User menu

The function of glycosomes in the metabolism of trypanosomatid particles and the promise of glycososomal proteins as drug targets

Bibliographic reference Gualdron-Lopez, M. ; Michels, Paulus ; Quinones, W. ; Caceres, A.J. ; Avilan, L. ; et. al. The function of glycosomes in the metabolism of trypanosomatid particles and the promise of glycososomal proteins as drug targets. In: Jäger T, Koch O, Flohé L, eds, Trypanosomatid diseases: Molecular routes to drug discovery, Wiley-VCH Verlag GmbH & Co. KGaA  2013, p. 121-51
Permanent URL http://hdl.handle.net/2078/122550
  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. Gualdrón-López Melisa, Brennand Ana, Hannaert Véronique, Quiñones Wilfredo, Cáceres Ana J., Bringaud Frédéric, Concepción Juan Luis, Michels Paul A.M., When, how and why glycolysis became compartmentalised in the Kinetoplastea. A new look at an ancient organelle, 10.1016/j.ijpara.2011.10.007
  3. Opperdoes Fred R., Szikora Jean-Pierre, In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes, 10.1016/j.molbiopara.2006.02.010
  4. HELFERT Sandra, ESTÉVEZ Antonio M., BAKKER Barbara, MICHELS Paul, CLAYTON Christine, Roles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei, 10.1042/0264-6021:3570117
  5. 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
  6. Opperdoes Fred R., Michels Paul A.M., Enzymes of carbohydrate metabolism as potential drug targets, 10.1016/s0020-7519(01)00155-2
  7. SEYFANG Andreas, DUSZENKO Michael, Specificity of glucose transport in Trypanosoma brucei. Effective inhibition by phloretin and cytochalasin B, 10.1111/j.1432-1033.1991.tb16362.x
  8. Albert Marie-Astrid, Haanstra Jurgen R., Hannaert Véronique, Van Roy Joris, Opperdoes Fred R., Bakker Barbara M., Michels Paul A. M., Experimental andin SilicoAnalyses of Glycolytic Flux Control in Bloodstream FormTrypanosoma brucei, 10.1074/jbc.m502403200
  9. Cáceres Ana Judith, Michels Paul A.M., Hannaert Véronique, Genetic validation of aldolase and glyceraldehyde-3-phosphate dehydrogenase as drug targets in Trypanosoma brucei, 10.1016/j.molbiopara.2009.09.001
  10. Bakker B. M., Walsh M. C., ter Kuile B. H., Mensonides F. I. C., Michels P. A. M., Opperdoes F. R., Westerhoff H. V., Contribution of glucose transport to the control of the glycolytic flux in Trypanosoma brucei, 10.1073/pnas.96.18.10098
  11. Wiemer E A C, Michels P A M, Opperdoes F R, The inhibition of pyruvate transport across the plasma membrane of the bloodstream form ofTrypanosoma bruceiand its metabolic implications, 10.1042/bj3120479
  12. 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
  13. Bakker Barbara M., Michels Paul A. M., Opperdoes Fred R., Westerhoff Hans V., What Controls Glycolysis in Bloodstream FormTrypanosoma brucei?, 10.1074/jbc.274.21.14551
  14. Bakker Barbara M, Westerhoff Hans V, Opperdoes Fred R, Michels Paul A.M, Metabolic control analysis of glycolysis in trypanosomes as an approach to improve selectivity and effectiveness of drugs, 10.1016/s0166-6851(99)00197-8
  15. Haanstra Jurgen R., Kerkhoven Eduard J., van Tuijl Arjen, Blits Marjolein, Wurst Martin, van Nuland Rick, Albert Marie-Astrid, Michels Paul A. M., Bouwman Jildau, Clayton Christine, Westerhoff Hans V., Bakker Barbara M., A domino effect in drug action: from metabolic assault towards parasite differentiation : Network-based drug target selection in T. brucei, 10.1111/j.1365-2958.2010.07435.x
  16. Schuster Ronny, Holzhutter Hermann-Georg, Use of Mathematical Models for Predicting the Metabolic Effect of Large-Scale Enzyme Activity Alterations. Application to Enzyme Deficiencies of Red Blood Cells, 10.1111/j.1432-1033.1995.0403k.x
  17. Hornberg, Prog. Drug. Res., 64, 172 (2007)
