• 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 ...
    • Molecular architecture of the antiophidic protein DM64 and its binding specificity to myotoxin II from Bothrops asper venom 

      Silva Soares, Bárbara da; Rocha, Surza Lucia Gonçalves; Almeida Bastos, Viviane; Borges Lima, Diogo; Costa Carvalho, Paulo; Gozzo, Fabio Cesar; Demeler, Borries; Williams, Tayler L.; Arnold, Janelle; Henrickson, Amy; Jørgensen, Thomas J.D.; Souza, ‪Tatiana de Arruda Campos Brasil de; Perales, Jonas; Valente, Richard H.; Lomonte, Bruno; Gomes Neto, Francisco; Neves Ferreira, Ana Gisele da Costa (2022)
      DM64 is a toxin-neutralizing serum glycoprotein isolated from Didelphis aurita, an ophiophagous marsupial naturally resistant to snake envenomation. This 64 kDa antitoxin targets myotoxic phospholipases A2, which account ...
    • 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 ...