko, J., Hodnik, V., Leippe, M., Volpi, E., Anderluh, G., Gilbert, R. J. C. (2012). Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and a novel mode of sphingomyelin recognition. 
Structure 20, 1498-1507. 

Hoeckendorf, A., Leippe, M. (2012). SPP-3, a saposin-like protein of Caenorhabditis elegans, displays antimicrobial and pore-forming activity and is located in the intestine and in one head neuron.
Dev. Comp. Immunol. 38, 181–186. 

Hoeckendorf, A., Stanisak, M., Leippe, M. (2012). The saposin-like protein SPP-12 is an antimicrobial polypeptide in pharyngeal neurons of Caenorhabditis elegans and participates in defence against a natural bacterial pathogen.
Biochem. J. 445, 205-212. 

Sommer, F., Awazu, S., Anton-Erxleben, F., Jiang, D., Klimovich, A.V., Klimovich, B.V., Samoilovich, M.P., Satou, Y., Krüss, M., Gelhaus, C., Kürn, U., Bosch, T.C., Khalturin, K. (2012). Blood system formation in the urochordate Ciona intestinalis requires the variable receptor vCRL1.
Mol. Biol. Evol. 29, 3081-3093. 

Jung, S., Sönnichsen, F.D., Hung, C.-W., Tholey, A., Boidin-Wichlacz, C., Haeusgen, W., Gelhaus, C., Desel, C., Podschun, R., Waetzig, V., Tasiemski, A., Leippe, M., Grötzinger, J. (2012). The macin family of antimicrobial proteins combines antimicrobial and nerve-repair activities.
J. Biol. Chem. 287, 14246-14258. 

Schlusselhuber, M., Jung, S., Bruhn, O., Goux, D., Leippe, M., Leclercq, R., Laugier, C., Grötzinger, J., Cauchard, J. (2012). In vitro potential of equine DEFA1 and eCATH1 as alternative antimicrobial drugs in rhodococcosis treatment.
Antimicrob. Agents Chemother. 56, 1749-1755. 

Philipp, S., Jakoby, T., Tholey, A., Janssen, O., Leippe, M., Gelhaus, C. (2012). Cationic detergents enable the separation of membrane proteins of Plasmodium falciparum-infected erythrocytes by 2D gel electrophoresis.
Electrophoresis 33, 1120-1128. 




Di Bella, M.A., Fedders, H., De Leo G., Leippe, M. (2011). Localization of antimicrobial peptides in the tunic of Ciona intestinalis (Ascidiacea, Tunicata) and their involvement in local inflammatory-like reactions.
Res. Immunol.1, 70-75. 

Langolf, S., Machon, U., Sicking, W., Schirmeister, T., Büchhold, C., Gelhaus, C., Rosenthal, P.J., Schmuck, C. (2011). Development of antitrypanosomal and antiplasmodial nonpeptidic cysteine protease inhibitors based on N-protected-guanidino-furan and -pyrrole building blocks.
ChemMedChem 6, 1581-1586. 

Jena, P., Mishra, B., Leippe, M., Hasilik, A., Griffiths, G., Sonawane, A. (2011). Membrane-active antimicrobial peptides and human placental lysosomal extracts are highly active against mycobacteria.
Peptides 32, 881-887. 

Schmidt, H., Gelhaus, C., Nebendahl, M., Lettau, M., Lucius, R., Leippe, M., Kabelitz, D., Janssen, O. (2011). Effector granules in human T lymphocytes: the luminal proteome of secretory lysosomes from human T cells.
Cell Commun. Signal. 9, 4. 

Schmidt, H., Gelhaus, C., Nebendahl, M., Lettau, M., Lucius, R., Leippe, M., Kabelitz, D., Janssen, O. (2011). Effector granules in human T lymphocytes: Proteomic evidence for two distinct species of cytotoxic effector vesicles.
J. Proteome Res. 10, 1603–1620. 

Jung, S., Mysliwy, J., Spudy, B., Lorenzen, I., Reiss, K., Gelhaus, C., Podschun, R., Leippe, M., Grötzinger, J. (2011). Human ß-defensin 2 and ß-defensin 3 chimeric peptides reveal the structural basis of the pathogen specificity of their parent molecules.
Antimicrob. Agents Chemother. 55, 954-960. 