  18. 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
  19. Cordeiro Artur T., Thiemann Otavio H., Michels Paul A.M., Inhibition of Trypanosoma brucei glucose-6-phosphate dehydrogenase by human steroids and their effects on the viability of cultured parasites, 10.1016/j.bmc.2009.01.068
  20. Gupta Shreedhara, Cordeiro Artur T., Michels Paul A.M., Glucose-6-phosphate dehydrogenase is the target for the trypanocidal action of human steroids, 10.1016/j.molbiopara.2010.12.006
  21. Hanau Stefania, Rinaldi Eliana, Dallocchio Franco, Gilbert Ian, Dardonville Christophe, Adams Margaret, Gover Sheila, Barrett Michael, 6-Phosphogluconate Dehydrogenase: A Target for Drugs in African Trypanosomes, 10.2174/0929867043364441
  22. Gupta Shreedhara, Igoillo-Esteve Mariana, Michels Paul A. M., Cordeiro Artur T., Glucose-6-Phosphate Dehydrogenase of Trypanosomatids: Characterization, Target Validation, and Drug Discovery, 10.4061/2011/135701
  23. Roper J. R., Guther M. L. S., Milne K. G., Ferguson M. A. J., Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei, 10.1073/pnas.092669999
  24. Roper Janine R., Güther M. Lucia S., MacRae James I., Prescott Alan R., Hallyburton Irene, Acosta-Serrano Alvaro, Ferguson Michael A. J., The Suppression of Galactose Metabolism in Procylic FormTrypanosoma bruceiCauses Cessation of Cell Growth and Alters Procyclin Glycoprotein Structure and Copy Number, 10.1074/jbc.m502370200
  25. Turnock Daniel C., Izquierdo Luis, Ferguson Michael A. J., Thede NovoSynthesis of GDP-fucose Is Essential for Flagellar Adhesion and Cell Growth inTrypanosoma brucei, 10.1074/jbc.m704742200
  26. Stokes Matthew J., Güther M. Lucia S., Turnock Daniel C., Prescott Alan R., Martin Kirstee L., Alphey Magnus S., Ferguson Michael A. J., The Synthesis of UDP-N-acetylglucosamine Is Essential for Bloodstream FormTrypanosoma brucei in Vitroandin Vivoand UDP-N-acetylglucosamine Starvation Reveals a Hierarchy in Parasite Protein Glycosylation, 10.1074/jbc.m709581200
  27. Marino K., Guther M. L. S., Wernimont A. K., Amani M., Hui R., Ferguson M. A., Identification, subcellular localization, biochemical properties, and high-resolution crystal structure of Trypanosoma brucei UDP-glucose pyrophosphorylase, 10.1093/glycob/cwq115
  28. Marino K., Guther M. L. S., Wernimont A. K., Qiu W., Hui R., Ferguson M. A. J., Characterization, Localization, Essentiality, and High-Resolution Crystal Structure of Glucosamine 6-Phosphate N-Acetyltransferase from Trypanosoma brucei, 10.1128/ec.05025-11
  29. Denton Helen, Fyffe Stewart, Smith Terry K., GDP-mannose pyrophosphorylase is essential in the bloodstream form ofTrypanosoma brucei, 10.1042/bj20090896
  30. Stoppani A.O.M., Docampo R., De Boiso J.F., Frasch A.C.C., Effect of inhibitors of electron transport and oxidative phosphorylation on trypanosoma cruzi respiration and growth, 10.1016/0166-6851(80)90044-4
  31. Cannata Joaquín J.B., Cazzulo Juan José, The aerobic fermentation of glucose by Trypanosoma cruzi, 10.1016/0305-0491(84)90380-8
  32. Sanchez-moreno M., Fernandez-becerra M.C, Castilla-calvente J.J., Osuna A., Metabolic studies by1H NMR of different forms ofTrypanosoma cruzias obtained by ‘in vitro’ culture, 10.1111/j.1574-6968.1995.tb07871.x
  33. Taylor Mark B., Gutteridge Winston E., Trypanosoma cruzi: Subcellular distribution of glycolytic and some related enzymes of epimastigotes, 10.1016/0014-4894(87)90081-6
  34. Besteiro Sébastien, Biran Marc, Biteau Nicolas, Coustou Virginie, Baltz Théo, Canioni Paul, Bringaud Frédéric, Succinate Secreted byTrypanosoma bruceiIs Produced by a Novel and Unique Glycosomal Enzyme, NADH-dependent Fumarate Reductase, 10.1074/jbc.m201759200
