P
Paula Juárez
Researcher at Spanish National Research Council
Publications - 18
Citations - 1535
Paula Juárez is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Disintegrin & Snake venom. The author has an hindex of 15, co-authored 18 publications receiving 1418 citations.
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Journal ArticleDOI
Snake venomics. Strategy and applications.
TL;DR: The combined strategy allows us to assign unambiguously all the isolated venom toxins representing over 0.05% of the total venom proteins to known protein families.
Journal ArticleDOI
Snake venom disintegrins: evolution of structure and function.
Juan J. Calvete,Cezary Marcinkiewicz,Daniel Monleon,Vicent Esteve,Vicent Esteve,Bernardo Celda,Paula Juárez,Libia Sanz +7 more
TL;DR: The role of the composition, conformation, and dynamics of the integrin inhibitory loop acting in concert with the C-terminal tail in determining the selective inhibition of integrin receptors is discussed.
Journal ArticleDOI
Evolution of Snake Venom Disintegrins by Positive Darwinian Selection
TL;DR: The adaptive advantage of the emergence of motifs targeting beta(1) integrins and the role of positively selected sites located within nonfunctional disintegrin regions appear to be difficult to rationalize in the context of a predator-prey arms race.
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Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus.
TL;DR: Detailed compositional analysis of the venom of E. ocellatus suggests that the final composition of venom is influenced by transcriptional and post-translational mechanisms that may be more complex than previously appreciated.
Journal ArticleDOI
Snake venomics: characterization of protein families in Sistrurus barbouri venom by cysteine mapping, N-terminal sequencing, and tandem mass spectrometry analysis.
TL;DR: The results show that the venom proteome of the pigmy rattlesnake S. barbouri is composed of proteins belonging to a few protein families, which can be structurally characterized by their disulfide bond contents.