Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and scaffolds typical of cobra (Elapidae) venoms: implications for snake toxin repertoire evolution.

@article{JunqueiradeAzevedo2006LachesisM,
  title={Lachesis muta (Viperidae) cDNAs reveal diverging pit viper molecules and scaffolds typical of cobra (Elapidae) venoms: implications for snake toxin repertoire evolution.},
  author={In{\'a}cio de L M Junqueira-de-Azevedo and Ana Tung Ching Ching and Eliedson Rafael de Carvalho and Fernanda Faria and Milton Yutaka Nishiyama and Paulo Lee Ho and Marcelo Ribeiro Vasconcelos Diniz},
  journal={Genetics},
  year={2006},
  volume={173 2},
  pages={877-89}
}
Efforts to describe toxins from the two major families of venomous snakes (Viperidae and Elapidae) usually reveal proteins belonging to few structural types, particular of each family. Here we carried on an effort to determine uncommon cDNAs that represent possible new toxins from Lachesis muta (Viperidae). In addition to nine classes of typical toxins, atypical molecules never observed in the hundreds of Viperidae snakes studied so far are highly expressed: a diverging C-type lectin that is… CONTINUE READING

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