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Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation

Laboratório de Imunopatologia, Instituto Butantan, São Paulo CEP 05503-900, Brazil
Laboratório de Toxinologia, Instituto Oswaldo Cruz, Rio de Janeiro CEP 21040-360, Brazil
Author to whom correspondence should be addressed.
Academic Editors: Jay Fox and José María Gutiérrez
Toxins 2016, 8(6), 183;
Received: 4 May 2016 / Revised: 27 May 2016 / Accepted: 3 June 2016 / Published: 9 June 2016
(This article belongs to the Special Issue Snake Venom Metalloproteinases)
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Snake venom metalloproteinases (SVMPs) are abundant in the venoms of vipers and rattlesnakes, playing important roles for the snake adaptation to different environments, and are related to most of the pathological effects of these venoms in human victims. The effectiveness of SVMPs is greatly due to their functional diversity, targeting important physiological proteins or receptors in different tissues and in the coagulation system. Functional diversity is often related to the genetic diversification of the snake venom. In this review, we discuss some published evidence that posit that processing and post-translational modifications are great contributors for the generation of functional diversity and for maintaining latency or inactivation of enzymes belonging to this relevant family of venom toxins. View Full-Text
Keywords: snake venom; metalloproteinase; post-translational processing; enzyme inhibitor; hemorrhage snake venom; metalloproteinase; post-translational processing; enzyme inhibitor; hemorrhage

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Moura-da-Silva, A.M.; Almeida, M.T.; Portes-Junior, J.A.; Nicolau, C.A.; Gomes-Neto, F.; Valente, R.H. Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation. Toxins 2016, 8, 183.

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