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Results: 6
Number of items: 6
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van der Kraan, M. I. A., Nazmi, K., van 't Hof, W., van Nieuw Amerongen, A., Veerman, E. C. I., & Bolscher, J. G. M. (2006). Distinct bactericidal activities of bovine lactoferrin peptides LF-ampin 268-284 and LF-ampin 265-284: Asp-Leu-Ile sequence makes the difference. Biochemistry and Cell Biology, 84, 358-362. https://doi.org/10.1139/O06-042
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Bolscher, J. G. M., van der Kraan, M. I. A., Nazmi, K., Kalay, H., Grün, C. H., Groenink, J., van 't Hof, W., Veerman, E. C. I., & van Nieuw Amerongen, A. (2006). A one-enzyme strategy to release an antimicrobial peptide from the LFampin-domain of bovine lactoferrin. Peptides, 27, 1-9. https://doi.org/10.1016/j.peptides.2005.06.012
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van der Kraan, M. I. A., Nazmi, K., Teeken, A., Groenink, J., van 't Hof, W., Veerman, E. C. I., Bolscher, J. G. M., & van Nieuw Amerongen, A. (2005). Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix facilitating N-terminal part. Biological chemistry, 386, 137-142. https://doi.org/10.1515/BC.2005.017
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van der Kraan, M. I. A., van Marle, J., Nazmi, K., Groenink, J., van 't Hof, W., Veerman, E. C. I., Bolscher, J. G. M., & van Nieuw Amerongen, A. (2005). Ultrastructural effects of antimicrobial peptides from bovine lactoferrin on the membranes of Candida albicans and Escherichia coli. A confocal and freeze-fracture electron microscopy study. Peptides, 26, 1537-1542. https://doi.org/10.1016/j.peptides.2005.02.011
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van der Kraan, M. I. A., Groenink, J., Nazmi, K., Veerman, E. C. I., Bolscher, J. G. M., & van Nieuw Amerongen, A. (2004). Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin. Peptides, 25, 177-183. https://doi.org/10.1016/j.peptides.2003.12.006
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