[1]
Hoare CA. The Trypanosomes of Mammals. Oxford: Blackwell 1972.
[13]
Teixeira DE, Benchimol M, Crepaldi PH, et al. Atlas didático: Ciclo de vida do Trypanosoma cruzi. Rio de Janeiro: Fundação CECIERJ, Consórcio CEDERJ 2011.
[17]
Guhl F. Geographical distribution of Chagas disease. Am. Trypanosom. Chagas Dis 2017; pp. 89-112.
[39]
Gumiel M, Da Mota FF. Characterization of the microbiota in the guts of Triatoma brasiliensis and Triatoma pseudomaculata infected by Trypanosoma cruzi in natural conditions using culture independent methods. Parasit Vectors 2015; 24(8): 245.
[67]
Brenière SF, Waleckx E, Barnabé C. Over Six Thousand Trypanosoma cruzi Strains Classified into Discrete Typing Units (DTUs): Attempt at an Inventory. PLoS Negl Trop Dis 2016; 10(8)e0004792
[91]
Andrade LO, Machado CR, Chiari E, et al. Differential tissue distribution of diverse clones of Trypanosoma cruzi in infected mice. Mol Biochem Parasitol 1999; 100(2): 163-72.
[121]
Moreira-Silva A, Ramirez LE, Vargas M, et al. Evaluation of rabbit as a model for Chagas disease: II histopatological studies of the heart, digestive tract and skeletal muscle. Memorias do Inst. Osw. Cruz 1996; 91: 199-202.
[152]
Oberholzer M, Langousis G, Nguyen HT, et al. Independent Analysis of the Flagellum Surface and Matrix Proteomes Provides Insight into Flagellum Signaling in Mammalian-Infectious Trypanosoma brucei. Mol Cell Proteomics 2011; 10(10)
[182]
Mugo E, Clayton C. Expression of the RNA-binding protein RBP10 promotes the bloodstream-form differentiation state in Trypanosoma brucei. PLoS Pathog 2017; 13(8)e1006560
[195]
Vercesi AE, Bernardes CF, Hoffmann ME, et al. Digitonin permeabilization does not affect mitochondrial function and allows the determination of the mitochondrial membrane potential of Trypanosoma cruzi in situ. J Biol Chem 1991; 2666(22): 14431-4.
[196]
Schneider A. Mitochondrial protein import in trypanosomatids: Variations on a theme or fundamentally different? PLoS Pathog 2018; 14(11)e1007351
[203]
Simpson L. The Mitochondrial Genome of Kinetoplastid Protozoa: Genomic Organization, Transcription, Replication, and Evolution. Ann Rev Microbiol 1987; p. 41.
[210]
Zhao Z, Lindsay ME, Roy Chowdhury A, et al. p166, a link between the trypanosome mitochondrial DNA and flagellum, mediates genome segregation. EMBO J 2008; 27(1): 143-54.
[211]
Schneider A, Ochsenreiter T. Failure is not an option - mitochondrial genome segregation in trypanosomes. J Cell Sci 2018; 131(18)
[213]
Selvapandiyan A, Kumar P, Salisbury JL, et al. Role of Centrins 2 and 3 in Organelle Segregation and Cytokinesis in Trypanosoma brucei. PLoS One 2012; 7(9)
[217]
Li Z, Lindsay ME. Identification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication. PLoS Pathog 2008; 4(4)e1000048
[221]
Cavalcanti DP, Shimada MK, Probst CM, et al. Expression and Subcellular Localization of Kinetoplast-Associated Proteins in the Different Developmental Stages of Trypanosoma cruzi. BMC Microbiol 2009; 9: 120.
[231]
Banerjee H, Knoblach B, Rachubinski RA. The early-acting glycosome biogenic protein Pex3 is essential for trypanosome viability Life Sci Alliance 2019; 2(4).
[259]
Jung G, Titus MA, Hammer JA. The Dictyostelium type V myosin MyoJ is responsible for the cortical association and motility of contractile vacuole membranes. J Cell Biol 2009; 186(4): 555-70.
[261]
Attias M, Vommaro RC, De Souza W. Computer aided threedimensional
reconstruction of the free-living protozoan Bodo sp.
(Kinetoplastida: Bodonidae). Cell Struct Funct 196 21(5): 297-
306.
[277]
Ooi CP, Smith TK, Gluenz E, et al. Blocking variant surface glycoprotein synthesis alters endoplasmic reticulum exit sites/Golgi homeostasis in Trypanosoma brucei. Traffic 2018; 19(6): 391-405.
[280]
Ho HH, He CY, De Graffenried CL, et al. Ordered assembly of the duplicating Golgi in Trypanosoma brucei. Proc Natl Acad Sci USA 2006; 103(2): 7676-81.
[281]
He CY, Ho HH, Malsam J, et al. Golgi duplication in Trypanosoma brucei. J Cell Biol 2004; 165(3): 313-21.
[283]
Alcantara CL, Vidal JC, de Souza W, et al. The three-dimensional structure of the cytostome-cytopharynx complex of Trypanosoma cruzi epimastigotes. J Cell Sci 2014; 127(Pt 10): 2227-37.
[286]
Ramirez IB, de Graffenried CL, Ebersberger I, et al. TbG63, a golgin involved in Golgi architecture in Trypanosoma brucei. J Cell Sci 2008; 121(Pt 9): 1538-46.
[311]
Monteiro AC, Abrahamson M, Lima AP, et al. Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi. J Cell Sci 2001; 114(Pt 21): 3933-42.
[312]
Santos CC, Sant’anna C, Terres A, et al. Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells. J Cell Sci 2005; 118(Pt 5): 901-15.
[340]
Schepilewsky E. Fadenförmige Anhängsel bei den Trypanosomen. - Zbl. Bakt. I Abt. Orig 1912; 65: 79-83.
[341]
Babudieri B, Tomasini N. Fine struttura dei trypanosomi. -. Parassitologia 1962; 4: 89-95.
[368]
Dey A, Chakrabarti K. Current perspectives of telomerase structure and function in eukaryotes with emerging views on telomerase in human parasites. Int J Mol Sci 2018; 19(2): 333.
[380]
Malaga S, Yoshida N. Targeted reduction in expression of Trypanosoma cruzi surface metacyclic trypomastigote surface molecule gp82 in adhesion to gastric mucin. Microbiol 2001; 4(11): 701-11.
[388]
Todeschini AR, Dias WB, Girard MF, et al. Enzimatically inactive trans-sialidase from T. cruzi infection. J Biol Chem 2004; 275: 32182-6.