Registro:

Referencias:

• Trouiller, P., Olliaro, P., Torreele, E., Orbinski, J., Laing, R., Drug development for neglected diseases: A deficient market and a public-health policy failure (2002) Lancet, 359, pp. 2188-2194
• Hotez, P.J.P., Molyneux, D.D.H., Fenwick, A., Kumaresan, J., Sachs, S.E., Control of neglected tropical diseases (2007) N Engl J Med, 357, pp. 1018-1027
• Buscaglia, C.A., Kissinger, J.C., Agüero, F., Neglected Tropical Diseases in the Post-Genomic Era (2015) Trends Genet, 31, pp. 539-555
• Wyatt, P.G., Gilbert, I.H., Read, K.D., Fairlamb, A.H., Target validation: linking target and chemical properties to desired product profile (2011) Curr Top Med Chem, 11, pp. 1275-1283
• DiMasi, J.A., Hansen, R.W., Grabowski, H.G., The price of innovation: new estimates of drug development costs (2003) J Heal Econ, 22, pp. 151-185
• Kola, I., Landis, J., Can the pharmaceutical industry reduce attrition rates (2004) Nat Rev Drug Discov, 3, pp. 711-715
• Robertson, S.A., Renslo, A.R., Drug discovery for neglected tropical diseases at the Sandler Center (2011) Futur Med Chem, 3, pp. 1279-1288
• Kesselheim, A.S., Darrow, J.J., Drug development and FDA approval, 1938–2013 (2014) N Engl J Med, 370, p. 39
• Ashburn, T.T., Thor, K.B., Drug repositioning: identifying and developing new uses for existing drugs (2004) Nat Rev Drug Discov, 3, pp. 673-683
• Chong, C.R., Sullivan, D.J., Jr., New uses for old drugs (2007) Nature, 448, pp. 645-646
• Novac, N., Challenges and opportunities of drug repositioning (2013) Trends Pharmacol Sci, 34, pp. 267-272
• Teo, S.K., Resztak, K.E., Scheffler, M.A., Kook, K.A., Zeldis, J.B., Thalidomide in the treatment of leprosy (2002) Microbes Infect, 4, pp. 1193-1202
• Haupt, V.J., Schroeder, M., Old friends in new guise: repositioning of known drugs with structural bioinformatics (2011) Br Bioinform, 12, pp. 312-326
• Pollastri, M.P., Campbell, R.K., Target repurposing for neglected diseases (2011) Futur Med Chem, 3, pp. 1307-1315
• Jin, G., Wong, S.T.C., Toward better drug repositioning: prioritizing and integrating existing methods into efficient pipelines (2014) Drug Discov Today, 19, pp. 637-644
• Campillos, M., Kuhn, M., Gavin, A.-C., Jensen, L.J., Bork, P., Drug target identification using side-effect similarity (2008) Science, 321, pp. 263-266
• Keiser, M.J., Roth, B.L., Armbruster, B.N., Ernsberger, P., Irwin, J.J., Relating protein pharmacology by ligand chemistry (2007) Nat Biotechnol, 25, pp. 197-206
• Keiser, M.J., Setola, V., Irwin, J.J., Laggner, C., Abbas, A.I., Predicting new molecular targets for known drugs (2009) Nature, 462, pp. 175-181
• Iorio, F., Bosotti, R., Scacheri, E., Belcastro, V., Mithbaokar, P., Discovery of drug mode of action and drug repositioning from transcriptional responses (2010) Proc Natl Acad Sci U S A, 107, pp. 14621-14626
• Meslamani, J., Bhajun, R., Martz, F., Rognan, D., Computational profiling of bioactive compounds using a target-dependent composite workflow (2013) J Chem Inf Model, 53, pp. 2322-2333
• Parkkinen, J.A., Kaski, S., Probabilistic drug connectivity mapping (2014) BMC Bioinformatics, 15, p. 113