  35. Acosta Héctor, Dubourdieu Michel, Quiñones Wilfredo, Cáceres Ana, Bringaud Frederic, Concepción Juan Luis, Pyruvate phosphate dikinase and pyrophosphate metabolism in the glycosome of Trypanosoma cruzi epimastigotes, 10.1016/j.cbpc.2004.04.017
  36. Concepcion JL, Acosta H, Quiñones W, Dubourdieu M, A α-glycerophosphate dehydrogenase is present in Trypanosoma cruzi glycosomes, 10.1590/s0074-02762001000500021
  37. Sarkar Mitali, Hamilton Christopher J., Fairlamb Alan H., Properties of Phosphoenolpyruvate Mutase, the First Enzyme in the Aminoethylphosphonate Biosynthetic Pathway inTrypanosoma cruzi, 10.1074/jbc.m302419200
  38. Kollien Astrid, Schaub Günter, The Development of Trypanosoma cruzi in Triatominae, 10.1016/s0169-4758(00)01724-5
  39. Maugeri Dante A., Cannata Joaquin J.B., Cazzulo Juan-José, Glucose metabolism inTrypanosoma cruzi, 10.1042/bse0510015
  40. Engel Juan Carlos, Franke de Cazzulo Berta M., Stoppani Andres O.M., Cannata Joaquin J.B., Cazzulo Juan Jose, Aerobic glucose fermentation by Trypanosoma cruzi axenic culture amastigote-like forms during growth and differentiation to epimastigotes, 10.1016/0166-6851(87)90123-x
  41. Atwood J. A., The Trypanosoma cruzi Proteome, 10.1126/science.1110289
  42. Silber Ariel M., Tonelli Renata R., Lopes Camila G., Cunha-e-Silva Narcisa, Torrecilhas Ana Cláudia T., Schumacher Robert I., Colli Walter, Alves Maria Júlia M., Glucose uptake in the mammalian stages of Trypanosoma cruzi, 10.1016/j.molbiopara.2009.07.006
  43. Berriman M., The Genome of the African Trypanosome Trypanosoma brucei, 10.1126/science.1112642
  44. Maugeri Dante A., Cazzulo Juan J., The pentose phosphate pathway inTrypanosoma cruzi, 10.1111/j.1574-6968.2004.tb09522.x
  45. Urbina Julio A, Concepcion Juan Luis, Rangel Salomé, Visbal Gonzalo, Lira Renee, Squalene synthase as a chemotherapeutic target in Trypanosoma cruzi and Leishmania mexicana, 10.1016/s0166-6851(02)00206-2
  46. Allen Thomas E., Ullman Buddy, Molecular characterization and overexpression of the hypoxanthine-guanine phosphoribosyltransferase gene from Trypanosoma cruzi, 10.1016/0166-6851(94)90075-2
  47. Urbina Julio A., Docampo Roberto, Specific chemotherapy of Chagas disease: controversies and advances, 10.1016/j.pt.2003.09.001
  48. Urbina Julio A., Specific chemotherapy of Chagas disease: Relevance, current limitations and new approaches, 10.1016/j.actatropica.2009.10.023
  49. Quiñones Wilfredo, Urbina Julio A., Dubourdieu Michel, Luis Concepción Juan, The glycosome membrane of Trypanosoma cruzi epimastigotes: protein and lipid composition, 10.1016/j.exppara.2004.03.006
  50. Aboushadi Nahla, Engfelt William Harrison, Paton Vincent G., Krisans Skaidrite K., Role of Peroxisomes in Isoprenoid Biosynthesis, 10.1177/002215549904700904
  51. Cáceres Ana Judith, Portillo Ramon, Acosta Hector, Rosales David, Quiñones Wilfredo, Avilan Luisana, Salazar Leiria, Dubourdieu Michel, Michels Paul A.M, Concepción Juan Luis, Molecular and biochemical characterization of hexokinase from Trypanosoma cruzi, 10.1016/s0166-6851(02)00294-3
  52. Cáceres Ana Judith, Quiñones Wilfredo, Gualdrón Melisa, Cordeiro Artur, Avilán Luisana, Michels Paul A.M., Concepción Juan Luis, Molecular and biochemical characterization of novel glucokinases from Trypanosoma cruzi and Leishmania spp., 10.1016/j.molbiopara.2007.08.007
  53. Cordeiro Artur T., Cáceres Ana J., Vertommen Didier, Concepción Juan Luis, Michels Paul A.M., Versées Wim, The Crystal Structure of Trypanosoma cruzi Glucokinase Reveals Features Determining Oligomerization and Anomer Specificity of Hexose-phosphorylating Enzymes, 10.1016/j.jmb.2007.07.021
  54. Murray Henry W, Berman Jonathan D, Davies Clive R, Saravia Nancy G, Advances in leishmaniasis, 10.1016/s0140-6736(05)67629-5