Fraune, S., Augustin, R., Anton-Erxleben, F., Wittlieb, J., Gelhaus, C., Klimovich, V.B., Samoilovich, M.P., Bosch, T.C.G. (2010). Embryo protection at the base of animal evolution: Bacterial colonization during embryogenesis is controlled by maternal AMPs. 
Proc. Natl. Acad. Sci. USA 107,18067-18072. 

Schmidt, H., Gelhaus, C., Nebendahl, M., Janssen, O., Petersen, A. (2010). Characterization of Phleum pratense pollen extracts by 2D-DIGE and allergen immunoreactivity.
Proteomics 10, 4352-4362. 

Waag, T., Gelhaus, C., Rath, J., Stich, A., Leippe, M., Schirmeister, T. (2010). Allicin and derivates are cysteine protease inhibitors with antiparasitic activity.
Bioorg. Med. Chem. Lett. 20, 5541-5543. 

Bova, F., Ettari, R., Micale, N., Carnovale, C., Schirmeister, T., Gelhaus, C., Leippe, M., Grasso, S., Zappalà, M. (2010). Constrained peptidomimetics as antiplasmodial falcipain-2 inhibitors.
Bioorg. Med. Chem. 18, 4928-4938. 

Schmidt, H., Krause, S., Gelhaus, C., Petersen, A., Janssen, O., Becker, W.-M. (2010). Detection and structural characterization of natural Ara h 7, the third peanut allergen of the 2S albumin family.
J. Proteome Res. 9, 3701-3709. 

Fedders, H., Podschun, R., Leippe, M. (2010). The antimicrobial peptide Ci-MAM-A24 is highly active against multidrug-resistant and anaerobic bacteria pathogenic for humans.
Int. J. Antimicrob. Agents 36, 264-266. 

Ettari, R., Zappalà, M., Micale, N., Schirmeister, T., Gelhaus, C., Leippe, M., Evers, A., Grasso, S. (2010). Synthesis of novel peptidomimetics as inhibitors of protozoan cysteine proteases falcipain-2 and rhodesain.
Eur. J. Med. Chem. 45, 3228-3233. 

Breuning, A., Degel, B., Schulz, F., Büchold, C., Stempka, M., Machon, U., Heppner, S., Gelhaus, C., Leippe, M., Leyh, M., Kisker, C., Rath, J., Stich, A., Gut, J., Rosenthal, P.J., Schmuck, C., Schirmeister, T. (2010). Michael acceptor based antiplasmodial and antitrypanosomal cysteine protease inhibitors with unusual amino acids.
J. Med. Chem. 53, 1951-1963. 

Lettau, M., Pieper, J., Gerneth, A., Lengl-Janßen, B., Voss, M., Linkermann, A., Schmidt, H., Gelhaus, C., Leippe, M., Kabelitz, D., Janssen, O. (2010). The adapter protein Nck: Role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytes.
Protein Sci. 19, 658-669. 

Mysliwy, J., Dingley, A.J., Stanisak, M., Jung, S., Lorenzen, I., Roeder, T., Leippe, M., Grötzinger, J. (2010). The solution structure of caenopore-5: an antimicrobial protein from Caenorhabditis elegans.
Dev. Comp. Immunol. 34, 323-330. 

Roeder, T., Stanisak, M., Gelhaus, C., Bruchhaus, I., Grötzinger, J., Leippe, M. (2010). Caenopores are antimicrobial peptides in the nematode Caenorhabditis elegans instrumental in nutrition and immunity.
Dev. Comp. Immunol. 34, 203-209. 




Machon, U., Büchold, C., Stempka, M., Schirmeister, T., Gelhaus, C., Leippe, M., Gut, J., Rosenthal, P.J., Kisker, C., Leyh, M., Schmuck, C. (2009). On-bead screening of a combinatorial fumaric acid derived peptide library yields antiplasmodial cysteine protease inhibitors with unusual peptide sequences. 
J. Med. Chem. 52, 5662-5672. 

Micale, N., Ettari, R., Schirmeister, T., Evers, A., Gelhaus, C., Leippe, M., Zappalà, M., Grasso, S. (2009). Novel 2H-isoquinolin-3-ones as antiplasmodial falcipain-2 inhibitors.
Bioorg. Med. Chem. 17, 6505-6511. 

Schmidt, H., Gelhaus, C., Lucius, R., Nebendahl, M., Leippe, M., Janssen, O. (2009). Enrichment and analysis of secretory lysosomes from lymphocyte populations.
BMC Immunology 10:41. 