• Iskar, M., Zeller, G., Blattmann, P., Campillos, M., Kuhn, M., Characterization of drug-induced transcriptional modules: towards drug repositioning and functional understanding (2013) Mol Syst Biol, 9, p. 662
• Emig, D., Ivliev, A., Pustovalova, O., Lancashire, L., Bureeva, S., Drug target prediction and repositioning using an integrated network-based approach (2013) PLoS One, 8, p. 60618
• Lo, Y.-C., Senese, S., Li, C.-M., Hu, Q., Huang, Y., Large-Scale Chemical Similarity Networks for Target Profiling of Compounds Identified in Cell-Based Chemical Screens (2015) PLoS Comput Biol, 11, p. 1004153
• Kruger, F.A., Overington, J.P., Global analysis of small molecule binding to related protein targets (2012) PLoS Comput Biol, 8, p. 1002333
• Agüero, F., Al-Lazikani, B., Aslett, M., Berriman, M., Buckner, F.S., Genomic-scale prioritization of drug targets: the TDR Targets database (2008) Nat Rev Drug Discov, 7, pp. 900-907
• Crowther, G.J., Shanmugam, D., Carmona, S.J., Doyle, M.A., Hertz-Fowler, C., Identification of attractive drug targets in neglected-disease pathogens using an [i]in silico[/i] approach (2010) PLoS Negl Trop Dis, 4, p. 804
• Magariños, M.P., Carmona, S.J., Crowther, G.J., Ralph, S.A., Roos, D.S., TDR Targets: a chemogenomics resource for neglected diseases (2012) Nucleic Acids Res, 40, pp. 1118-1127
• Gamo, F.-J., Sanz, L.M., Vidal, J., de Cozar, C., Alvarez, E., Thousands of chemical starting points for antimalarial lead identification (2010) Nature, 465, pp. 305-310
• Guiguemde, W.A., Shelat, A.A., Bouck, D., Duffy, S., Crowther, G.J., Chemical genetics of Plasmodium falciparum (2010) Nature, 465, pp. 311-315
• Spangenberg, T., Burrows, J.N., Kowalczyk, P., McDonald, S., Wells, T.N.C., The open access malaria box: a drug discovery catalyst for neglected diseases (2013) PLoS One, 8, p. 62906
• Cheng, F., Liu, C., Jiang, J., Lu, W., Li, W., Prediction of drug-target interactions and drug repositioning via network-based inference (2012) PLoS Comput Biol, 8, p. 1002503
• Alaimo, S., Pulvirenti, A., Giugno, R., Ferro, A., Drug-target interaction prediction through domain-tuned network-based inference (2013) Bioinformatics, 29, pp. 2004-2008
• Csermely, P., Agoston, V., Pongor, S., The efficiency of multi-target drugs: the network approach might help drug design (2005) Trends Pharmacol Sci, 26, pp. 178-182
• Harrold, J.M., Ramanathan, M., Mager, D.E., Network-based approaches in drug discovery and early development (2013) Clin Pharmacol Ther, 94, pp. 651-658
• Yabuuchi, H., Niijima, S., Takematsu, H., Ida, T., Hirokawa, T., Analysis of multiple compound-protein interactions reveals novel bioactive molecules (2011) Mol Syst Biol, 7, p. 472
• Yamanishi, Y., Kotera, M., Kanehisa, M., Goto, S., Drug-target interaction prediction from chemical, genomic and pharmacological data in an integrated framework (2010) Bioinformatics, 26, pp. 246-254
• van Laarhoven, T., Marchiori, E., Predicting Drug-Target Interactions for New Drug Compounds Using a Weighted Nearest Neighbor Profile (2013) PLoS One, 8, p. 66952
• Martínez-Jiménez, F., Marti-Renom, M.A., Ligand-Target Prediction by Structural Network Biology Using nAnnoLyze (2015) PLOS Comput Biol, 11, p. 1004157
