Kim, Yong-Tae
(Department of Food Science and Technology, Kunsan National University)
Kim, Se-Kwon (Department of Chemistry, Pukyong National University) Jeon, You-Jin (Department of Marine Life Sciences, Jeju National University) Park, Sun Joo (Department of Chemistry, Pukyong National University) |
1 | Takei, N., Kondo, J., Nagaike, K., Ohsawa, K., Kato, K. and Kohsaka, S. (1991) Neuronal survival factor from bovine brain is identical to neuron-specific enolase. J. Neurochem. 57, 1178-1184. DOI |
2 | al-Giery, A. G. and Brewer, J. M. (1992) Characterization of the interaction of yeast enolase with polynucleotides. Biochim. Biophys. Acta. 1159, 134-140. DOI ScienceOn |
3 | Vanegas, G., Quinones, W., Carrasco-Lopez, C., Concepcion, J. L., Albericio, F. and Avilan, L. (2007) Enolase as a plasminogen binding protein in Leishmania mexicana. Parasitol. Res. 101, 1511-1516. DOI |
4 | Mundodi, V., Kucknoor, A. S. and Alderete, J. F. (2008) Immunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalis. Infect. Immun. 76, 523-531. DOI ScienceOn |
5 | Plow, E. F., Felez, J. and Miles, L. A. (1991) Cellular regulation of fibrinolysis. Thromb. Haemost. 66, 32-36. |
6 | Plow, E. F., Herren, T., Redlitz, A., Miles, L. A. and Hoover-Plow, J. L. (1995) The cell biology of the plasminogen system. FASEB J. 9, 939-945. DOI |
7 | Wiman, B. and Collen, D. (1979) On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin. J. Biol. Chem. 254, 9291-9297. |
8 | Lancefield, R. C. (1957) Differentiation of group A streptococci with a common R antigen into three serological types, with special reference to the bactericidal test. J. Exp. Med. 106, 525-544. DOI |
9 | Gentile, F., Pizzimenti, S., Arcaro, A., Pettazzoni, P., Minelli, R., D'Angelo, D., Mamone, G., Ferranti, P., Toaldo, C., Cetrangolo, G., Formisano, S., Dianzani, M. U., Uchida, K., Dianzani, C. and Barrera, G. (2009) Exposure of HL-60 human leukaemic cells to 4-hydroxynonenal promotes the formation of adduct(s) with alpha-enolase devoid of plasminogen binding activity. Biochem. J. 422, 285-294. DOI ScienceOn |
10 | Ryu, B., Qian, Z. J. and Kim, S. K. (2010) Purification of a peptide from seahorse, that inhibits TPA-induced MMP, iNOS and COX-2 expression through MAPK and NF-kappaB activation, and induces human osteoblastic and chondrocytic differentiation. Chem. Biol. Interact. 184, 413-422. DOI ScienceOn |
11 | Quinones, W., Pena, P., Domingo-Sananes, M., Caceres, A., Michels, P. A., Avilan, L. and Concepcion, J. L. (2007) Leishmania mexicana: molecular cloning and characterization of enolase. Exp. Parasitol. 116, 241-251. DOI ScienceOn |
12 | Pancholi, V. (2001) Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci. 58, 902-920. DOI ScienceOn |
13 | Boyle, M. D. and Lottenberg, R. (1997) Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77, 1-10. |
14 | Coleman, J. L. and Benach, J. L. (1999) Use of the plasminogen activation system by microorganisms. J. Lab. Clin. Med. 134, 567-576. DOI ScienceOn |
15 | Bergmann, S., Wild, D., Diekmann, O., Frank, R., Bracht, D., Chhatwal, G. S. and Hammerschmidt, S. (2003) Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol. Microbiol. 49, 411-423. DOI ScienceOn |
16 | Ehinger, S., Schubert, W. D., Bergmann, S., Hammerschmidt, S. and Heinz, D. W. (2004) Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. J. Mol. Biol. 343, 997-1005. DOI ScienceOn |
17 | Felez, J., Chanquia, C. J., Levin, E. G., Miles, L. A. and Plow, E. F. (1991) Binding of tissue plasminogen activator to human monocytes and monocytoid cells. Blood 78, 2318-2327. |
18 | Del Pozo, V., Rojo, M., Rubio, M. N., Cortegano, I., Cardaba, B., Gallardo, S., Ortega, M., Civantos, E., Lopez, E., Martin-Mosquero, C., Peces-Barba, G., Palomino, P., Gonzalez-Mangado, N. and Lahoz, C. (2002) Gene therapy with galectin-3 inhibits bronchial obstruction and inflammation in antigen-challenged rats through inerleukin-5 gene downregulation. Am. J. Respir. Crit. Care Med. 166, 732-737. DOI ScienceOn |
19 | Fluit, A. C., Wolfhagen, M. J., Jansze, M., Torensma, R. and Verhoef, J. (1993) Toxin B of Clostridium difficile does not have enolase activity. FEBS Lett. 316, 103-105. DOI ScienceOn |
20 | Lahteenmaki, K., Edelman, S. and Korhonen, T. K. (2005) Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends. Microbiol. 13, 79-85. DOI ScienceOn |