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Head of Department Prof. Dr. Matthias Leippe - Secretary - Heidrun Wegner
Zoologisches
Institut,
Zoologisches
Institut,
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page updated on 27/04/12 Höckendorf,
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. 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. 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. 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. 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.
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. 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. 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.
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. Schmidt,
H., Gelhaus, C., Nebendahl, M., Janssen, O., Petersen, A. (2010). Characterization
of Phleum pratense pollen extracts by 2D-DIGE and allergen immunoreactivity. 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. 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. 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. 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. 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. 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. 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. 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. 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. Schmidt,
H., Gelhaus, C., Lucius, R., Nebendahl, M., Leippe, M., Janssen, O. (2009).
Enrichment and analysis of secretory lysosomes from lymphocyte populations. 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. 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. 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. 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. 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. 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. 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. 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. 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. Regenhard,
P., Leippe, M., Schubert, S., Podschun, R., Kalm, E., Grötzinger,
J., Looft, C. (2009). Antimicrobial activity of bovine psoriasin. 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.
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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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.
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. 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. 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. 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. Wehling,
C., Beimgraben, C., Gelhaus, C., Friedrich, T., Saftig, P., Grötzinger,
J., Schwake, M. (2007). Self-assembly of the isolated KCNQ2 subunit
interaction domain.
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. Winkelmann,
J., Leippe, M. and Bruhn, H. (2006). A novel saposin-like protein of
Entamoeba histolytica with membrane-fusogenic activity. 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.
Kolter,
T., Winau, F., Schaible, U.E., Leippe, M., Sandhoff, K. (2005). Lipid-binding
proteins in membrane digestion, antigen presentation, and antimicrobial
defense. 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. 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. Bruhn,
H., Jacobs, T., Urban, B., Leippe, M. (2005). An exceptionally short alpha-actinin-like
protein from the protozoan parasite Entamoeba histolytica. 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. 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. Leippe,
M., Bruhn, H., Hecht, O., Grötzinger, J. (2005). Ancient weapons:
the three-dimensional structure of amoebapore A.
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. 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. Leippe,
M., Herbst, R (2004). Ancient weapons for attack and defense: The pore-forming
polypeptides of pathogenic enteric and free-living amoeboid protozoa.
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. 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. 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. Andrä,
J., Berninghausen, O., Leippe, M. (2004). Membrane lipid composition protects
Entamoeba histolytica from self-destruction by its pore-forming
toxins. 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.
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. 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. 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. 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. 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. Steinert,
M., Leippe, M., Röder, T. (2003). Surrogate hosts: protozoa and invertebrates
as models for studying pathogen-host interactions.
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. Herbst,
R., Ott, C., Jacobs, T., Marti, T., Marciano-Cabral, F., Leippe, M. (2002).
Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. 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. Bruhn,
H., Leippe, M. (2001). Novel putative saposin-like proteins of Entamoeba
histolytica different from amoebapores. Bruhn,
H., Leippe, M. (2001). Membrane-permeabilizing polypeptides of amoebae
– constituents of an archaic antimicrobial system. Andrä
J., Berninghausen, O., Leippe, M. (2001). Cecropins, antibacterial peptides
from insects and mammals, are potently fungicidal against Candida
albicans. 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. 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.
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. Nickel,
R., Stern, R., Leippe, M. (2000). Evidence that hyaluronidase is not involved
in tissue invasion of the protozoan parasite Entamoeba histolytica.
Hellberg,
A., Leippe, M., Bruchhaus, I. (2000). Two major `higher molecular mass
proteinases´of Entamoeba histolytica are identified as
cysteine proteinases 1 and 2. Andrä,
J., Leippe, M. (1999). Candidacidal activity of shortened synthetic analogs
of amoebapores and NK-lysin. Bracha,
R., Nuchamowitz, Y., Leippe, M., Mirelman, D. (1999). Antisense inhibition
of amoebapore expression in Entamoeba histolytica causes decrease
in amoebic virulence. Leippe,
M. (1999). Amöben durchlöchern Zellmembranen. Leippe,
M. (1999). Antimicrobial and cytolytic polypeptides of amoeboid protozoa--effector
molecules of primitive phagocytes. 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. Bruhn,
H., Leippe, M. (1999). Comparative modeling of amoebapores and granulysin
based on the NK-lysin structure – structural and functional implications.
