User menu

Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism.

Bibliographic reference Blattner, J ; Helfert, S ; Michels, Paulus ; Clayton, C. Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism.. In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, no. 20, p. 11596-600 (1998)
Permanent URL http://hdl.handle.net/2078.1/26813
  1. 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
  2. Clayton Christine E., Michels Paul, Metabolic compartmentation in African trypanosomes, 10.1016/s0169-4758(96)10073-9
  3. Osinga, The EMBO Journal, 4, 3811 (1985)
  4. Le Blancq S.M., Swinkels B.W., Gibson W.C., Borst P., Evidence for gene conversion between the phosphoglycerate kinase genes of Trypanosoma brucei, 10.1016/0022-2836(88)90534-7
  5. Alexander Keith, Parsons Marilyn, Characterization of a divergent glycosomal microbody phosphoglycerate kinase from Trypanosoma brucei, 10.1016/0166-6851(93)90137-m
  6. Swinkels Bart W., Loiseau Ann, Opperdoes Fred R., Borst Piet, A phosphoglycerate kinase-related gene conserved between Trypanosoma brucei and Crithidia fasciculata, 10.1016/0166-6851(92)90245-f
  7. Fung Kelly, Clayton Christine, Recognition of a peroxisomal tripeptide entry signal by the glycosomes of Trypanosoma brucei, 10.1016/0166-6851(91)90093-l
  8. Blattner J., Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal, 10.1083/jcb.119.5.1129
  9. Sommer Jürg M., Peterson Gregory, Keller Gilbert-A., Parsons Marilyn, Wang C.C., The C-terminal tripeptide of glycosomal phosphoglycerate kinase is both necessary and sufficient for import into the glycosomes ofTrypanosoma brucei, 10.1016/0014-5793(93)81735-i
  10. Blattner Judith, Clayton Christine E., The 3′-untranslated regions from the Trypanosoma brucei phosphoglycerate kinase-encoding genes mediate developmental regulation, 10.1016/0378-1119(95)00366-e
  11. Biebinger Susanne, Elizabeth Wirtz L., Lorenz Patrick, Christine Clayton, Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei, 10.1016/s0166-6851(96)02815-0
  12. Hausler T., Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin, 10.1083/jcb.132.3.311
  13. MISSET Onno, BOS Octaaf J. M., OPPERDOES Fred R., Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification, intraglycosomal concentrations and physical properties, 10.1111/j.1432-1033.1986.tb09687.x
  14. VISSER Nico, OPPERDOES Fred. R., BORST Piet, Subcellular Compartmentation of Glycolytic Intermediates in Trypanosoma brucei, 10.1111/j.1432-1033.1981.tb05550.x
  15. Stitt Mark, Lilley Ross McC., Gerhardt Richard, Heldt Hans W., [32] Metabolite levels in specific cells and subcellular compartments of plant leaves, Biomembranes Part U: Cellular and Subcellular Transport: Eukaryotic (Nonepithelial) Cells (1989) ISBN:9780121820756 p.518-552, 10.1016/0076-6879(89)74035-0
  16. Valdes J, The viral thymidine kinase gene as a tool for the study of mutagenesis in Trypanosoma brucei, 10.1093/nar/24.10.1809
  17. Wilson C A B, Hardman N, Fothergill-Gilmore L A, Gamblin S J, Watson H C, Yeast phosphoglycerate kinase: investigation of catalytic function by site-directed mutagenesis, 10.1042/bj2410609
  18. GRAHAM Heidi C., WILLIAMS Robert J. P., LITTLECHILD Jennifer A., WATSON Herman C., A proton-NMR study of a site-directed mutation (His388 Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement, 10.1111/j.1432-1033.1991.tb15813.x
  19. Mas Maria T., Resplandor Zenaida E., Structure-function relationships in 3-phosphoglycerate kinase: Role of the carboxy-terminal peptide, 10.1002/prot.340040108
  20. Brohn Fredrick H., Clarkson Allen B., Trypanosoma brucei brucei: Patterns of glycolysis at 37°C in vitro, 10.1016/0166-6851(80)90062-6
  21. VISSER Nico, OPPERDOES Fred R., Glycolysis in Trypanosoma brucei, 10.1111/j.1432-1033.1980.tb05988.x
  22. van Roermund, The EMBO Journal, 14, 3480 (1995)
  23. Parker H, Three genes and two isozymes: gene conversion and the compartmentalization and expression of the phosphoglycerate kinases of Trypanosoma (Nannomonas) congolense, 10.1016/0166-6851(94)00208-5
  24. MISSET Onno, BEEUMEN Jozef, LAMBEIR Anne-Marie, MEER Rob, OPPERDOES Fred R., Glyceraldehyde-phosphate dehydrogenase from Trypanosoma brucei. Comparison of the glycosomal and cytosolic isoenzymes, 10.1111/j.1432-1033.1987.tb10668.x
  25. Webster G.D., Edwards P.A., Jackson J.B., Interconversion of two kinetically distinct states of the membrane-bound and solubilised H+-translocating ATPase fromRhodospirillum rubrum, 10.1016/0014-5793(77)80114-2
  26. Opperdoes F R, Compartmentation of Carbohydrate Metabolism in Trypanosomes, 10.1146/annurev.mi.41.100187.001015
  27. Hart David T., Opperdoes Fred R., The occurrence of glycosomes (microbodies) in the promastigote stage of four major Leishmania species, 10.1016/0166-6851(84)90110-5
  28. Mottram Jeremy C., Coombs Graham H., Leishmania mexicana: Subcellular distribution of enzymes in amastigotes and promastigotes, 10.1016/0014-4894(85)90081-5
  29. KOHL Linda, CALLENS Mia, WIERENGA Rik K., OPPERDOES Fred R., MICHELS Paul A. M., Triose-phosphate isomerase of Leishmania mexicana mexicana Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein, 10.1111/j.1432-1033.1994.tb18629.x
  30. Cronín Ciaran N., Nolan Derek P., Paul Voorheis H., The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms ofTrypanosoma brucei, 10.1016/0014-5793(89)81154-8
  31. Bakker Barbara M., Michels Paul A. M., Opperdoes Fred R., Westerhoff Hans V., Glycolysis in Bloodstream FormTrypanosoma bruceiCan Be Understood in Terms of the Kinetics of the Glycolytic Enzymes, 10.1074/jbc.272.6.3207