Xun, Y., Tremouilhac, P., Carraher, C., Gelhaus, C., Ozawa, K., Otting, G., Dixon, N.E., Leippe, M., Grötzinger, J., Dingley, A.J., Kralicek, A.V. (2009). Cell-free synthesis and combinatorial selective 15N-labeling of the cytotoxic protein amoebapore A from Entamoeba histolytica.
Prot. Expr. Purif. 68, 22-27. 

Biller, L., Schmidt, H., Krause, E., Gelhaus, C., Handal, G., Lotter, H., Janssen, O., Tannich, E., Bruchhaus, I. (2009).
Comparison of two genetically related Entamoeba histolytica cell lines derived from the same isolate with different pathogenic properties.
Proteomics 9, 4107-4120. 

Schmidt, H., Gelhaus, C., Latendorf, T., Nebendahl, M., Petersen, A., Krause, S., Leippe, M., Becker, W.-M., Janssen, O. (2009). 2D-DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents.
Proteomics 9, 3507-3521. 

Irmer, H., Tillack, M., Biller, L., Handal, G., Leippe, M., Roeder, T., Tannich, E., Bruchhaus, I. (2009). Major cysteine peptidases of Entamoeba histolytica are required for aggregation and digestion of erythrocytes but are dispensable for phagocytosis and cytopathogenicity. 
Mol. Microbiol. 72, 658-667. 

Harrington, J.M., Chou, H.-T., Gutsmann, T., Gelhaus, C., Stahlberg, H., Leippe, M., Armstrong, P.B. (2009). Membrane activity of a C-reactive protein.
FEBS Lett. 583, 1001-1005. 

Ettari, R., Micale, N., Schirmeister, T., Gelhaus, C., Leippe, M., Nizi, E., Di Francesco, E.M., Grasso, S., Zappalà, M. (2009). Novel peptidomimetics containing a vinyl ester moiety as highly potent and selective falcipain-2 Inhibitors.
J. Med. Chem. 52, 2157-2160. 

Andrä, J., Hammer, M.U., Grötzinger, J., Jakovkin, I., Lindner, B., Vollmer, E., Fedders, H., Leippe, M., Gutsmann, T. (2009). Significance of the cyclic structure and of arginine residues for the antibacterial activity of arenicin-1 and its interaction with phospholipid and lipopolysaccharide model membranes.
Biol. Chem. 390, 337-349. 

Bruhn, O., Cauchard, J., Schlusselhuber, M., Gelhaus, C., Podschun, R., Thaller, G., Laugier, C., Leippe, M., Grötzinger, J. (2009). Antimicrobial properties of the equine alpha-defensin DEFA1 against bacterial horse pathogens.
Vet. Immunol. Immunopathol. 130, 102-106. 

Michalek, M., Gelhaus, C., Hecht, O., Podschun, R., Schröder, J.M., Leippe, M., Grötzinger, J. (2009). The human antimicrobial protein psoriasin acts by permeabilization of bacterial membranes.
Dev. Comp. Immunol. 33, 740-746. 

Regenhard, P., Leippe, M., Schubert, S., Podschun, R., Kalm, E., Grötzinger, J., Looft, C. (2009). Antimicrobial activity of bovine psoriasin.
Vet. Microbiol. 136, 335-340. 

Jung, S., Dingley, A.J., Augustin, R., Anton-Erxleben, F., Stanisak, M., Gelhaus, C., Gutsmann, T., Hammer, M.U., Podschun, R., Bonvin, A.M.J.J., Leippe, M., Bosch, T.C.G., Grötzinger, J. (2009). Hydramacin-1: Structure and antibacterial activity of a protein from the basal metazoan Hydra. 
J. Biol. Chem. 284, 1896-1905. 

Bosch, T.C.G., Augustin, R., Anton-Erxleben, F., Fraune, S., Hemmrich, G., Zill, H., Rosenstiel, P., Jacobs, G., Schreiber, S., Leippe, M., Stanisak, M., Grötzinger, J., Jung, S., Podschun, R., Bartels, J., Harder, J., Schröder, J.M. (2009). Uncovering the evolutionary history of innate immunity: the simple metazoan Hydra uses epithelial cells for host defense.
Dev. Comp. Immunol. 33, 559-569. 

