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Mostrando ítems 51-55 de 55
Venom, venomics, antivenomics
(2009)
Venoms comprise mixtures of peptides and proteins tailored by Natural Selection to act on vital systems
of the prey or victim. Here we review our proteomic protocols for uncoiling the composition,
immunological profile, ...
Antivenomics of Atropoides mexicanus and Atropoides picadoi snake venoms: Relationship to the neutralization of toxic and enzymatic activities
(2010-09-30)
Viperid snakes of the genus Atropoides are distributed in Mexico and Central America and, owing to their size and venom yield, are capable of provoking severe envenomings in humans. This study evaluated, using an ‘antivenomics’ ...
Novel catalytically-inactive PII metalloproteinases from a viperid snake venom with substitutions in the canonical zinc-binding motif
(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 ...
Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming
(2009-03-06)
Snakebite envenoming represents a neglected tropical disease that has a heavy public health impact, particularly in Asia, Africa and Latin America. A global initiative, aimed at increasing antivenom production and ...
Understanding structural and functional aspects of PII snake venom metalloproteinases: Characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralis
(2014-06)
A new homodimeric PII metalloproteinase, named BlatH1, was purified from the venom of the Central American arboreal viperid snake Bothriechis lateralis by a combination of anion-exchange chromatography, hydrophobic interaction ...