Andrä J - Search Results

1

The antimicrobial peptide NK-2, the core region of mammalian NK-lysin, kills intraerythrocytic Plasmodium falciparum.

Gelhaus C, Jacobs T, Andrä J, Leippe M. Gelhaus C, et al. Among authors: andra j. Antimicrob Agents Chemother. 2008 May;52(5):1713-20. doi: 10.1128/AAC.01342-07. Epub 2008 Mar 10. Antimicrob Agents Chemother. 2008. PMID: 18332165 Free PMC article.

2

Pore-forming peptide of Entamoeba histolytica. Significance of positively charged amino acid residues for its mode of action.

Andrä J, Leippe M. Andrä J, et al. FEBS Lett. 1994 Oct 31;354(1):97-102. doi: 10.1016/0014-5793(94)01103-6. FEBS Lett. 1994. PMID: 7525351 Free article.

3

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, Nickel R, Tannich E, Müller-Eberhard HJ. Leippe M, et al. Among authors: andra j. Mol Microbiol. 1994 Dec;14(5):895-904. doi: 10.1111/j.1365-2958.1994.tb01325.x. Mol Microbiol. 1994. PMID: 7715451

4

Cytolytic and antibacterial activity of synthetic peptides derived from amoebapore, the pore-forming peptide of Entamoeba histolytica.

Leippe M, Andrä J, Müller-Eberhard HJ. Leippe M, et al. Among authors: andra j. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2602-6. doi: 10.1073/pnas.91.7.2602. Proc Natl Acad Sci U S A. 1994. PMID: 8146160 Free PMC article.

5

Shortened amoebapore analogs with enhanced antibacterial and cytolytic activity.

Andrä J, Berninghausen O, Wülfken J, Leippe M. Andrä J, et al. FEBS Lett. 1996 Apr 29;385(1-2):96-100. doi: 10.1016/0014-5793(96)00359-6. FEBS Lett. 1996. PMID: 8641476 Free article.

6

Molecular basis of aggressive and defensive functions of Entamoeba histolytica.

Benkert C, Jacobs T, Berninghausen O, Andrä J, Leippe M. Benkert C, et al. Among authors: andra j. Arch Med Res. 1997;28 Spec No:152-3. Arch Med Res. 1997. PMID: 9033050 No abstract available.

7

Potency of amoebapores compared to that of other membrane-permeating peptides.

Andrä J, Berninghausen O, Leippe M. Andrä J, et al. Arch Med Res. 1997;28 Spec No:156-7. Arch Med Res. 1997. PMID: 9033052 No abstract available.

8

Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin.

Andrä J, Leippe M. Andrä J, et al. Med Microbiol Immunol. 1999 Dec;188(3):117-24. doi: 10.1007/s004300050113. Med Microbiol Immunol. 1999. PMID: 10776841

9

Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans.

Andrä J, Berninghausen O, Leippe M. Andrä J, et al. Med Microbiol Immunol. 2001 Apr;189(3):169-73. doi: 10.1007/s430-001-8025-x. Med Microbiol Immunol. 2001. PMID: 11388616

10

Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes.

Andrä J, Herbst R, Leippe M. Andrä J, et al. Dev Comp Immunol. 2003 Apr;27(4):291-304. doi: 10.1016/s0145-305x(02)00106-4. Dev Comp Immunol. 2003. PMID: 12590963

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