Linkermann, A., Gelhaus, C., Lettau, M., Qian, J., Kabelitz, D., Janssen, O. (2009). Identification of interaction partners for individual SH3 domains of Fas ligand associated members of the PCH protein family in T lymphocytes.
Biochim. Biophys. Acta - Proteins and Proteomics 1794, 168-176. 




Dude, M.-A., Kaeppler, U., Herb, M., Schiller, M., Schulz, F., Vedder, B., Heppner, S., Pradel, G., Gut, J., Rosenthal, P.J., Schirmeister, T., Leippe, M., Gelhaus, C. (2008). Synthesis and evaluation of non-peptidic cysteine protease inhibitors of P. falciparum derived from etacrynic acid.
Molecules 14, 19-35. 

Evers, A., Heppner, S., Leippe, M., Gelhaus, C. (2008). An efficient fluorimetric method to measure the viability of intraerythrocytic Plasmodium falciparum.
Biol. Chem. 389, 1523-1525. 

Schikorski, D., Cuvillier-Hot, V., Leippe, M., Boidin-Wichlacz, C., Slomianny, C., Macagno, E., Salzet, M., Tasiemski, A. (2008). Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia. 
J. Immunol. 181, 1083-1095. 

Fedders, H., Michalek, M., Grötzinger, J., Leippe, M. (2008). An exceptional salt tolerant antimicrobial peptide derived from a novel gene family of haemocytes of the marine invertebrate Ciona intestinalis.
Biochem. J. 416, 65-75. 

Schmidt, H., Gelhaus, C., Nebendahl, M., Lettau, M., Watzl, C., Kabelitz, D., Leippe, M., Janssen, O. (2008). 2D-DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells.
Proteomics 8, 2911-2925.

Harrington, J.M., Chou, H.T., Gutsmann, T., Gelhaus, C., Stahlberg, H., Leippe, M., Armstrong, P.B. (2008). Membrane pore formation by pentraxin proteins from Limulus, the American horseshoe crab.
Biochem. J. 413, 305-313. 

Gelhaus, C., Jacobs, T., Andrä, J., Leippe, M. (2008). The antimicrobial peptide NK-2, the core region of mammalian NK-lysin, kills intraerythrocytic Plasmodium falciparum.
Antimicrob. Agents Chemother. 52, 1713-1720. 

Harrington, J.M., Leippe, M., Armstrong, P.B. (2008). Epithelial immunity in a marine invertebrate: a cytolytic activity from a cuticular secretion of the American horseshoe crab, Limulus polyphemus.
Mar. Biol. 153, 1165-1171. 

Fedders, H., Leippe, M. (2008). A reverse search for antimicrobial peptides in Ciona intestinalis: Identification of a gene family expressed in hemocytes and evaluation of activity.
Dev. Comp. Immunol. 32, 286-298. 

Andrä, J., Jakovkin, I., Grötzinger, J., Hecht, O., Krasnosdembskaya, A.D., Goldmann, T., Gutsmann, T., Leippe, M. (2008). Structure and mode of action of the antimicrobial peptide arenicin.
Biochem. J. 410, 113-122. 




Bringmann, G., Gampe, C., Reichert, Y., Bruhn, T., Faber, J., Mikyna, M., Reichert, M., Leippe, M., Brun, R., Gelhaus, C. (2007). Synthesis and pharmacological evaluation of fluorescent and photoactivateable analogs of antiplasmodial naphthylisoquinolines. 
J. Med. Chem. 50, 6104-6115. 

Bruhn, O., Regenhard, P., Michalek, M., Paul, S., Gelhaus, C., Jung, S., Thaller, G., Podschun, R., Leippe, M., Grötzinger, J., Kalm, E. (2007). A novel alpha-defensin of the horse: gene transcription, recombinant expression and characterisation of the structure and function.
Biochem. J. 407, 267-276. 

Clark, C.G., Alsmark, U.C.M., Tazreiter, M., Saito-Nakano, Y, Ali, V., Marion, S., Weber, C., Mukherjee, C., Bruchhaus, I., Tannich, E., Leippe, M., Sicheritz-Ponten, T., Foster, P.G., Samuelson, J., Noël, C.J., Hirt, R.P., Embley, T.M., Gilchrist, C.A., Mann, B.J., Singh, U., Ackers, J.P., Bhattacharya, S., Bhattacharya, A., Lohia, A., Guillén, N., Duchêne, M., Nozaki, T., and Hall, N. (2007). Structure and content of the Entamoeba histolytica genome.
Advances in Parasitology 65, 51-190 (Review). 