  55. Naderer Thomas, McConville Malcolm J., Intracellular growth and pathogenesis ofLeishmaniaparasites, 10.1042/bse0510081
  56. McConville Malcolm J., Naderer Thomas, Metabolic Pathways Required for the Intracellular Survival of Leishmania, 10.1146/annurev-micro-090110-102913
  57. Coombs G. H., Tetley L., Moss V. A., Vickerman K., Three dimensional structure of the leishmania amastigote as revealed by computer-aided reconstruction from serial sections, 10.1017/s0031182000063411
  58. Coombs Graham H., Craft John A., Hart David T., A comparative study of Leishmania mexicana amastigotes and promastigotes, enzyme activities and subcellular locations, 10.1016/0166-6851(82)90021-4
  59. Mottram Jeremy C., Coombs Graham H., Leishmania mexicana: Subcellular distribution of enzymes in amastigotes and promastigotes, 10.1016/0014-4894(85)90081-5
  60. Pabón Miguel A., Cáceres Ana J., Gualdrón Melisa, Quiñones Wilfredo, Avilán Luisana, Concepción Juan L., Purification and characterization of hexokinase from Leishmania mexicana, 10.1007/s00436-006-0351-4
  61. Rosenzweig D., Smith D., Opperdoes F., Stern S., Olafson R. W., Zilberstein D., Retooling Leishmania metabolism: from sand fly gut to human macrophage, 10.1096/fj.07-9254com
  62. Naderer Thomas, McConville Malcolm J., The Leishmania-macrophage interaction: a metabolic perspective : Leishmania metabolism in macrophages, 10.1111/j.1462-5822.2007.01096.x
  63. Burchmore R. J. S., Rodriguez-Contreras D., McBride K., Barrett M. P., Modi G., Sacks D., Landfear S. M., Genetic characterization of glucose transporter function in Leishmania mexicana, 10.1073/pnas.0630165100
  64. Feng Xiuhong, Rodriguez-Contreras Dayana, Buffalo Cosmo, Bouwer H. G. Archie, Kruvand Elizabeth, Beverley Stephen M., Landfear Scott M., Amplification of an alternate transporter gene suppresses the avirulent phenotype of glucose transporter null mutants inLeishmania mexicana, 10.1111/j.1365-2958.2008.06531.x
  65. Brotherton Marie-Christine, Racine Gina, Foucher Aude L., Drummelsmith Jolyne, Papadopoulou Barbara, Ouellette Marc, Analysis of Stage-Specific Expression of Basic Proteins inLeishmania infantum, 10.1021/pr100048m
  66. Naderer T., Ellis M. A., Sernee M. F., De Souza D. P., Curtis J., Handman E., McConville M. J., Virulence of Leishmania major in macrophages and mice requires the gluconeogenic enzyme fructose-1,6-bisphosphatase, 10.1073/pnas.0509196103
  67. Keegan Frank P., Joseph Blum J., Utilization of a carbohydrate reserve comprised primarily of mannose by Leishmania donovani, 10.1016/0166-6851(92)90021-b
  68. Ralton Julie E., Naderer Thomas, Piraino Helena L., Bashtannyk Tanya A., Callaghan Judy M., McConville Malcolm J., Evidence That Intracellular β1-2 Mannan Is a Virulence Factor inLeishmaniaParasites, 10.1074/jbc.m307660200
  69. Garami A., Disruption of mannose activation in Leishmania mexicana: GDP-mannose pyrophosphorylase is required for virulence, but not for viability, 10.1093/emboj/20.14.3657
  70. Naderer Thomas, Wee Edmund, McConville Malcolm J., Role of hexosamine biosynthesis inLeishmaniagrowth and virulence, 10.1111/j.1365-2958.2008.06314.x
  71. Joshi Manju B., Rogers Matthew E., Shakarian Alison M., Yamage Mat, Al-Harthi Saeed A., Bates Paul A., Dwyer Dennis M., Molecular Characterization, Expression, andin VivoAnalysis ofLmexCht1 : THE CHITINASE OF THE HUMAN PATHOGEN,LEISHMANIA MEXICANA, 10.1074/jbc.m412299200
  72. Naderer Thomas, Heng Joanne, McConville Malcolm J., Evidence That Intracellular Stages of Leishmania major Utilize Amino Sugars as a Major Carbon Source, 10.1371/journal.ppat.1001245
  73. 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
