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Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase.

Bibliographic reference Hannaert, Véronique ; Albert, Marie-Astrid ; Rigden, Daniel J ; da Silva Giotto, M Theresa ; Thiemann, Otavio ; et. al. Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase.. In: European journal of biochemistry / FEBS, Vol. 270, no. 15, p. 3205-13 (2003)
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  1. Wold F., The Enzymes, 5, 499 (1971)
  2. Schurig H., Protein Sci., 4, 228 (1995)
  3. Brown C. Kent, Kuhlman Peter L., Mattingly Susan, Slates Kevin, Calie Patrick J., Farrar William W., 10.1023/a:1020790604887
  4. Stec B., J. Mol. Biol., 211, 235 (1990)
  5. Lebioda L., Biochemistry, 30, 2817 (1991)
  6. Duquerroy S., Biochemistry, 34, 12513 (1995)
  7. Zhang Erli, Brewer John M., Minor Wladek, Carreira Lionel A., Lebioda Lukasz, Mechanism of Enolase:  The Crystal Structure of Asymmetric Dimer Enolase−2-Phospho-d-glycerate/Enolase−Phosphoenolpyruvate at 2.0 Å Resolution†,‡, 10.1021/bi9712450
  8. Lebioda L., J. Biol. Chem., 264, 3685 (1989)
  9. I. Elliott James, M. Brewer John, Binding of inhibitory metals to yeast enolase, 10.1016/s0162-0134(00)80273-1
  10. Lee B.H., Biochemistry, 31, 2165 (1992)
  11. Faller L.D., Biochemistry, 16, 3864 (1977)
  12. Poyner Russell R., Cleland W. W., Reed George H., Role of Metal Ions in Catalysis by Enolase:  An Ordered Kinetic Mechanism for a Single Substrate Enzyme†, 10.1021/bi0103922
  13. Kornblatt Mary Judith, Lange Reinhard, Balny Claude, Can monomers of yeast enolase have enzymatic activity ?, 10.1046/j.1432-1327.1998.2510775.x
  14. Tanaka M., Biochem. Biophys. Res. Commun., 133, 868 (1985)
  15. Segil N, Shrutkowski A, Dworkin M B, Dworkin-Rastl E, Enolase isoenzymes in adult and developingXenopus laevisand characterization of a cloned enolase sequence, 10.1042/bj2510031
  16. McAlister L., J. Biol. Chem., 257, 7181 (1982)
  17. Entian Karl-D., Fröhlich Kai-U., Mecke Dieter, Regulation of enzymes and isoenzymes of carbohydrate metabolism in the yeast Saccharomyces cerevisiae, 10.1016/0304-4165(84)90293-9
  18. Entian Karl-Dieter, Meurer Bernd, Helmut Köhler, Mann Karl-Heinz, Mecke Dieter, Studies on the regulation of enolases and compartmentation of cytosolic enzymes in Saccharomyces cerevisiae, 10.1016/0304-4165(87)90006-7
  19. World Health Organization, WHO Fifteenth Programme Report: UNDP/World Bank/WHO Special Programme for Research and Training in Tropical Diseases (TDR). (2001)
  20. Gelb M. H., PARASITOLOGY: Enhanced: Drugs to Combat Tropical Protozoan Parasites, 10.1126/science.1073126
  21. Verlinde Christophe L.M.J., Hannaert Véronique, Blonski Casimir, Willson Michèle, Périé Jacques J., Fothergill-Gilmore Linda A., Opperdoes Fred R., Gelb Michael H., Hol Wim G.J., Michels Paul A.M., Glycolysis as a target for the design of new anti-trypanosome drugs, 10.1054/drup.2000.0177
  22. Opperdoes Fred R., Borst Piet, Localization of nine glycolytic enzymes in a microbody-like organelle inTrypanosoma brucei: The glycosome, 10.1016/0014-5793(77)80476-6
