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Addlagatta, A., Gay, L. and Matthews, B. W. 2006. Structure of aminopeptidase N from Escherichia coli<\/i> suggests a compartmentalized, gated active site. Proc. Natl. Acad. Sci. U.S.A.<\/i> 103: 13339\u201313344."},{"key":"2","doi-asserted-by":"crossref","unstructured":"2. Albiston, A. L., Ye, S. and Chai, S. Y. 2004. Membrane bound members of the M1 family: more than aminopeptidases. Protein Pept. Lett.<\/i> 11: 491\u2013500.","DOI":"10.2174\/0929866043406643"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3. Arfin, S. M., Kendall, R. L., Hall, L., Weaver, L. H., Stewart, A. E., Matthews, B. W. and Bradshaw, R. A. 1995. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. U.S.A.<\/i> 92: 7714\u20137718.","DOI":"10.1073\/pnas.92.17.7714"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4. Azimzadeh, O., Sow, C., G\u00e8ze, M., Nyalwidhe, J. and Florent, I. 2010. Plasmodium falciparum<\/i> PfA-M1 aminopeptidase is trafficked via the parasitophorousvacuole and marginally delivered to the food vacuole. Malar. J.<\/i> 9: 189.","DOI":"10.1186\/1475-2875-9-189"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5. Biasini, M., Bienert, S., Waterhouse, A., Arnold, K., Studer, G., Schmidt, T., Kiefer, F., Gallo Cassarino, T., Bertoni, M., Bordoli, L. and Schwede, T. 2014. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res.<\/i> 42: W252-8.","DOI":"10.1093\/nar\/gku340"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6. Dalal, S. and Klemba, M. 2007. Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum<\/i>. J. Biol. Chem.<\/i> 282: 35978\u201335987.","DOI":"10.1074\/jbc.M703643200"},{"key":"7","unstructured":"7. Drag, M., Bogyo, M., Ellman, J. A. and Salvesen, G. S. 2010. Aminopeptidase fingerprints, an integrated approach for identification of good substrates and optimal inhibitors. J. Biol. Chem.<\/i> 285: 3310\u20133318."},{"key":"8","doi-asserted-by":"crossref","unstructured":"8. Fok, A. K., Lee, Y. and Allen, R. D. 1982. The correlation of digestive vacuole pH and size with the digestive cycle in Paramecium caudatum<\/i>. J. Protozool.<\/i> 29: 409\u2013414.","DOI":"10.1111\/j.1550-7408.1982.tb05423.x"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9. Frankel, M. B. and Knoll, L. J. 2009. The ins and outs of nuclear trafficking: unusual aspects in apicomplexan parasites. DNA Cell Biol.<\/i> 28: 277\u2013284.","DOI":"10.1089\/dna.2009.0853"},{"key":"10","unstructured":"10. Gras, S., Byzia, A., Gilbert, F. B., McGowan, S., Drag, M., Silvestre, A., Niepceron, A., Lecaille, F., Lalmanach, G. and Brossier, F. 2014. Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella<\/i>, participates in parasite development. Eukaryot. Cell<\/i> 13: 884\u2013895."},{"key":"11","doi-asserted-by":"crossref","unstructured":"11. Jia, H., Nishikawa, Y., Luo, Y., Yamagishi, J., Sugimoto, C. and Xuan, X. 2010. Characterization of a leucine aminopeptidase from Toxoplasma gondii<\/i>. Mol. Biochem. Parasitol.<\/i> 170: 1\u20136.","DOI":"10.1016\/j.molbiopara.2009.11.005"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12. Kanayama, N., Kajiwara, Y., Goto, J., el Maradny, E., Maehara, K., Andou, K. and Terao, T. 1995. Inactivation of interleukin-8 by aminopeptidase N (CD13). J. Leukoc. Biol.<\/i> 57: 129\u2013134.","DOI":"10.1002\/jlb.57.1.129"},{"key":"13","unstructured":"13. Kim, K. I., Baek, S. H., Hong, Y. M., Kang, M. S., Ha, D. B., Goldberg, A. L. and Chung, C. H. 1995. Purification and characterization of protease Ci, a cytoplasmic metalloendoprotease in Escherichia coli<\/i>. J. Biol. Chem.<\/i> 270: 29799\u201329805."},{"key":"14","doi-asserted-by":"crossref","unstructured":"14. Larsen, S. L., Pedersen, L. O., Buus, S. and Stryhn, A. 1996. T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides. J. Exp. Med.<\/i> 184: 183\u2013189.","DOI":"10.1084\/jem.184.1.183"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15. Lun, Z. R., Lai, D. H., Wen, Y. Z., Zheng, L. L., Shen, J. L., Yang, T. B., Zhou, W. L., Qu, L. H., Hide, G. and Ayala, F. J. 2015. Cancer in the parasitic protozoans Trypanosoma brucei<\/i> and Toxoplasma gondii<\/i>. Proc. Natl. Acad. Sci. U.S.A.<\/i> 112: 8835\u20138842.","DOI":"10.1073\/pnas.1502599112"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16. Mistry, S. N., Drinkwater, N., Ruggeri, C., Sivaraman, K. 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Parasitol.<\/i> 32: 187\u2013197.","DOI":"10.1016\/S0020-7519(01)00317-4"},{"key":"19","unstructured":"19. Pasqualini, R., Koivunen, E., Kain, R., Lahdenranta, J., Sakamoto, M., Stryhn, A., Ashmun, R. A., Shapiro, L. H., Arap, W. and Ruoslahti, E. 2000. Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res.<\/i> 60: 722\u2013727."},{"key":"20","doi-asserted-by":"crossref","unstructured":"20. Pillay, D., Boulang\u00e9, A. F., Coustou, V., Baltz, T. and Coetzer, T. H. 2013. Recombinant expression and biochemical characterisation of two alanyl aminopeptidases of Trypanosoma congolense<\/i>. Exp. Parasitol.<\/i> 135: 675\u2013684.","DOI":"10.1016\/j.exppara.2013.10.005"},{"key":"21","unstructured":"21. Poreba, M., McGowan, S., Skinner-Adams, T. S., Trenholme, K. R., Gardiner, D. L., Whisstock, J. C., To, J., Salvesen, G. S., Dalton, J. P. and Drag, M. 2012. Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum<\/i>. PLoS One<\/i> 7: e31938."},{"key":"22","doi-asserted-by":"crossref","unstructured":"22. Rich, D. H., Moon, B. J. and Harbeson, S. 1984. Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes. J. Med. Chem.<\/i> 27: 417\u2013422.","DOI":"10.1021\/jm00370a001"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23. Sj\u00f6str\u00f6m, H., Nor\u00e9n, O. and Olsen, J. 2000. Structure and function of aminopeptidase N. Adv. Exp. Med. Biol.<\/i> 477: 25\u201334.","DOI":"10.1007\/0-306-46826-3_2"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24. Skinner-Adams, T. S., Stack, C. M., Trenholme, K. R., Brown, C. L., Grembecka, J., Lowther, J., Mucha, A., Drag, M., Kafarski, P., McGowan, S., Whisstock, J. C., Gardiner, D. L. and Dalton, J. P. 2010. 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