  74. Paape Daniel, Lippuner Christoph, Schmid Monika, Ackermann Renate, Barrios-Llerena Martin E., Zimny-Arndt Ursula, Brinkmann Volker, Arndt Benjamin, Pleissner Klaus Peter, Jungblut Peter R., Aebischer Toni, Transgenic, FluorescentLeishmania mexicanaAllow Direct Analysis of the Proteome of Intracellular Amastigotes, 10.1074/mcp.m700343-mcp200
  75. Pena-Diaz J., Mitochondrial Localization of the Mevalonate Pathway Enzyme 3-Hydroxy-3-methyl-glutaryl-CoA Reductase in the Trypanosomatidae, 10.1091/mbc.e03-10-0720
  76. Ginger M. L., McFadden G. I., Michels P. A. M., Rewiring and regulation of cross-compartmentalized metabolism in protists, 10.1098/rstb.2009.0259
  77. Carrero-Lérida Juana, Pérez-Moreno Guiomar, Castillo-Acosta Victor M., Ruiz-Pérez Luis M., González-Pacanowska Dolores, Intracellular location of the early steps of the isoprenoid biosynthetic pathway in the trypanosomatids Leishmania major and Trypanosoma brucei, 10.1016/j.ijpara.2008.08.012
  78. Colotti Gianni, Ilari Andrea, Polyamine metabolism in Leishmania: from arginine to trypanothione, 10.1007/s00726-010-0630-3
  79. Krauth-Siegel Luise R., Comini Marcelo A., Schlecker Tanja, The Trypanothione System, Subcellular Biochemistry (2007) ISBN:9781402060502 p.231-251, 10.1007/978-1-4020-6051-9_11
  80. Gaur U., Roberts S. C., Dalvi R. P., Corraliza I., Ullman B., Wilson M. E., An Effect of Parasite-Encoded Arginase on the Outcome of Murine Cutaneous Leishmaniasis, 10.4049/jimmunol.179.12.8446
  81. Balaña-Fouce Rafael, Calvo-Álvarez Estefanía, Álvarez-Velilla Raquel, Prada Christopher F., Pérez-Pertejo Yolanda, Reguera Rosa M., Role of trypanosomatid's arginase in polyamine biosynthesis and pathogenesis, 10.1016/j.molbiopara.2011.10.007
  82. Das Priyanka, Lahiri Amit, Lahiri Ayan, Chakravortty Dipshikha, Modulation of the Arginase Pathway in the Context of Microbial Pathogenesis: A Metabolic Enzyme Moonlighting as an Immune Modulator, 10.1371/journal.ppat.1000899
  83. Opperdoes, Leishmania: After the Genome, 123 (2008)
  84. Wilkinson S. R., Prathalingam S. R., Taylor M. C., Horn D., Kelly J. M., Vitamin C biosynthesis in trypanosomes: A role for the glycosome, 10.1073/pnas.0504251102
  85. Biyani Neha, Madhubala Rentala, Leishmania donovani encodes a functional enzyme involved in vitamin c biosynthesis: Arabino-1,4-lactone oxidase, 10.1016/j.molbiopara.2011.08.005
  86. Hassan H.F., Mottram J.C., Coombs G.H., Subcellular localisation of purinemetabolising enzymes in Leishmania mexicana mexicana, 10.1016/0305-0491(85)90110-5
  87. Zarella-Boitz Jan M, Rager Nicolle, Jardim Armando, Ullman Buddy, Subcellular localization of adenine and xanthine phosphoribosyltransferases in Leishmania donovani, 10.1016/j.molbiopara.2003.08.016
  88. Boitz Jan M., Ullman Buddy, A Conditional Mutant Deficient in Hypoxanthine-guanine Phosphoribosyltransferase and Xanthine Phosphoribosyltransferase Validates the Purine Salvage Pathway ofLeishmania donovani, 10.1074/jbc.m600188200
  89. Carter, Mol. Microbiol., 78, 92 (2010)
  90. French Jarrod B., Yates Phillip A., Soysa D. Radika, Boitz Jan M., Carter Nicola S., Chang Bailey, Ullman Buddy, Ealick Steven E., TheLeishmania donovaniUMP Synthase Is Essential for Promastigote Viability and Has an Unusual Tetrameric Structure That Exhibits Substrate-controlled Oligomerization, 10.1074/jbc.m111.228213
  91. Yernaux Cédric, Fransen Marc, Brees Chantal, Stephan Lorenzen L, Michels Paul A. M., Trypanosoma bruceiglycosomal ABC transporters: identification and membrane targeting, 10.1080/09687860500460124
  92. Igoillo-Esteve Mariana, Mazet Muriel, Deumer Gladys, Wallemacq Pierre, Michels Paul A.M., Glycosomal ABC transporters of Trypanosoma brucei: Characterisation of their expression, topology and substrate specificity, 10.1016/j.ijpara.2010.11.002