• Yamanishi, Y., Kotera, M., Moriya, Y., Sawada, R., Kanehisa, M., DINIES: drug-target interaction network inference engine based on supervised analysis (2014) Nucleic Acids Res, 42, pp. 39-45
• Jones, P., Binns, D., Chang, H.-Y., Fraser, M., Li, W., InterProScan 5: genome-scale protein function classification (2014) Bioinformatics, 30, pp. 1236-1240
• Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M., KEGG for integration and interpretation of large-scale molecular data sets (2012) Nucleic Acids Res, 40, pp. 109-114
• Chen, F., Mackey, A.J., Stoeckert, C.J., Jr., Roos, D.S., OrthoMCL-DB: querying a comprehensive multi-species collection of ortholog groups (2006) Nucleic Acids Res, 34, pp. 363-368
• Fischer, S., Brunk, B.P., Chen, F., Gao, X., Harb, O.S., Using OrthoMCL to Assign Proteins to OrthoMCL-DB Groups or to Cluster Proteomes Into New Ortholog Groups (2011) Curr Protoc Bioinforma
• Gaulton, A., Bellis, L.J., Bento, A.P., Chambers, J., Davies, M., ChEMBL: a large-scale bioactivity database for drug discovery (2012) Nucleic Acids Res, 40, pp. 1100-1107
• Haider, N., Functionality pattern matching as an efficient complementary structure/reaction search tool: an open-source approach (2010) Molecules, 15, pp. 5079-5092
• Willett, P., Barnard, J.M., Downs, G.M., (1998) Chemical Similarity Searching. J Chem Inf Model, 38, pp. 983-996
• Baldi, P., Nasr, R., When is chemical similarity significant? the statistical distribution of chemical similarity scores and its extreme values (2010) J Chem Inf Model, 50, pp. 1205-1222
• Martin, Y.C., Kofron, J.L., Traphagen, L.M., Do structurally similar molecules have similar biological activity? (2002) J Med Chem, 45, pp. 4350-4358
• Law, V., Knox, C., Djoumbou, Y., Jewison, T., Guo, A.C., DrugBank 4.0: shedding new light on drug metabolism (2014) Nucleic Acids Res, 42, pp. 1091-1097
• Finn, R.D., Bateman, A., Clements, J., Coggill, P., Eberhardt, R.Y., Pfam: The protein families database (2014) Nucleic Acids Res, 42
• Li, L., Stoeckert, C.J., Roos, D.S., OrthoMCL: identification of ortholog groups for eukaryotic genomes (2003) Genome Res, 13, pp. 2178-2189
• Chen, F., Mackey, A.J., Vermunt, J.K., Roos, D.S., Assessing performance of orthology detection strategies applied to eukaryotic genomes (2007) PLoS One, 2, p. 383
• Faust, K., Centrality in affiliation networks (1997) Soc Networks, 19, pp. 157-191
• Newman, M., (2010) Networks: An Introduction
• Pearson, W.R., Flexible sequence similarity searching with the FASTA3 program package (2000) Methods Mol Biol, 132, pp. 185-219
• McClish, D.K., Analyzing a portion of the ROC curve (1989) Med Decis Making, 9, pp. 190-195
• Gillis, J., Pavlidis, P., The role of indirect connections in gene networks in predicting function (2011) Bioinformatics, 27, pp. 1860-1866
• Nabieva, E., Jim, K., Agarwal, A., Chazelle, B., Singh, M., Whole-proteome prediction of protein function via graph-theoretic analysis of interaction maps (2005) Bioinformatics, 21, pp. 302-310
• Kissinger, J.C., A tale of three genomes: the kinetoplastids have arrived (2006) Trends Parasitol, 22, pp. 240-243
• Hanks, S., Hunter, T., Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification (1995) FASEB J, 9, pp. 576-596