Schulz, F., Gelhaus, C., Degel, B., Vicik, R., Heppner, S., Breuning, A., Leippe, M., Gut, J., Rosenthal, P.J., Schirmeister, T. (2007). Screening of protease inhibitors as antiplasmodial agents. Part I: aziridines and epoxides.
ChemMedChem 2, 1214-1224. 

Wehling, C., Beimgraben, C., Gelhaus, C., Friedrich, T., Saftig, P., Grötzinger, J., Schwake, M. (2007). Self-assembly of the isolated KCNQ2 subunit interaction domain.
FEBS Lett. 581, 1594-1598. 




Vicik, R., Busemann, M., Gelhaus, C., Stiefl, N., Scheiber, J., Schmitz, W., Schulz, F., Mladenovic, M., Engels, B., Leippe, M., Baumann, K., Schirmeister, T. (2006). Aziridine based inhibitors of cathepsin L - synthesis, inhibition activity and docking studies.
ChemMedChem 1, 1126-1141. 

Winkelmann, J., Leippe, M. and Bruhn, H. (2006). A novel saposin-like protein of Entamoeba histolytica with membrane-fusogenic activity.
Mol. Biochem. Parasitol. 147, 85-94. 

Bruhn, H., Winkelmann, J., Andersen, C., Andrä, J. and Leippe, M. (2006). Dissection of the mechanisms of cytolytic and antibacterial activity of lysenin, a defence protein of the annelid Eisenia fetida.
Dev. Comp. Immunol. 30, 597-606. 




Kolter, T., Winau, F., Schaible, U.E., Leippe, M., Sandhoff, K. (2005). Lipid-binding proteins in membrane digestion, antigen presentation, and antimicrobial defense.
J. Biol. Chem. 280, 41125-41128.

Gelhaus, C., Vicik, R., Schirmeister, T., Leippe, M. (2005). Blocking effect of a biotinylated protease inhibitor on the egress of Plasmodium falciparum merozoites from infected red blood cells.
Biol. Chem. 386, 499-502. 

Gelhaus, C., Fritsch, J., Krause, E., Leippe, M. (2005). Fractionation and identification of proteins by two-dimensional electrophoresis and mass spectrometry: towards proteome analysis of Plasmodium falciparum.
Proteomics 5, 4213-4222. 

Bruhn, H., Jacobs, T., Urban, B., Leippe, M. (2005). An exceptionally short alpha-actinin-like protein from the protozoan parasite Entamoeba histolytica
J. Biol. Sci. 5, 76-81.

Loftus, B., Anderson, I., Davies, R., Alsmark, U.C., Samuelson, J., Amedeo, P., Roncaglia, P., Berriman, M., Hirt, R.P., Mann, B.J., Nozaki, T., Suh, B., Pop, M., Duchene, M., Ackers, J., Tannich, E., Leippe, M., Hofer, M., Bruchhaus, I., Willhoeft, U., Bhattacharya, A., Chillingworth, T., Churcher, C., Hance, Z., Harris, B., Harris, D., Jagels, K., Moule, S., Mungall, K., Ormond, D., Squares, R., Whitehead, S., Quail, M.A., Rabbinowitsch, E., Norbertczak, H., Price, C., Wang, Z., Guillen, N., Gilchrist, C., Stroup, S.E., Bhattacharya, S., Lohia, A., Foster, P.G., Sicheritz-Ponten, T., Weber, C., Singh, U., Mukherjee, C., El-Sayed, N.M., Petri, W.A. Jr, Clark, C.G., Embley, T.M., Barrell, B., Fraser, C.M., Hall, N. (2005). The genome of the protist parasite Entamoeba histolytica
Nature 433, 865-868. 

Müller, I., Subert, N., Otto, H., Herbst, R., Rühling, H., Maniak, M., Leippe, M. (2005). A Dictyostelium mutant with reduced lysozyme levels compensates by increased phagocytic activity. 
J. Biol. Chem. 280, 10435-10443.

Leippe, M., Bruhn, H., Hecht, O., Grötzinger, J. (2005). Ancient weapons: the three-dimensional structure of amoebapore A. 
Trends Parasitol. 21, 5-7. 