  93. VISSER Nico, OPPERDOES Fred. R., BORST Piet, Subcellular Compartmentation of Glycolytic Intermediates in Trypanosoma brucei, 10.1111/j.1432-1033.1981.tb05550.x
  94. Hammond, J. Biol. Chem., 260, 15646 (1985)
  95. Haanstra J. R., van Tuijl A., Kessler P., Reijnders W., Michels P. A. M., Westerhoff H. V., Parsons M., Bakker B. M., Compartmentation prevents a lethal turbo-explosion of glycolysis in trypanosomes, 10.1073/pnas.0806664105
  96. Bakker B. M., Mensonides F. I. C., Teusink B., van Hoek P., Michels P. A. M., Westerhoff H. V., Compartmentation protects trypanosomes from the dangerous design of glycolysis, 10.1073/pnas.030539197
  97. Gualdron-López Melisa, Vapola Miia H., Miinalainen Ilkka J., Hiltunen J. Kalervo, Michels Paul A. M., Antonenkov Vasily D., Channel-Forming Activities in the Glycosomal Fraction from the Bloodstream Form of Trypanosoma brucei, 10.1371/journal.pone.0034530
  98. Reumann S., The Structural Properties of Plant Peroxisomes and Their Metabolic Significance, 10.1515/bc.2000.084
  99. Antonenkov Vasily D., Hiltunen J. Kalervo, Transfer of metabolites across the peroxisomal membrane, 10.1016/j.bbadis.2011.12.011
  100. Moyersoen Juliette, Choe Jungwoo, Fan Erkang, Hol Wim G.J., Michels Paul A.M., Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target, 10.1016/j.femsre.2004.06.004
  101. Galland Nathalie, Michels Paul A.M., Comparison of the peroxisomal matrix protein import system of different organisms. Exploration of possibilities for developing inhibitors of the import system of trypanosomatids for anti-parasite chemotherapy, 10.1016/j.ejcb.2010.04.001
  102. Rokka Aare, Antonenkov Vasily D., Soininen Raija, Immonen Hanna L., Pirilä Päivi L., Bergmann Ulrich, Sormunen Raija T., Weckström Matti, Benz Roland, Hiltunen J. Kalervo, Pxmp2 Is a Channel-Forming Protein in Mammalian Peroxisomal Membrane, 10.1371/journal.pone.0005090
  103. Duszenko Michael, Ginger Michael L., Brennand Ana, Gualdrón-López Melisa, Colombo María Isabel, Coombs Graham H., Coppens Isabelle, Jayabalasingham Bamini, Langsley Gordon, Lisboa de Castro Solange, Menna-Barreto Rubem, Mottram Jeremy C., Navarro Miguel, Rigden Daniel J., Romano Patricia S., Stoka Veronika, Turk Boris, Michels Paul A.M., Autophagy in protists, 10.4161/auto.7.2.13310
  104. Brennand Ana, Gualdrón-López Melisa, Coppens Isabelle, Rigden Daniel J., Ginger Michael L., Michels Paul A.M., Autophagy in parasitic protists: Unique features and drug targets, 10.1016/j.molbiopara.2011.02.003
  105. Herman Murielle, Pérez-Morga David, Schtickzelle Nicolas, Michels Paul A.M., Turnover of glycosomes during life-cycle differentiation ofTrypanosoma brucei, 10.4161/auto.5443
  106. Herman Murielle, Gillies Stuart, Michels Paul A., Rigden Daniel J., Autophagy and Related processes in Trypanosomatids: Insights from Genomic and Bioinformatic Analyses, 10.4161/auto.2.2.2369
  107. Eakin, Antimicrob. Agents Chemother., 41, 1686 (1997)
  108. Monzani Paulo S, Trapani Stefano, Thiemann Otavio H, Oliva Glaucius, Crystal structure of Leishmania tarentolae hypoxanthine-guanine phosphoribosyltransferase, 10.1186/1472-6807-7-59
  109. Shaw Matthew P., Bond Charles S., Roper Janine R., Gourley David G., Ferguson Michael A.J., Hunter William N., High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: a potential target for structure-based development of novel trypanocides, 10.1016/s0166-6851(02)00243-8
  110. Willson Michèle, Callens Mia, Kuntz Douglas A., Perié Jacques, Opperdoes Fred R., Synthesis and activity of inhibitors highly specific for the glycolytic enzymes from Trypanosoma brucei, 10.1016/0166-6851(93)90218-m