• Knight, Z.A., Lin, H., Shokat, K.M., Targeting the cancer kinome through polypharmacology (2010) Nat Rev Cancer, 10, pp. 130-137
• Bao, Y., Weiss, L.M., Braunstein, V.L., Huang, H., Role of protein kinase A in Trypanosoma cruzi (2008) Infect Immun, 76, pp. 4757-4763
• Bao, Y., Weiss, L.M., Ma, Y.F., Kahn, S., Huang, H., Protein kinase A catalytic subunit interacts and phosphorylates members of trans-sialidase super-family in Trypanosoma cruzi (2010) Microbes Infect, 12, pp. 716-726
• Allocco, J.J., Donald, R., Zhong, T., Lee, A., Tang, Y.S., Inhibitors of casein kinase 1 block the growth of Leishmania major promastigotes in vitro (2006) Int J Parasitol, 36, pp. 1249-1259
• Marhadour, S., Marchand, P., Pagniez, F., Bazin, M.-A., Picot, C., Synthesis and biological evaluation of 2,3-diarylimidazo[1,2-a]pyridines as antileishmanial agents (2012) Eur J Med Chem, 58, pp. 543-556
• Spadafora, C., Repetto, Y., Torres, C., Pino, L., Robello, C., Two casein kinase 1 isoforms are differentially expressed in Trypanosoma cruzi Mol Biochem Parasitol, 124, pp. 23-36
• Knockaert, M., Gray, N., Damiens, E., Chang, Y.T., Grellier, P., Intracellular targets of cyclin-dependent kinase inhibitors: identification by affinity chromatography using immobilised inhibitors (2000) Chem Biol, 7, pp. 411-422
• Bao, Y., Weiss, L.M., Ma, Y.F., Lisanti, M.P., Tanowitz, H.B., Molecular cloning and characterization of mitogen-activated protein kinase 2 in Trypanosoma cruzi (2010) Cell Cycle, 9, pp. 2888-2896
• Patterson, R.L., Boehning, D., Snyder, S.H., Inositol 1,4,5-trisphosphate receptors as signal integrators (2004) Annu Rev Biochem, 73, pp. 437-465
• Huang, G., Bartlett, P.J., Thomas, A.P., Moreno, S.N.J., Docampo, R., Acidocalcisomes of Trypanosoma brucei have an inositol 1,4,5-trisphosphate receptor that is required for growth and infectivity (2013) Proc Natl Acad Sci U S A, 110, pp. 1887-1892
• Hashimoto, M., Enomoto, M., Morales, J., Kurebayashi, N., Sakurai, T., Inositol 1,4,5-trisphosphate receptor regulates replication, differentiation, infectivity and virulence of the parasitic protist Trypanosoma cruzi (2013) Mol Microbiol, 87, pp. 1133-1150
• Bahia, D., Oliveira, L.M., Lima, F.M., Oliveira, P., Silveira, J.F., The TryPIKinome of five human pathogenic trypanosomatids: Trypanosoma brucei,} rypanosoma cruzi, Leishmania major, Leishmania braziliensis and Leishmania infantum—new tools for designing specific inhibitors (2009) Biochem Biophys Res Commun, 390, pp. 963-970
• Sutherlin, D.P., Bao, L., Berry, M., Castanedo, G., Chuckowree, I., Discovery of a potent, selective, and orally available class I phosphatidylinositol 3-kinase (PI3K)/mammalian target of rapamycin (mTOR) kinase inhibitor (GDC-0980) for the treatment of cancer (2011) J Med Chem, 54, pp. 7579-7587
• Woolsey, A.M., Sunwoo, L., Petersen, C.A., Brachmann, S.M., Cantley, L.C., Novel PI 3-kinase-dependent mechanisms of trypanosome invasion and vacuole maturation (2003) J Cell Sci, 116, pp. 3611-3622
• Andrade, L.O., Andrews, N.W., Lysosomal fusion is essential for the retention of Trypanosoma cruzi inside host cells (2004) J Exp Med, 200, pp. 1135-1143