Riekenberg, S., Flockenhaus, B., Vahrmann, A., Müller M.C.M., Leippe, M., Kieß, M., Scholze, H. (2004). The beta-N-acetylhexosaminidase of Entamoeba histolytica is composed of two homologous chains and has been localized to cytoplasmic granules. 
Mol. Biochem. Parasitol. 138, 217-225. 

Saito-Nakano, Y., Yasuda, T., Nakada-Tsukui, K., Leippe, M., Nozaki, T. (2004). Rab5-associated vacuoles play a unique role in phagocytosis of the enteric protozoan parasite Entamoeba histolytica
J. Biol. Chem. 279, 49497-49507.

Leippe, M., Herbst, R (2004). Ancient weapons for attack and defense: The pore-forming polypeptides of pathogenic enteric and free-living amoeboid protozoa. 
J. Euk. Microbiol. 51, 516-521 (Review). 

Herbst, R., Marciano-Cabral, F., Leippe, M. (2004). Antimicrobial and pore-forming peptides of free-living and potentially highly pathogenic Naegleria fowleri are released from the same precursor molecule. 
J. Biol. Chem. 279, 25955- 25958. 

Dominguez-Bello, M.G., Pacheco, A., Ruiz, M.C., Michelangeli, F., Leippe, M., De Pedro, M. A. (2004). Resistance of rumen bacteria murein to bovine gastric lysozyme.
BMC Ecol. 4, 1-6. 

Gelhaus, C., Vicik, R., Hilgenfeld,R., Schmidt, C.L., Leippe, M., Schirmeister, T. (2004). Synthesis and antiplasmodial activity of a cysteine-protease inhibiting biotinylated aziridine-2,3-dicarboxylate. 
Biol. Chem. 385, 435-438. 

Andrä, J., Berninghausen, O., Leippe, M. (2004). Membrane lipid composition protects Entamoeba histolytica from self-destruction by its pore-forming toxins. 
FEBS Lett. 564, 109-115. 

Hecht, O., van Nuland, N., Schleinkofer, K., Dingley, A.J., Bruhn, H., Leippe, M., Grötzinger, J. (2004). Solution structure of the pore-forming protein of Entamoeba histolytica
J. Biol. Chem. 279, 17834-17841. 




Bruhn, H., Riekens, B., Berninghausen, O., Leippe, M. (2003). Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals - a comparative functional analysis. 
Biochem. J. 375, 737-744. 

Gutsmann, T., Riekens, B., Bruhn, H., Wiese, A., Seydel, U., Leippe, M. (2003). Interaction of amoebapores and NK-lysin with symmetric phospholipid and asymmetric lipopolysaccharide/phospholipid bilayers. 
Biochemistry 42, 9804-9812. 

Bente, M., Harder, S., Wiesgigl, M., Heukeshoven, J., Gelhaus, C., Krause, E., Clos, J., Bruchhaus, I. (2003). Developmentally induced changes of the proteome in the protozoan parasite Leishmania donovani
Proteomics 3, 1811-1829. 

Jacobs, T., Bruhn, H., Gaworski, I., Fleischer, B., Leippe, M. (2003) NK-lysin and its shortened analog NK-2 exhibit potent activity against Trypanosoma cruzi.
Antimicrob. Agents Chemother., 47, 607-613. 

Andrä, J., Herbst, R., Leippe, M. (2003). Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes.
Dev. Comp. Immunol. 27, 291-304. 

Steinert, M., Leippe, M., Röder, T. (2003). Surrogate hosts: protozoa and invertebrates as models for studying pathogen-host interactions. 
Int. J. Med. Microbiol. 293, 321-332 (Review). 


before 2003


Gao, T., Ehrenman, K., Tang, L., Leippe, M., Brock, D. A., Gomer, R.H. (2002). Cells respond to and bind countin, a component of a multisubunit cell-number counting factor. 
J. Biol. Chem. 277, 32596-32605. 

Herbst, R., Ott, C., Jacobs, T., Marti, T., Marciano-Cabral, F., Leippe, M. (2002). Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri.
J. Biol. Chem. 277, 22353-22360. 

Hellberg, A., Nowak, N., Leippe, M., Tannich, E., Bruchhaus, I. (2002). Recombinant expression and purification of an enzymatically active cysteine proteinase of the protozoan parasite Entamoeba histolytica.
Protein Expres. Purif. 24, 131-137. 