  111. Morgan Hugh P., McNae Iain W., Nowicki Matthew W., Zhong Wenhe, Michels Paul A. M., Auld Douglas S., Fothergill-Gilmore Linda A., Walkinshaw Malcolm D., The Trypanocidal Drug Suramin and Other Trypan Blue Mimetics Are Inhibitors of Pyruvate Kinases and Bind to the Adenosine Site, 10.1074/jbc.m110.212613
  112. Nowicki Matthew W., Tulloch Lindsay B., Worralll Liam, McNae Iain W., Hannaert Véronique, Michels Paul A.M., Fothergill-Gilmore Linda A., Walkinshaw Malcolm D., Turner Nicholas J., Design, synthesis and trypanocidal activity of lead compounds based on inhibitors of parasite glycolysis, 10.1016/j.bmc.2008.03.045
  113. Dax Chantal, Duffieux Francis, Chabot Nicolas, Coincon Mathieu, Sygusch Jurgen, Michels Paul A. M., Blonski Casimir, Selective Irreversible Inhibition of Fructose 1,6-Bisphosphate Aldolase fromTrypanosoma brucei, 10.1021/jm050237b
  114. Azéma Laurent, Lherbet Christian, Baudoin Cécile, Blonski Casimir, Cell permeation of a Trypanosoma brucei aldolase inhibitor: Evaluation of different enzyme-labile phosphate protecting groups, 10.1016/j.bmcl.2006.04.010
  115. Aronov A. M., Suresh S., Buckner F. S., Van Voorhis W. C., Verlinde C. L. M. J., Opperdoes F. R., Hol W. G. J., Gelb M. H., Structure-based design of submicromolar, biologically active inhibitors of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase, 10.1073/pnas.96.8.4273
  116. Bressi Jerome C., Verlinde Christophe L. M. J., Aronov Alex M., Shaw My Le, Shin Sam S., Nguyen Lisa N., Suresh Stephen, Buckner Frederick S., Van Voorhis Wesley C., Kuntz Irwin D., Hol Wim G. J., Gelb Michael H., Adenosine Analogues as Selective Inhibitors of Glyceraldehyde-3-phosphate Dehydrogenase ofTrypanosomatidaevia Structure-Based Drug Design, 10.1021/jm000472o
  117. Kennedy Kevin J, Bressi Jerome C, Gelb Michael H, A disubstituted NAD + analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase, 10.1016/s0960-894x(00)00608-9
  118. Bressi Jerome C., Choe Jungwoo, Hough Melinda T., Buckner Frederick S., Van Voorhis Wesley C., Verlinde Christophe L. M. J., Hol Wim G. J., Gelb Michael H., Adenosine Analogues as Inhibitors ofTrypanosomabruceiPhosphoglycerate Kinase:  Elucidation of a Novel Binding Mode for a 2-Amino-N6-Substituted Adenosine, 10.1021/jm000287a
  119. Sharlow Elizabeth R., Lyda Todd A., Dodson Heidi C., Mustata Gabriela, Morris Meredith T., Leimgruber Stephanie S., Lee Kuo-Hsiung, Kashiwada Yoshiki, Close David, Lazo John S., Morris James C., A Target-Based High Throughput Screen Yields Trypanosoma brucei Hexokinase Small Molecule Inhibitors with Antiparasitic Activity, 10.1371/journal.pntd.0000659
  120. Chambers Jeremy W., Kearns Margaret T., Morris Meredith T., Morris James C., Assembly of Heterohexameric Trypanosome Hexokinases Reveals That Hexokinase 2 Is a Regulable Enzyme, 10.1074/jbc.m802124200
  121. Montalvetti Andrea, Bailey Brian N., Martin Michael B., Severin Gregory W., Oldfield Eric, Docampo Roberto, Bisphosphonates Are Potent Inhibitors ofTrypanosoma cruziFarnesyl Pyrophosphate Synthase, 10.1074/jbc.m103950200
  122. Hudock Michael P., Sanz-Rodríguez C. E., Song Yongcheng, Chan Julian M. W., Zhang Yonghui, Odeh Sarah, Kosztowski Thomas, Leon-Rossell Annette, Concepción J. L., Yardley Vanessa, Croft Simon L., Urbina Julio A., Oldfield Eric, Inhibition ofTrypanosomacruziHexokinase by Bisphosphonates, 10.1021/jm0582625
  123. Sanz-Rodríguez Carlos E., Concepción Juan L., Pekerar Sara, Oldfield Eric, Urbina Julio A., Bisphosphonates as Inhibitors ofTrypanosoma cruziHexokinase : KINETIC AND METABOLIC STUDIES, 10.1074/jbc.m607286200
  124. Orenes Lorente Silvia, Gómez Rosario, Jiménez Carmen, Cammerer Simon, Yardley Vanessa, de Luca-Fradley Kate, Croft Simon L., Ruiz Perez Luis M., Urbina Julio, Gonzalez Pacanowska Dolores, Gilbert Ian H., Biphenylquinuclidines as inhibitors of squalene synthase and growth of parasitic protozoa, 10.1016/j.bmc.2005.02.060
