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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Moura-da-Silva, Ana M. [1] ; Almeida, Michelle T. [1] ; Portes-Junior, Jose A. [1] ; Nicolau, Carolina A. [2] ; Gomes-Neto, Francisco [2] ; Valente, Richard H. [2]
Total Authors: 6
Affiliation:
[1] Inst Butantan, Lab Imunopatol, BR-05503900 Sao Paulo - Brazil
[2] Inst Oswaldo Cruz, Lab Toxinol, BR-21040360 Rio De Janeiro - Brazil
Total Affiliations: 2
Document type: Review article
Source: TOXINS; v. 8, n. 6 JUN 2016.
Web of Science Citations: 10
Abstract

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. (AU)

FAPESP's process: 14/26058-8 - Inhibition of mammalian and snake venom metalloproteinases by the recombinant pro-domain of jararhagin and its relevant peptide fragments
Grantee:Ana Maria Moura da Silva
Support Opportunities: Regular Research Grants