Bruhn, H., Leippe, M. (2001). Novel putative saposin-like proteins of Entamoeba histolytica different from amoebapores. 
Biochim. Biophys. Acta (Biomembranes) 1514, 14-20. 

Bruhn, H., Leippe, M. (2001). Membrane-permeabilizing polypeptides of amoebae – constituents of an archaic antimicrobial system.
Zoology 104, 3-11 (Review). 

Andrä J., Berninghausen, O., Leippe, M. (2001). Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans
Med. Microbiol. Immunol. 189, 169-173. 

Ebert, F., Guillén, N., Leippe, M., Tannich, E. (2000). Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins. 
Mol. Biochem. Parasitol. 111, 459-464. 

Ernst, W.A., Thoma-Uszynski, S., Teitelbaum, R., Ko, C., Hanson, D.A., Clayberger, C., Krensky, A.M., Leippe, M., Bloom, B.R., Ganz, T., Modlin, R.L. (2000). Granulysin, a T cell product, kills bacteria by altering membrane permeability. 
J. Immunol. 165, 7102-7108. 

Nickel, R., Jacobs, T., Urban, B., Scholze, H., Bruhn, H., Leippe, M. (2000). Two novel calcium-binding proteins from cytoplasmic granules of the protozoan parasite Entamoeba histolytica
FEBS Lett. 486, 112-116. 

Nickel, R., Stern, R., Leippe, M. (2000). Evidence that hyaluronidase is not involved in tissue invasion of the protozoan parasite Entamoeba histolytica
Infect. Immun. 68, 3053-3055. 

Hellberg, A., Leippe, M., Bruchhaus, I. (2000). Two major `higher molecular mass proteinases´of Entamoeba histolytica are identified as cysteine proteinases 1 and 2.
Mol. Biochem. Parasitol. 105, 305-309. 

Andrä, J., Leippe, M. (1999). Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin. 
Med. Microbiol. Immunol. 188, 117-124. 

Bracha, R., Nuchamowitz, Y., Leippe, M., Mirelman, D. (1999). Antisense inhibition of amoebapore expression in Entamoeba histolytica causes decrease in amoebic virulence. 
Mol. Microbiol. 34, 463-472. 

Leippe, M. (1999). Amöben durchlöchern Zellmembranen. 
BIOspectrum 5, 383-385 (Review).

Leippe, M. (1999). Antimicrobial and cytolytic polypeptides of amoeboid protozoa--effector molecules of primitive phagocytes.
Dev. Comp. Immunol. 23(4-5), 267-279 (Review). 

Nickel, R., Ott, C., Dandekar, T., Leippe, M. (1999). Pore-forming peptides of Entamoeba dispar: similarity and divergence to amoebapores in structure, expression and activity. 
Eur. J. Biochem. 265, 1002-1007. 

Bruhn, H., Leippe, M. (1999). Comparative modeling of amoebapores and granulysin based on the NK-lysin structure – structural and functional implications. 
Biol. Chem. 380, 1001-1007. 

Nickel, R., Jacobs, T., Leippe, M. (1998). Molecular characterization of an exceptionally acidic lysozyme-like protein from the protozoon Entamoeba histolytica.
FEBS Lett. 437, 153-157. 

Jacobs, T., Bruchhaus, I., Dandekar, T., Tannich, E., Leippe, M. (1998). Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
Mol. Microbiol. 27, 269-276. 

Berninghausen, O., Leippe, M. (1997). Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica
Infect. Immun. 65, 3615-3621. 

Dandekar, T., Leippe, M. (1997). Molecular modeling of amoebapore and NK-lysin: A four-a-helix bundle motif of cytolytic effector molecules from distantly related organisms.
Folding and Design 2, 47-52. 

Berninghausen, O., Leippe, M. (1997). Calcium-independent cytolysis of target cells induced by Entamoeba histolytica.
Arch. Med. Res. 28, 158-160. 

Benkert, C., Jacobs, T., Berninghausen, O., Andrä, J., Leippe, M. (1997). Molecular basis of aggressive and defensive functions of Entamoeba histolytica.
Arch. Med. Res. 28, 152-153 (Review). 

Leippe, M. (1997). Amoebapores. 
Trends Parasitol. (formerly Parasitol. Today) 13, 178-183 (Review). 

