Publications

Atwood JA III, Weatherly DB, Minning TA, Bundy B, et al. (2005). The Trypanosoma cruzi proteome. Science 309: 473-476. http://dx.doi.org/10.1126/science.1110289 PMid:16020736   Cano MI, Gruber A, Vazquez M, Cortes A, et al. (1995). Molecular karyotype of clone CL Brener chosen for the Trypanosoma cruzi genome project. Mol. Biochem. Parasitol. 71: 273-278. http://dx.doi.org/10.1016/0166-6851(95)00066-A   Coura JR and Borges-Pereira J (2010). Chagas disease: 100 years after its discovery. A systemic review. Acta Trop. 115: 5-13. http://dx.doi.org/10.1016/j.actatropica.2010.03.008 PMid:20382097   de Carvalho EF, de Castro FT, Rondinelli E, Soares CM, et al. (1990). HSP 70 gene expression in Trypanosoma cruzi is regulated at different levels. J. Cell Physiol. 143: 439-444. http://dx.doi.org/10.1002/jcp.1041430306 PMid:2193034   Doyle SM and Wickner S (2009). Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 34: 40-48. http://dx.doi.org/10.1016/j.tibs.2008.09.010 PMid:19008106   Dragon EA, Sias SR, Kato EA and Gabe JD (1987). The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein. Mol. Cell Biol. 7: 1271-1275. PMid:3550435 PMCid:365202   Drummond AJ, Ashton B, Buxton S, Cheung M, et al (2011). Geneious v5.4. Geneious. Available at [http://www.geneious.com]. Accessed July 24, 2011.   Engman DM, Kirchhoff LV and Donelson JE (1989). Molecular cloning of mtp70, a mitochondrial member of the hsp70 family. Mol. Cell Biol. 9: 5163-5168. PMid:2689873 PMCid:363668   Eswar N, Webb B, Marti-Renom MA, Madhusudhan MS, et al. (2007). Comparative protein structure modeling using MODELLER. Curr. Protoc. Protein Sci. Chapter 2: Unit.   Eswar N, Eramian D, Webb B, Shen MY, et al. (2008). Protein structure modeling with MODELLER. Methods Mol. Biol. 426: 145-159. http://dx.doi.org/10.1007/978-1-60327-058-8_8 PMid:18542861   Fernandes M, Silva R, Rossle SC, Bisch PM, et al. (2005). Gene characterization and predicted protein structure of the mitochondrial chaperonin HSP10 of Trypanosoma cruzi. Gene 349: 135-142. http://dx.doi.org/10.1016/j.gene.2004.11.047 PMid:15780998   Folgueira C and Requena JM (2007). A postgenomic view of the heat shock proteins in kinetoplastids. FEMS Microbiol. Rev. 31: 359-377. http://dx.doi.org/10.1111/j.1574-6976.2007.00069.x PMid:17459115   Giambiagi-de Marval M, Gottesdiener K, Rondinelli E and Van der Ploeg LH (1993). Predicted amino acid sequence and genomic organization of Trypanosoma cruzi hsp 60 genes. Mol. Biochem. Parasitol. 58: 25-31. http://dx.doi.org/10.1016/0166-6851(93)90087-E   Gottesman S, Squires C, Pichersky E, Carrington M, et al. (1990). Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes. Proc. Natl. Acad. Sci. U. S. A. 87: 3513-3517. http://dx.doi.org/10.1073/pnas.87.9.3513 PMid:2185473 PMCid:53931   Guex N and Peitsch MC (1997). SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18: 2714-2723. http://dx.doi.org/10.1002/elps.1150181505 PMid:9504803   Hartl FU and Hayer-Hartl M (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858. http://dx.doi.org/10.1126/science.1068408 PMid:11884745   Hübel A, Brandau S, Dresel A and Clos J (1995). A member of the ClpB family of stress proteins is expressed during heat shock in Leishmania spp. Mol. Biochem. Parasitol. 70: 107-118. http://dx.doi.org/10.1016/0166-6851(95)00012-P   Humphrey W, Dalke A and Schulten K (1996). VMD: visual molecular dynamics. J. Mol. Graph. 14: 33-38. http://dx.doi.org/10.1016/0263-7855(96)00018-5   Kim KS, Teixeira SM, Kirchhoff LV and Donelson JE (1994). Transcription and editing of cytochrome oxidase II RNAs in Trypanosoma cruzi. J. Biol. Chem. 269: 1206-1211. PMid:8288582   Krobitsch S, Brandau S, Hoyer C, Schmetz C, et al. (1998). Leishmania donovani heat shock protein 100. Characterization and function in amastigote stage differentiation. J. Biol. Chem. 273: 6488-6494. http://dx.doi.org/10.1074/jbc.273.11.6488 PMid:9497383   Laskowski RA, Moss DS and Thornton JM (1993). Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231: 1049-1067. http://dx.doi.org/10.1006/jmbi.1993.1351 PMid:8515464   Lee S, Sowa ME, Watanabe YH, Sigler PB, et al. (2003). The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115: 229-240. http://dx.doi.org/10.1016/S0092-8674(03)00807-9   Martí-Renom MA, Stuart AC, Fiser A, Sanchez R, et al. (2000). Comparative protein structure modeling of genes and genomes. Annu. Rev. Biophys. Biomol. Struct. 29: 291-325. http://dx.doi.org/10.1146/annurev.biophys.29.1.291 PMid:10940251   Pérez-Morales D, Ostoa-Saloma P and Espinoza B (2009). Trypanosoma cruzi SHSP16: Characterization of an alpha-crystallin small heat shock protein. Exp. Parasitol. 123: 182-189. http://dx.doi.org/10.1016/j.exppara.2009.06.019 PMid:19595996   Rodrigues DC, Silva R, Rondinelli E and Urmenyi TP (2010). Trypanosoma cruzi: modulation of HSP70 mRNA stability by untranslated regions during heat shock. Exp. Parasitol. 126: 245-253. http://dx.doi.org/10.1016/j.exppara.2010.05.009 PMid:20493845   Rondinelli E (1994). Conservation of heat-shock proteins in Trypanosoma cruzi. Parasitol. Today 10: 172-176. http://dx.doi.org/10.1016/0169-4758(94)90020-5   Sali A and Blundell TL (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234: 779-815. http://dx.doi.org/10.1006/jmbi.1993.1626 PMid:8254673   Schrödinger LCC (2011). The PyMol Molecular Graphics System. Version 1.3. pymol.org. Available at [http://www.pymol.org/]. Accessed August 22, 2011.   Vonlaufen N, Kanzok SM, Wek RC and Sullivan WJ Jr (2008). Stress response pathways in protozoan parasites. Cell Microbiol. 10: 2387-2399. http://dx.doi.org/10.1111/j.1462-5822.2008.01210.x PMid:18647172