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Campo Dublin Core | Valor | Idioma |
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dc.contributor.author | Stabeli, Rodrigo Guerino | - |
dc.contributor.author | Amui, Saulo França | - |
dc.contributor.author | Sant'Ana, Carolina Dalaqua | - |
dc.contributor.author | Pires, Matheus Godoy | - |
dc.contributor.author | Nomizo, Auro | - |
dc.contributor.author | Monteiro, Marta Chagas | - |
dc.contributor.author | Romão, Pedro Roosevelt Torres | - |
dc.contributor.author | Cota, Renata Guerra de Sá | - |
dc.contributor.author | Vieira, Carlos Alberto | - |
dc.contributor.author | Giglio, José Roberto | - |
dc.contributor.author | Fontes, Marcos Roberto de Mattos | - |
dc.contributor.author | Soares, Andreimar Martins | - |
dc.date.accessioned | 2015-03-06T18:36:29Z | - |
dc.date.available | 2015-03-06T18:36:29Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | STABELI, R. G. et al. Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue: an example of function versatility of snake venom proteins. Comparative Biochemistry and Physiology. C, Toxicology & Pharmacology, v. 142, p. 371-381, 2006. Disponível em: <http://ac.els-cdn.com/S1532045605002565/1-s2.0-S1532045605002565-main.pdf?_tid=6121ee92-9a94-11e4-b446-00000aab0f27&acdnat=1421092460_810f42242bb6648bdbafdb9fc2d3538f>. Acesso em: 08 nov. 2014. | pt_BR |
dc.identifier.issn | 1532-0456 | - |
dc.identifier.uri | http://www.repositorio.ufop.br/handle/123456789/4553 | - |
dc.description.abstract | MjTX-II, a myotoxic phospholipase A2 (PLA2) homologue from Bothrops moojeni venom, was functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr), acetic anhydride and 2-nitrobenzenesulphonyl fluoride (NBSF); (iii) enzymatic characterization: inhibition by low molecular weight heparin and EDTA; and (iv) molecular characterization: cDNA sequence and molecular structure prediction. The results demonstrated that MjTX-II displayed antimicrobial activity by growth inhibition against Escherichia coli and Candida albicans, antitumoral activity against Erlich ascitic tumor (EAT), human breast adenocarcinoma (SK-BR-3) and human T leukemia cells (JURKAT) and antiparasitic effects against Schistosoma mansoni and Leishmania spp., which makes MjTX-II a promising molecular model for future therapeutic applications, as well as other multifunctional homologous Lys49-PLA2s or even derived peptides. This work provides useful insights into the structural determinants of the action of Lys49-PLA2 homologues and, together with additional strategies, supports the concept of the presence of others “bioactive sites” distinct from the catalytic site in snake venom myotoxic PLA2s. | pt_BR |
dc.language.iso | en_US | pt_BR |
dc.subject | Bothrops | pt_BR |
dc.subject | Chemical modification | pt_BR |
dc.subject | Myotoxin | pt_BR |
dc.subject | Microbial | pt_BR |
dc.subject | Phospholipase | pt_BR |
dc.title | Bothrops moojeni myotoxin-II, a Lys49-phospholipase A2 homologue : an example of function versatility of snake venom proteins. | pt_BR |
dc.type | Artigo publicado em periodico | pt_BR |
dc.rights.license | O periódico Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3547120459813. | pt_BR |
dc.identifier.doi | https://doi.org/10.1016/j.cbpc.2005.11.020 | - |
Aparece nas coleções: | DECBI - Artigos publicados em periódicos |
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ARTIGO_BothropsMoojeniMyotoxin.pdf | 551,49 kB | Adobe PDF | Visualizar/Abrir |
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