• Schoijet, A.C., Miranda, K., Girard-Dias, W., de Souza, W., Flawiá, M.M., A Trypanosoma cruzi phosphatidylinositol 3-kinase (TcVps34) is involved in osmoregulation and receptor-mediated endocytosis (2008) J Biol Chem, 283, pp. 31541-31550
• Hashimoto, M., Morales, J., Fukai, Y., Suzuki, S., Takamiya, S., Critical importance of the de novo pyrimidine biosynthesis pathway for Trypanosoma cruzi growth in the mammalian host cell cytoplasm (2012) Biochem Biophys Res Commun, 417, pp. 1002-1006
• Cosentino, R.O., Agüero, F., Genetic Profiling of the Isoprenoid and Sterol Biosynthesis Pathway Genes of Trypanosoma cruzi (2014) PLoS One, 9, p. 96762
• Lepesheva, G.I., Zaitseva, N.G., Nes, W.D., Zhou, W., Arase, M., CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B’ helix defines substrate preferences of sterol 14alpha-demethylase (2006) J Biol Chem, 281, pp. 3577-3585
• Lepesheva, G.I., Park, H.-W., Hargrove, T.Y., Vanhollebeke, B., Wawrzak, Z., Crystal structures of Trypanosoma brucei sterol 14alpha-demethylase and implications for selective treatment of human infections (2010) J Biol Chem, 285, pp. 1773-1780
• Andrade-Neto, V.V., Matos-Guedes, H.L., Gomes, D.C.O., Canto-Cavalheiro, M.M., Rossi-Bergmann, B., The stepwise selection for ketoconazole resistance induces upregulation of C14-demethylase (CYP51) in Leishmania amazonensis (2012) Mem Inst Oswaldo Cruz, 107, pp. 416-419
• Tate, E.W., Bell, A.S., Rackham, M.D., Wright, M.H., N-Myristoyltransferase as a potential drug target in malaria and leishmaniasis (2014) Parasitology, 141, pp. 37-49
• Sheng, C., Zhu, J., Zhang, W., Zhang, M., Ji, H., 3D-QSAR and molecular docking studies on benzothiazole derivatives as Candida albicans N-myristoyltransferase inhibitors (2007) Eur J Med Chem, 42, pp. 477-486
• Rackham, M.D., Brannigan, J.A., Rangachari, K., Meister, S., Wilkinson, A.J., Design and synthesis of high affinity inhibitors of Plasmodium falciparum and Plasmodium vivax N-myristoyltransferases directed by ligand efficiency dependent lipophilicity (LELP) (2014) J Med Chem, 57, pp. 2773-2788
• Wright, M.H., Clough, B., Rackham, M.D., Rangachari, K., Brannigan, J.A., Validation of N -myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach (2014) Nat Chem, 6, pp. 112-121
• Bowyer, P.W., Gunaratne, R.S., Grainger, M., Withers-Martinez, C., Wickramsinghe, S.R., Molecules incorporating a benzothiazole core scaffold inhibit the N-myristoyltransferase of Plasmodium falciparum (2007) Biochem J, 408, pp. 173-180
• Calí, P., Naerum, L., Mukhija, S., Hjelmencrantz, A., Isoxazole-3-hydroxamic acid derivatives as peptide deformylase inhibitors and potential antibacterial agents (2004) Bioorg Med Chem Lett, 14, pp. 5997-6000
• Wiesner, J., Sanderbrand, S., Altincicek, B., Beck, E., Jomaa, H., Seeking new targets for antiparasitic agents (2001) Trends Parasitol, 17, pp. 7-8
• Hynes, J.B., Hydroxylamine derivatives as potential antimalarial agents. 1. Hydroxamic acids (1970) J Med Chem, 13, pp. 1235-1237
• Gupta, S., (2013) Hydroxamic Acids: A Unique Family of Chemicals with Multiple Biological Activities
• McGowan, S., Sitagliptin does not inhibit the M1 alanyl aminopeptidase from Plasmodium falciparum (2013) Bioinformation, 9, pp. 661-662
