• A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase 

      Jiménez Sandoval, Pedro; Vique Sánchez, José Luis; López Hidalgo, Marisol; Velázquez Juárez, Gilberto; Díaz Quezada, Corina; Arroyo Navarro, Luis Fernando; Montero Morán, Gabriela Margarita; Fattori, Juliana; Díaz Salazar, Alma Jessica; Rudiño Piñera, Enrique; Sotelo Mundo, Rogerio Rafael; Migliorini Figueira, Ana Carolina; Lara González, Samuel; Benítez Cardoza, Claudia Guadalupe; Brieba de Castro, Luis Gabriel (Elsevier, 2017)
      "The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the ...
    • Substrate-induced dimerization of engineered monomeric variants of triosephosphate isomerase from Trichomonas vaginalis 

      Lara González, Samuel; Estrella, Priscilla; Portillo, Carmen; Cruces, María E; Jiménez Sandoval, Pedro; Fattori, Juliana; Migliorin Figueira, Ana C.; López Hidalgo, Marisol; Díaz Quezada, Corina; López Castillo, Laura Margarita; Trasviña Arenas, Carlos Humberto; Sánchez Sandoval, Maria Eugenia; Gómez Puyou, Armando; Ortega López, Jaime; Arroyo, Rossana; Benítez Cardoza, Claudia Guadalupe; Brieba, Luis G (2015-11)
      "The dimeric nature of triosephosphate isomerases (TIMs) is maintained by an extensive surface area interface of more than 1600 angstrom 2. TIMs from Trichomonas vaginalis (TvTIM) are held in their dimeric state by two ...