  125. Sealey-Cardona M., Cammerer S., Jones S., Ruiz-Perez L. M., Brun R., Gilbert I. H., Urbina J. A., Gonzalez-Pacanowska D., Kinetic Characterization of Squalene Synthase from Trypanosoma cruzi: Selective Inhibition by Quinuclidine Derivatives, 10.1128/aac.01454-06
  126. Urbina J. A., Concepcion J. L., Caldera A., Payares G., Sanoja C., Otomo T., Hiyoshi H., In Vitro and In Vivo Activities of E5700 and ER-119884, Two Novel Orally Active Squalene Synthase Inhibitors, against Trypanosoma cruzi, 10.1128/aac.48.7.2379-2387.2004
  127. Urbina J. A., Concepcion J. L., Montalvetti A., Rodriguez J. B., Docampo R., Mechanism of Action of 4-Phenoxyphenoxyethyl Thiocyanate (WC-9) against Trypanosoma cruzi, the Causative Agent of Chagas' Disease, 10.1128/aac.47.6.2047-2050.2003
  128. Wilkinson S. R., Meyer D. J., Taylor M. C., Bromley E. V., Miles M. A., Kelly J. M., The Trypanosoma cruzi Enzyme TcGPXI Is a Glycosomal Peroxidase and Can Be Linked to Trypanothione Reduction by Glutathione or Tryparedoxin, 10.1074/jbc.m111126200
  129. Wilkinson S. R., Kelly J. M., The Role of Glutathione Peroxidases in Trypanosomatids, 10.1515/bc.2003.060
  130. Gutierrez-Correa Jose, Fairlamb Alan H., Stoppani Andres O.M., Trypanosoma Cruzitrypanothione reductase is inactivated by peroxidase-generated phenothiazine cationic radicals, 10.1080/10715760100300311
  131. W. Rivarola, A. R. Fernandez, J. E. H., Thioridazine treatment modifies the evolution of Trypanosoma cruzi infection in mice, 10.1080/00034989957943
  132. Lo Presti M.S, Rivarola H.W, Bustamante J.M, Fernández A.R, Enders J.E, Fretes R, Gea S, Paglini-Oliva P.A, Thioridazine treatment prevents cardiopathy in Trypanosoma cruzi infected mice, 10.1016/j.ijantimicag.2003.10.006
  133. Ruda Gian Filippo, Wong Pui Ee, Alibu Vincent P., Norval Suzanne, Read Kevin D., Barrett Michael P., Gilbert Ian H., Aryl Phosphoramidates of 5-Phospho Erythronohydroxamic Acid, A New Class of Potent Trypanocidal Compounds, 10.1021/jm1004754
  134. Marr J.Joseph, Berens Randolph L., Pyrazolopyrimidine metabolism in the pathogenic trypanosomatidae, 10.1016/0166-6851(83)90016-6
  135. Ullman Buddy, Carter Darrick, Molecular and biochemical studies on the hypoxanthine-guanine phosphoribosyltransferases of the pathogenic haemoflagellates, 10.1016/s0020-7519(96)00150-6
  136. Koutinas Alexander F, Saridomichelakis Manolis N, Mylonakis Mathios E, Leontides Leonidas, Polizopoulou Zoe, Billinis Charalambos, Argyriadis Dimitris, Diakou Natasa, Papadopoulos Orestis, A randomised, blinded, placebo-controlled clinical trial with allopurinol in canine leishmaniosis, 10.1016/s0304-4017(01)00399-5
  137. Torres Marta, Bardagí Mar, Roura Xavier, Zanna Giordana, Ravera Iván, Ferrer Lluís, Long term follow-up of dogs diagnosed with leishmaniosis (clinical stage II) and treated with meglumine antimoniate and allopurinol, 10.1016/j.tvjl.2010.05.025
  138. Gobbi Paola, Lo Presti María S., Fernández Alicia R., Enders Julio E., Fretes Ricardo, Gea Susana, Paglini-Oliva Patricia A., Rivarola Héctor W., Allopurinol is effective to modify the evolution of Trypanosoma cruzi infection in mice, 10.1007/s00436-007-0644-2
  139. Apt W, Pérez C, Rodriguez J, Zulantay I, Juri D, Miranda C, Aguilera X, Arribada A, Cortés P, Sánchez G, Treatment of chronic Chagas' disease with itraconazole and allopurinol., 10.4269/ajtmh.1998.59.133
  140. Freymann Douglas M, Wenck Mary Anne, Engel Juan C, Feng Jun, Focia Pamela J, Eakin Ann E, Craig Sydney P, Efficient identification of inhibitors targeting the closed active site conformation of the HPRT from Trypanosoma cruzi, 10.1016/s1074-5521(00)00045-4