• Skinner-Adams, T.S., Stack, C.M., Trenholme, K.R., Brown, C.L., Grembecka, J., Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials (2010) Trends Biochem Sci, 35, pp. 53-61
• Flipo, M., Florent, I., Grellier, P., Sergheraert, C., Deprez-Poulain, R., Design, synthesis and antimalarial activity of novel, quinoline-Based, zinc metallo-aminopeptidase inhibitors (2003) Bioorg Med Chem Lett, 13, pp. 2659-2662
• Harbut, M.B., Velmourougane, G., Dalal, S., Reiss, G., Whisstock, J.C., Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases (2011) Proc Natl Acad Sci U S A, 108, pp. 526-534
• Kannan, S.K., Paiardini, A., Sieńczyk, M., Ruggeri, C., Oellig, C.A., Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum (2013) J Med Chem, 56, pp. 5213-5217
• Poreba, M., McGowan, S., Skinner-Adams, T.S., Trenholme, K.R., Gardiner, D.L., Fingerprinting the substrate specificity of M1 and M17 aminopeptidases of human malaria, Plasmodium falciparum (2012) PLoS One, 7, p. 31938
• Belluti, F., Perozzo, R., Lauciello, L., Colizzi, F., Kostrewa, D., Design, synthesis, and biological and crystallographic evaluation of novel inhibitors of Plasmodium falciparum enoyl-ACP-reductase (PfFabI) (2013) J Med Chem, 56, pp. 7516-7526
• Heerding, D.A., Chan, G., DeWolf, W.E., Fosberry, A.P., Janson, C.A., 1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI) (2001) Bioorg Med Chem Lett, 11, pp. 2061-2065
• am Ende, C.W., Knudson, S.E., Liu, N., Childs, J., Sullivan, T.J., Synthesis and in vitro antimycobacterial activity of B-ring modified diaryl ether InhA inhibitors (2008) Bioorg Med Chem Lett, 18, pp. 3029-3033
• Samal, R.P., Khedkar, V.M., Pissurlenkar, R.R.S., Bwalya, A.G., Tasdemir, D., Design, synthesis, structural characterization by IR, (1) H, (13) C, (15) N, 2D-NMR, X-ray diffraction and evaluation of a new class of phenylaminoacetic acid benzylidene hydrazines as pfENR inhibitors (2013) Chem Biol Drug Des, 81, pp. 715-729
• Schrader, F.C., Glinca, S., Sattler, J.M., Dahse, H.-M., Afanador, G.A., Novel type II fatty acid biosynthesis (FAS II) inhibitors as multistage antimalarial agents (2013) ChemMedChem, 8, pp. 442-461
• Muhammad, A., Anis, I., Ali, Z., Awadelkarim, S., Khan, A., Methylenebissantin: a rare methylene-bridged bisflavonoid from Dodonaea viscosa which inhibits Plasmodium falciparum enoyl-ACP reductase (2012) Bioorg Med Chem Lett, 22, pp. 610-612
• Muench, S.P., Stec, J., Zhou, Y., Afanador, G.A., McPhillie, M.J., Development of a triclosan scaffold which allows for adaptations on both the A- and B-ring for transport peptides (2013) Bioorg Med Chem Lett, 23, pp. 3551-3555
• Guggisberg, A.M., Amthor, R.E., Odom, A.R., Isoprenoid biosynthesis in Plasmodium falciparum (2014) Eukaryot Cell, 13, pp. 1348-1359
• Lindner, S.E., Sartain, M.J., Hayes, K., Harupa, A., Moritz, R.L., Enzymes involved in plastid-targeted phosphatidic acid synthesis are essential for P lasmodium yoelii liver-stage development (2014) Mol Microbiol, 91, pp. 679-693
• Kumar, S., Chaudhary, K., Foster, J.M., Novelli, J.F., Zhang, Y., Mining predicted essential genes of brugia malayi for nematode drug targets (2007) PLoS One, 2, p. 1189
• Chen, Y., Xu, R., Network-based gene prediction for Plasmodium falciparum malaria towards genetics-based drug discovery (2015) BMC Genomics, 16, p. 9
