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Gene Review:

Tc00.1047053508647.200 - triosephosphate isomerase

Trypanosoma cruzi strain CL Brener

Espinoza-Fonseca, L.M. et al., Cevallos, A.M. et al., Gao, X.G. et al.

Espinoza-Fonseca, Trujillo-Ferrara,

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High impact information on Tc00.1047053508647.200

Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane [1].
The relative steady state concentration of mRNAs of four housekeeping single-copy type Trypanosoma cruzi genes (actin, triosephosphate isomerase, trypanothion reductase and the ribosomal protein S4) was analyzed throughout the growth curve [2].
Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design [3].

Biological context of Tc00.1047053508647.200

To explore the possible binding sites at the interface of tripanosomal triosephosphate isomerase, fully flexible benzothiazoles were docked onto the dimer interface [3].

References

Crystal structure of triosephosphate isomerase from Trypanosoma cruzi in hexane. Gao, X.G., Maldonado, E., Pérez-Montfort, R., Garza-Ramos, G., de Gómez-Puyou, M.T., Gómez-Puyou, A., Rodríguez-Romero, A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
The stabilization of housekeeping transcripts in Trypanosoma cruzi epimastigotes evidences a global regulation of RNA decay during stationary phase. Cevallos, A.M., Pérez-Escobar, M., Espinosa, N., Herrera, J., López-Villaseñor, I., Hernández, R. FEMS Microbiol. Lett. (2005) [Pubmed]
Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design. Espinoza-Fonseca, L.M., Trujillo-Ferrara, J.G. Bioorg. Med. Chem. Lett. (2004) [Pubmed]

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