4 24 15 Biochemistry 1990, 29:10323–9 PubMedCrossRef 51 Niemiro

4.24.15. Biochemistry 1990, 29:10323–9.H 89 datasheet PubMedCrossRef 51. Niemirowicz G, Parussini F, Agüero F, Cazzulo JJ: Two metallocarboxypeptidases from the protozoan Trypanosoma cruzi belong to the M32 family, Selleck Doramapimod found so far only in prokaryotes. Biochem J 2007, 401:399–410.PubMedCrossRef 52. Doucet A, Butler GS, Rodriguez D, Prudova A, Overall CM: Quantitative degradomics analysis of proteolytic post-translational modifications of the cancer proteome. Mol Cell Proteomics 2008, 7:1925–1951.PubMedCrossRef 53. Pellé

R, Schramm VL, Parkin DW: Molecular cloning and expression of a purine-specific N-ribohydrolase from Trypanosoma brucei brucei . Sequence, expression, and molecular analysis. J Biol Chem 1998, 273:2118–26.PubMedCrossRef 54. Di Virgilio F, Chiozzi P, Ferrari selleck products D, Falzoni S, Sanz JM, Morelli A, Torboli M, Bolognesi G, Baricordi OR: Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood 2001, 97:587–600.PubMedCrossRef 55. Haskó G, Cronstein : Adenosine: an endogenous regulator of innate immunity. Trends Immunol 2004, 25:33–9.PubMedCrossRef 56. Ribeiro JM, Valenzuela JG: The salivary purine nucleosidase of the mosquito, Aedes aegypti

. Insect Biochem Mol Biol 2003, 33:13–22.PubMedCrossRef 57. Gounaris K, Selkirk ME: Parasite nucleotide-metabolizing enzymes and host purinergic signalling. Trends Parasitol 2005, 21:17–21.PubMedCrossRef 58. Opperdoes FR, Borst P: Localization of nine glycolytic enzymes in a microbody-like organelle in Trypanosoma brucei Phospholipase D1 : the glycosome. FEBS Lett 1977, 80:360–4.PubMedCrossRef 59. Albert MA, Haanstra JR, Hannaert V, Van Roy J, Opperdoes FR, Bakker BM, Michels PA: Experimental and in silico analyses of glycolytic flux control in bloodstream form Trypanosoma brucei . J Biol Chem 2005, 280:28306–15.PubMedCrossRef

60. Lay AJ, Jiang XM, Daly E, Sun L, Hogg PJ: Plasmin reduction by phosphoglycerate kinase is a thiol-independent process. J Biol Chem 2002, 277:9062–9068.PubMedCrossRef 61. Veiga-Malta I, Duarte M, Dinis M, Tavares D, Videira A, Ferreira P: Enolase from Streptococcus sobrinus is an immunosuppressive protein. Cell Microbiol 2004, 6:79–88.PubMedCrossRef 62. Huang LJ, Chen SX, Luo WJ, Jiang HH, Zhang PF, Yi H: Proteomic analysis of secreted proteins of non-small cell lung cancer. Ai Zheng 2006, 25:1361–7.PubMed 63. Labbé M, Péroval M, Bourdieu C, Girard-Misguich F, Péry P: Eimeria tenella enolase and pyruvate kinase: a likely role in glycolysis and in others functions. Int J Parasitol 2006, 36:1443–52.PubMedCrossRef 64. Rokeach LA, Zimmerman PA, Unnasch TR: Epitopes of the Onchocerca volvulus RAL1 antigen, a member of the calreticulin family of proteins, recognized by sera from patients with onchocerciasis. Infect Immun 1994, 62:3696–704.PubMed 65. Dupuis M, Schaerer E, Krause KH, Tschopp J: The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J Exp Med 1993, 177:1–7.

Comments are closed.