Nickel,
R., Jacobs, T., Leippe, M. (1998). Molecular characterization of an exceptionally
acidic lysozyme-like protein from the protozoon Entamoeba histolytica. Jacobs,
T., Bruchhaus, I., Dandekar, T., Tannich, E., Leippe, M. (1998). Isolation
and molecular characterization of a surface-bound proteinase of Entamoeba
histolytica. Berninghausen,
O., Leippe, M. (1997). Necrosis versus apoptosis as the mechanism of target
cell death induced by Entamoeba histolytica. 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. Berninghausen,
O., Leippe, M. (1997). Calcium-independent cytolysis of target cells induced
by Entamoeba histolytica. Benkert,
C., Jacobs, T., Berninghausen, O., Andrä, J., Leippe, M. (1997).
Molecular basis of aggressive and defensive functions of Entamoeba
histolytica. Leippe,
M. (1997). Amoebapores. Bruchhaus,
I., Jacobs, T., Leippe, M., Tannich, E. (1996). Entamoeba histolytica
and Entamoeba dispar: differences in numbers and expression of
cysteine proteinase genes. Andrä,
J., Berninghausen, O., Wülfken, J., Leippe, M. (1996). Shortened
amoebapore analogs with enhanced antibacterial and cytolytic activity. Leippe,
M. (1995). Ancient weapons: NK-lysin is a mammalian homolog to pore-forming
peptides of a protozoan parasite. Jacobs,
T., Leippe, M. (1995). Purification and molecular cloning of a major antibacterial
protein of the protozoan parasite Entamoeba histolytica with
lysozyme-like properties. 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. Andrä,
J., Leippe, M. (1994) Pore-forming peptide of Entamoeba histolytica:
Significance of positively charged amino acid residues for its mode of
action. 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. 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. Leippe,
M., Müller-Eberhard, H.J. (1994) The pore-forming peptide of Entamoeba
histolytica, the protozoan parasite causing human amoebiasis. Bruchhaus,
I., Leippe, M., Lioutas, C., Tannich, E. (1993) Unusual gene organization
of Entamoeba histolytica. Leippe,
M., Bahr, E., Tannich, E., Horstmann, R.D. (1993) Comparison of pore-forming
peptides from pathogenic and nonpathogenic Entamoeba histolytica.
Leippe,
M. (1992) Membrane perforation by Entamoeba histolytica: Structural implications
derived from the sequence of the pore-forming peptide. 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. Horstmann,
R.D., Sievertsen, H.J., Leippe, M., Fichetti, V.A. (1992) Role of fibrinogen
in complement inhibition by streptococcal M protein. Horstmann,
R.D., Leippe, M., Tannich, E. (1992) Recent progress in the molecular
biology of Entamoeba histolytica. Tannich,
E., Leippe, M., Horstmann, R.D. (1992) Aktuelle Befunde zur Pathogenität
von Entamoeba histolytica. Horstmann,
R.D., Leippe, M., Tannich, E. (1992) Host tissue destruction by Entamoeba
histolytica: Molecules mediating adhesion, cytolysis, and proteolysis.
Leippe,
M., Ebel, S., Schoenberger, O.L., Horstmann, R.D., Müller-Eberhard,
H.J. (1991) Pore-forming peptide of pathogenic Entamoeba histolytica. 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. Leippe,
M., Renwrantz, L. (1985) On the capability of bivalve and gastropod hemocytes
to secrete cytotoxic molecules.
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