Now showing items 1-3 of 3

    • Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum 

      Rocha, Surza Lucia Gonçalves; Lomonte, Bruno; Neves Ferreira, Ana Gisele da Costa; Trugilho, Monique Ramos de Oliveira; Junqueira de Azevedo, Inácio de Loiola Meirelles; Ho, Paulo Lee; Domont, Gilberto B.; Gutiérrez, José María; Perales, Jonas (2002-12-11)
      Bothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim ...
    • Novel catalytically-inactive PII metalloproteinases from a viperid snake venom with substitutions in the canonical zinc-binding motif 

      Camacho Umaña, Erika; Sanz, Libia; Escalante Muñoz, Teresa; Pérez, Alicia; Villalta Romero, Fabián; Lomonte, Bruno; Neves Ferreira, Ana Gisele da Costa; Feoli Grant, Andrés; Calvete Chornet, Juan José; Gutiérrez, José María; Rucavado Romero, Alexandra (2016-10-12)
      Snake venom metalloproteinases (SVMPs) play key biological roles in prey immobilization and digestion. The majority of these activities depend on the hydrolysis of relevant protein substrates in the tissues. Hereby, we ...
    • Screening for target toxins of the antiophidic protein DM64 through a gel-based interactomics approach 

      Rocha, Surza Lucia Gonçalves; Neves Ferreira, Ana Gisele da Costa; Trugilho, Monique Ramos de Oliveira; Angulo Ugalde, Yamileth; Lomonte, Bruno; Valente, Richard H.; Domont, Gilberto B.; Perales, Jonas (2017-01)
      DM64 is a glycosylated protein with antivenomactivity isolated fromthe serum of the opossumDidelphis aurita. It binds non-covalently to myotoxins I (Asp49) and II (Lys49) from Bothrops asper venom and inhibits their myotoxic ...