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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.)

The proteinase-rich proteome of Bothrops jararaca venom

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Author(s):
Serrano, Solange M. T. [1] ; Oliveira, Ana K. [1] ; Menezes, Milene C. [1] ; Zelanis, Andre [1, 2]
Total Authors: 4
Affiliation:
[1] Inst Butantan, Lab Especial Toxinol Aplicada, Ctr Toxins Immune Response & Cell Signaling CeTIC, BR-05503000 Sao Paulo - Brazil
[2] Univ Fed Sao Paulo ICT UNIFESP, Inst Ciencia & Tecnol, Sao Jose Dos Campos - Brazil
Total Affiliations: 2
Document type: Review article
Source: Toxin Reviews; v. 33, n. 4, p. 169-184, DEC 2014.
Web of Science Citations: 8
Abstract

By catalyzing limited proteolysis or extensive degradation, proteolytic enzymes determine the fate of most proteins in an organism. In the evolutionary process of snake venoms, genes encoding proteinases were tailored to generate potent toxins to target key physiological proteins and thereby play a critical role in prey capture, immobilization and defense against predators. In Bothrops jararaca, metalloproteinases and serine proteinases are among the most abundant toxins both in newborn and adult venoms. In this review, we examine the proteinase-rich venom proteome of B. jararaca and how the proteinases act in a complex and heterogeneous fashion to exert their deleterious local and systemic effects. (AU)

FAPESP's process: 10/17328-0 - Comparative proteomic characterization of platelet aggregation induced by thrombin and PA-BJ, a serine proteinase from the venom of Bothrops jararaca.
Grantee:Ana Karina de Oliveira
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC