Proteomic profiling of secretory granules of different T cell subpopulations (2009)
Schmidt, H, Gelhaus, C, Nebendahl, M, Leippe, M, Janssen, O
No abstract available.
Identification of interaction partners of the adapter protein Nck in T cells (2009)
Pieper, J, Lengl-Janßen, B, Voss, M, Gelhaus, C, Leippe, M, Janssen, O, ...
No abstract available.
Leippe, M., Tannich, E., Nickel, R., Pattus, F., Horstmann, R. D., ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...
Leippe, M, Andrä, J, Müller-Eberhard, H J
The pore-forming peptide amoebapore is considered part of the cytolytic armament of pathogenic Entamoeba histolytica. Amoebapore is composed of 77 amino acid residues arranged in four alpha-helical...
Pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Ebel, S, Schoenberger, O L, Horstmann, R D, Müller-Eberhard, H J
A polypeptide that causes pore formation in target-cell membranes is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Pore-forming material was purified to apparent...
Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica.
The human pathogen Entamoeba histolytica is known to kill a variety of host cells, including leukocytes. Using human myeloid cells as targets, we studied whether cytotoxicity of amoebic trophozoites...
Role of fibrinogen in complement inhibition by streptococcal M protein.
Horstmann, R D, Sievertsen, H J, Leippe, M, Fischetti, V A
M protein, the major virulence factor of group A streptococci, has antiopsonic activity in that it inhibits activation of the alternative complement pathway on the streptococcal surface. Two...
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Tannich, E, Nickel, R, Pattus, F, Horstmann, R D, ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...
Leippe, M, Andrä, J, Müller-Eberhard, H J
The pore-forming peptide amoebapore is considered part of the cytolytic armament of pathogenic Entamoeba histolytica. Amoebapore is composed of 77 amino acid residues arranged in four alpha-helical...
Pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Ebel, S, Schoenberger, O L, Horstmann, R D, Müller-Eberhard, H J
A polypeptide that causes pore formation in target-cell membranes is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Pore-forming material was purified to apparent...
Necrosis versus apoptosis as the mechanism of target cell death induced by Entamoeba histolytica.
The human pathogen Entamoeba histolytica is known to kill a variety of host cells, including leukocytes. Using human myeloid cells as targets, we studied whether cytotoxicity of amoebic trophozoites...
Role of fibrinogen in complement inhibition by streptococcal M protein.
Horstmann, R D, Sievertsen, H J, Leippe, M, Fischetti, V A
M protein, the major virulence factor of group A streptococci, has antiopsonic activity in that it inhibits activation of the alternative complement pathway on the streptococcal surface. Two...
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Tannich, E, Nickel, R, Pattus, F, Horstmann, R D, ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...