@article{ref1,
title="Moving Pieces in a Venomic Puzzle: Unveiling Post-Translationally Modified Toxins from Tityus serrulatus",
journal="Journal of proteome research",
year="2013",
author="Verano-Braga, Thiago and Dutra, Alexandre A. A. and León, Ileana R. and Melo-Braga, Marcella N. and Roepstorff, Peter and Pimenta, Adriano M. C. and Kjeldsen, Frank",
volume="12",
number="7",
pages="3460-3470",
abstract="Besides being a public health problem, scorpion venoms have a potential biotechnological application since they contain peptides that may be used as drug leads and/or to reveal novel pharmacological targets. A comprehensive Tityus serrulatus venom proteome study with emphasis on the phosphoproteome and N-glycoproteome was performed to improve our knowledge on the molecular diversity of the proteinaceous toxins. We combined two peptide identification methodologies - i.e., database search and de novo sequencing to achieve a more comprehensive overview of the molecular diversity of the venoms. A total of 147 proteins were identified, including neurotoxins, enzymes, bradykinin-potentiating peptides and molecules with antimicrobial and diuretic activities. Among those, three proteins were found to be phosphorylated and one N-glycosylated. Finally, cleavage of toxin polypeptide chains seems to be a common post-translational modification in the venom since 80% of the identified molecules were, in fact, products of toxins proteolysis.<p /> <p>Language: en</p>",
language="en",
issn="1535-3893",
doi="10.1021/pr4003068",
url="http://dx.doi.org/10.1021/pr4003068"
}