https://www.selleckchem.com/products/Azacitidine(Vidaza).html Apicomplexan parasites harbor chimeric proteins embodying P4-type ATPase and guanylate cyclase domains. Such proteins - serving as the actuator of cGMP signaling in this group of important pathogens - are indeed unusual in terms of their sheer size, modus operandi, and evolutionary repurposing. Much like the mythological Sphinx, a human-lion chimeric creature that posed challenging riddles, the P4-type ATPase-guanylate cyclase chimeras present both structural and functional conundrums. Here we review the function, topology, mechanism, and intramolecular coordination of the alveolate-specific chimeras in apicomplexan parasites. The steep technological challenge to understand these molecular Sphinxes will surely keep many interdisciplinary researchers busy in the next decades. To successfully infect, Trypanosoma cruzi evades and modulates the host immune response. T. cruzi calreticulin (TcCalr) is a multifunctional, endoplasmic reticulum (ER)-resident chaperone that, translocated to the external microenvironment, mediates crucial host-parasite interactions. TcCalr binds and inactivates C1 and mannose-binding lectin (MBL)/ficolins, important pattern- recognition receptors (PRRs) of the complement system. Using an apoptotic mimicry strategy, the C1-TcCalr association facilitates the infection of target cells. T. cruzi infection also seems to confer protection against tumorigenesis. Thus, recombinant TcCalr has important antiangiogenic properties, detected in vitro, ex vivo, and in ovum, most likely contributing at least in part, to its antitumor properties. Consequently, TcCalr is useful for investigating key issues of host-parasite interactions and possible new immunological/pharmacological interventions in the areas of Chagas' disease and experimental cancer. Elimination programs targeting TriTryp diseases (Leishmaniasis, Chagas' disease, human African trypanosomiasis) significantly reduced the number of ca