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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.)

High-resolution proteomic profiling of spider venom: expanding the toxin diversity of Phoneutria nigriventer venom

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Author(s):
Liberato, Tarcisio [1, 2] ; Paolo Troncone, Lanfranco Ranieri [1] ; Yamashiro, Edson T. [3] ; Serrano, Solange M. T. [3] ; Zelanis, Andre [2, 3]
Total Authors: 5
Affiliation:
[1] Inst Butantan, Farmacol Lab, Sao Paulo - Brazil
[2] Univ Fed Sao Paulo, Lab Prote Func, Dept Ciencia & Tecnol, ICT UNIFESP, Campus Sao Jose dos Campos, Rua Talim 330, BR-12231280 Sao Paulo, SP - Brazil
[3] Inst Butantan, Lab Especial Toxinol Aplicada, Ctr Toxins Immune Response & Cell Signaling CeTIC, Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Amino Acids; v. 48, n. 3, p. 901-906, MAR 2016.
Web of Science Citations: 4
Abstract

Here we present a proteomic characterization of Phoneutria nigriventer venom. A shotgun proteomic approach allowed the identification, for the first time, of O-glycosyl hydrolases (chitinases) in P. nigriventer venom. The electrophoretic profiles under nonreducing and reducing conditions, and protein identification by mass spectrometry, indicated the presence of oligomeric toxin structures in the venom. Complementary proteomic approaches allowed for a qualitative and semi-quantitative profiling of P. nigriventer venom complexity, expanding its known venom proteome diversity. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 11/08514-8 - Study of the degradome of HF3, a PIII-class snake venom metalloproteinase from Bothrops jararaca venom, on cultured fibroblasts
Grantee:André Zelanis Palitot Pereira
Support Opportunities: Scholarships in Brazil - Post-Doctoral