• Morel, C., Ibarz, G., Oiry, C., Carnazzi, E., Bergé, G., Cross-interactions of two p38 mitogen-activated protein (MAP) kinase inhibitors and two cholecystokinin (CCK) receptor antagonists with the CCK1 receptor and p38 MAP kinase (2005) J Biol Chem, 280, pp. 21384-21393
• Rix, U., Hantschel, O., Dürnberger, G., Remsing, R.L.L., Planyavsky, M., Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets (2007) Blood, 110, pp. 4055-4063
• Ross-Macdonald, P., de Silva, H., Guo, Q., Xiao, H., Hung, C.-Y., Identification of a nonkinase target mediating cytotoxicity of novel kinase inhibitors (2008) Mol Cancer Ther, 7, pp. 3490-3498
• Tanaka, M., Bateman, R., Rauh, D., Vaisberg, E., Ramachandani, S., An unbiased cell morphology-based screen for new, biologically active small molecules (2005) PLoS Biol, 3, p. 128
• Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Boesche, M., Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors (2007) Nat Biotechnol, 25, pp. 1035-1044
• Anighoro, A., Bajorath, J., Rastelli, G., Polypharmacology: Challenges and Opportunities in Drug Discovery (2014) J Med Chem, 57, pp. 7874-7887
• Keiser, M.J., Setola, V., Irwin, J.J., Laggner, C., Abbas, A.I., Predicting new molecular targets for known drugs (2009) Nature, 462, pp. 175-181
• Kaiser, M., Mäser, P., Tadoori, L.P., Ioset, J.-R., Brun, R., Antiprotozoal Activity Profiling of Approved Drugs: A Starting Point toward Drug Repositioning (2015) PLoS One, 10, p. 0135556
• Kodadek, T., Rethinking screening (2010) Nat Chem Biol, 6, pp. 162-165
• Arrowsmith, C.H., Audia, J.E., Austin, C., Baell, J., Bennett, J., The promise and peril of chemical probes (2015) Nat Chem Biol, 11, pp. 536-541
• Peña, I., Pilar, M.M., Cantizani, J., Kessler, A., Alonso-Padilla, J., New compound sets identified from high throughput phenotypic screening against three kinetoplastid parasites: an open resource (2015) Sci Rep, 5, p. 8771
• Tsai, I.J., Zarowiecki, M., Holroyd, N., Garciarrubio, A., Sanchez-Flores, A., The genomes of four tapeworm species reveal adaptations to parasitism (2013) Nature, 496, pp. 57-63
• Desjardins, C.A., Cerqueira, G.C., Goldberg, J.M., Dunning, H.J.C., Haas, B.J., Genomics of [i]Loa loa[/i], a Wolbachia-free filarial parasite of humans (2013) Nat Genet, 45, pp. 495-500
• Cwiklinski, K., Dalton, J.P., Dufresne, P.J., La Course, J., Williams, D.J., The [i]Fasciola hepatica[/i] genome: gene duplication and polymorphism reveals adaptation to the host environment and the capacity for rapid evolution (2015) Genome Biol, 16, p. 71
• Carlton, J.M., Hirt, R.P., Silva, J.C., Delcher, A.L., Schatz, M., Draft genome sequence of the sexually transmitted pathogen [i]Trichomonas vaginalis[/i] (2007) Science, 315, pp. 207-212
• Adam, R.D., The Giardia lamblia genome (2000) Int J Parasitol, 30, pp. 475-484
• Franzén, O., Jerlström-Hultqvist, J., Castro, E., Sherwood, E., Ankarklev, J., Draft genome sequencing of giardia intestinalis assemblage B isolate GS: is human giardiasis caused by two different species? (2009) PLoS Pathog, 5, p. 1000560. , http://dx.plos.org/10.1371/journal.ppat.1000560

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------