Bruchhaus, I., Jacobs, T., Leippe, M., Tannich, E. (1996). Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes. 
Mol. Microbiol. 22, 255-263. 

Andrä, J., Berninghausen, O., Wülfken, J., Leippe, M. (1996). Shortened amoebapore analogs with enhanced antibacterial and cytolytic activity.
FEBS Lett. 385, 96-100. 

Leippe, M. (1995). Ancient weapons: NK-lysin is a mammalian homolog to pore-forming peptides of a protozoan parasite.
Cell 83, 17-18. 

Jacobs, T., Leippe, M. (1995). Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties.
Eur. J. Biochem. 231, 831-838. 

Leippe, M., Sievertsen, H. J., Tannich, E., Horstmann, R.D. (1995). Spontaneous release of cysteine proteinases but not of pore-forming peptides by viable Entamoeba histolytica
Parasitology 111, 569-574. 

Andrä, J., Leippe, M. (1994) Pore-forming peptide of Entamoeba histolytica: Significance of positively charged amino acid residues for its mode of action. 
FEBS Lett. 354, 97-102. 

Leippe, M., Andrä, J., Nickel, R., Tannich, E., Müller-Eberhard, H.J. (1994) Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeba histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. 
Mol. Microbiol. 14, 895-904. 

Leippe, M., Andrä, J., Müller-Eberhard, H.J. (1994) Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.
Proc. Natl. Acad. Sci. USA 91, 2602-2606. 

Leippe, M., Müller-Eberhard, H.J. (1994) The pore-forming peptide of Entamoeba histolytica, the protozoan parasite causing human amoebiasis. 
Toxicology 87 (Special Issue: "Pore-forming toxins"), 5-18 (Review). 

Bruchhaus, I., Leippe, M., Lioutas, C., Tannich, E. (1993) Unusual gene organization of Entamoeba histolytica
DNA Cell Biol. 12, 925-933. 

Leippe, M., Bahr, E., Tannich, E., Horstmann, R.D. (1993) Comparison of pore-forming peptides from pathogenic and nonpathogenic Entamoeba histolytica
Mol. Biochem. Parasitol. 59, 101-110. 

Leippe, M. (1992) Membrane perforation by Entamoeba histolytica: Structural implications derived from the sequence of the pore-forming peptide. 
Arch. Med. Res. 23, 35-37. 

Leippe, M., Tannich, E., Nickel, R., van der Goot, G., Pattus, F., Horstmann, R.D., Müller-Eberhard, H.J. (1992) Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
EMBO J. 11, 3501-3506. 

Horstmann, R.D., Sievertsen, H.J., Leippe, M., Fichetti, V.A. (1992) Role of fibrinogen in complement inhibition by streptococcal M protein.
Infect. Immun. 60, 5036-5041.

Horstmann, R.D., Leippe, M., Tannich, E. (1992) Recent progress in the molecular biology of Entamoeba histolytica
Trop. Med. Parasitol. 43, 213-218 (Review). 

Tannich, E., Leippe, M., Horstmann, R.D. (1992) Aktuelle Befunde zur Pathogenität von Entamoeba histolytica
Immunität und Infektion 5, 146-150 (Review).

Horstmann, R.D., Leippe, M., Tannich, E. (1992) Host tissue destruction by Entamoeba histolytica: Molecules mediating adhesion, cytolysis, and proteolysis. 
Mem. Inst. Oswaldo Cruz 87, Suppl. V, 57-60 (Review). 

Leippe, M., Ebel, S., Schoenberger, O.L., Horstmann, R.D., Müller-Eberhard, H.J. (1991) Pore-forming peptide of pathogenic Entamoeba histolytica.
Proc. Natl. Acad. Sci. USA 88, 7659-7663. 

Timmann, C., Leippe, M., and Horstmann, R.D. (1991) Two major serum components antigenically related to complement factor H are different glycosylation forms of a single protein with no factor H-like complement regulatory functions.
J. Immunol. 146, 1265-1270. 

Leippe, M., Renwrantz, L. (1988) Release of cytotoxic and agglutinating molecules by Mytilus hemocytes. 
Dev. Comp. Immunol. 12, 297-308. 

Leippe, M., Renwrantz, L. (1985) On the capability of bivalve and gastropod hemocytes to secrete cytotoxic molecules.
J. Invertebr. Pathol. 46, 209-210.