  23. Oduro K.K., Exp. Parasitol., 50, 240 (1980)
  24. Hannaert V., Brinkmann H., Nowitzki U., Lee J. A., Albert M.-A., Sensen C. W., Gaasterland T., M M., Michels P., Martin W., Enolase from Trypanosoma brucei, from the Amitochondriate Protist Mastigamoeba balamuthi, and from the Chloroplast and Cytosol of Euglena gracilis: Pieces in the Evolutionary Puzzle of the Eukaryotic Glycolytic Pathway, 10.1093/oxfordjournals.molbev.a026395
  25. Keeling Patrick J., Palmer Jeffrey D., 10.1038/35015167
  26. Opperdoes F.R., Exp. Parasitol., 40, 198 (1976)
  27. Brun R., Acta Trop., 36, 289 (1979)
  28. Steiger R.F., Eur. J. Biochem., 105, 163 (1980)
  29. Bradford M, A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, 10.1006/abio.1976.9999
  30. Laemmli U.K., Nature, 227, 680 (1970)
  31. Towbin H., Proc. Natl Acad. Sci. USA, 76, 4350 (1979)
  32. Lambeir A.-M., Eur. J. Biochem., 198, 429 (1991)
  33. Cleland W.W., Methods Enzymol., 63, 103 (1970)
  34. Bairoch A., The ENZYME database in 2000, 10.1093/nar/28.1.304
  35. Higgins D., Nucleic Acids Res., 22, 4673 (1994)
  36. Kühnel Karin, Luisi Ben F, Crystal structure of the Escherichia coli RNA degradosome component enolase, 10.1006/jmbi.2001.5065
  37. Šali Andrej, Blundell Tom L., Comparative Protein Modelling by Satisfaction of Spatial Restraints, 10.1006/jmbi.1993.1626
  38. Wedekind J.E., Biochemistry, 34, 4325 (1995)
  39. Frishman D., Proteins, 23, 566 (1995)
  40. Kabsch W., Biopolymers, 22, 2577 (1983)
  41. Opperdoes F., Compartmentation Of Carbohydrate Metabolism In Trypanosomes, 10.1146/annurev.micro.41.1.127
  42. Michels P.A.M., Trypanosomiasis and Leishmaniasis: Biology and Control, 133 (1996)
  43. HART D, MISSET O, EDWARDS S, OPPERDOES F, A comparison of the glycosomes (microbodies) isolated from Trypanosoma brucei bloodstream form and cultured procyclic trypomastigotes, 10.1016/0166-6851(84)90041-0
  44. Chevalier Nathalie, Rigden Daniel J., Van Roy Joris, Opperdoes Fred R., Michels Paul A. M., Trypanosoma brucei contains a 2,3-bisphosphoglycerate independent phosphoglycerate mutase : Trypanosoma brucei phosphoglycerate mutase, 10.1046/j.1432-1327.2000.01145.x
  45. Kornblatt M.J., Biochem. Cell. Biol., 67, 103 (1989)
  46. Reed George H, Poyner Russell R, Larsen Todd M, Wedekind Joseph E, Rayment Ivan, Structural and mechanistic studies of enolase, 10.1016/s0959-440x(96)80002-9
  47. Wedekind J.E., Biochemistry, 33, 9333 (1994)
  48. López Claudia, Chevalier Nathalie, Hannaert Véronique, Rigden Daniel J., Michels Paul A. M., Ramirez Jose Luis, Leishmania donovani phosphofructokinase : Gene characterization, biochemical properties and structure-modelling studies, 10.1046/j.1432-1033.2002.03086.x
  49. Ferre-D'Amare A.R., Methods Enzymol., 276, 157 (1997)
  50. Beaufay Henri, Amar-Costesec Alain, Cell Fractionation Techniques, Methods in Membrane Biology (1976) ISBN:9781475758191 p.1-100, 10.1007/978-1-4757-5817-7_1
  51. Barton G.J., Protein Eng., 6, 37 (1993)
  52. 52. W.L. DeLano (2002 ) The PyMOL Molecular Graphics System on World Wide Web: