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Experimental Lachesis muta rhombeata envenomation and effects of soursop (Annona muricata) as natural antivenom J. Venom. Anim. Toxins incl. Trop. Dis.
Cremonez,Caroline Marroni; Leite,Flávia Pine; Bordon,Karla de Castro Figueiredo; Cerni,Felipe Augusto; Cardoso,lara Aimê; Gregório,Zita Maria de Oliveira; Souza,Rodrigo Cançado Gonçalves de; Souza,Ana Maria de; Arantes,Eliane Candiani.
Abstract Background In the Atlantic forest of the North and Northeast regions of Brazil, local population often uses the fruit juice and the aqueous extract of leaves of soursop (Annona muricata L.) to treat Lachesis muta rhombeata envenomation. Envenomation is a relevant health issue in these areas, especially due to its severity and because the production and distribution of antivenom is limited in these regions. The aim of the present study was to evaluate the relevance of the use of soursop leaf extract and its juice against envenomation by Lachesis muta rhombeata. Methods We evaluated the biochemical, hematological and hemostatic parameters, the blood pressure, the inflammation process and the lethality induced by Lachesis muta rhombeata snake...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lachesis muta rhombeata; Bushmaster; Natural antivenom; Antiophidic action; Soursop; Annona muricata L..
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100310
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Purification and enzymatic characterization of a novel metalloprotease from Lachesis muta rhombeata snake venom J. Venom. Anim. Toxins incl. Trop. Dis.
Cordeiro,Francielle Almeida; Coutinho,Bárbara Marques; Wiezel,Gisele Adriano; Bordon,Karla de Castro Figueiredo; Bregge-Silva,Cristiane; Rosa-Garzon,Nathalia Gonsales; Cabral,Hamilton; Ueberheide,Beatrix; Arantes,Eliane Candiani.
Abstract Background: Lachesis muta rhombeata (Lmr) is the largest venomous snake in Latin America and its venom contains mainly enzymatic components, such as serine and metalloproteases, L-amino acid oxidase and phospholipases A2. Metalloproteases comprise a large group of zinc-dependent proteases that cleave basement membrane components such as fibronectin, laminin and collagen type IV. These enzymes are responsible for local and systemic changes, including haemorrhage, myonecrosis and inflammation. This study aimed the isolation and enzymatic characterization of the first metalloprotease (Lmr-MP) from Lmr venom (LmrV). Methods and results: Lmr-MP was purified through two chromatographic steps and submitted to enzymatic characterization. It showed...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lachesis muta rhombeata; Metalloprotease; Proteases; Snake venom.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100323
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Cell migration inhibition activity of a non-RGD disintegrin from Crotalus durissus collilineatus venom J. Venom. Anim. Toxins incl. Trop. Dis.
Oliveira,Isadora Sousa de; Manzini,Rafaella Varzoni; Ferreira,Isabela Gobbo; Cardoso,Iara Aimê; Bordon,Karla de Castro Figueiredo; Machado,Ana Rita Thomazela; Antunes,Lusânia Maria Greggi; Rosa,José Cesar; Arantes,Eliane Candiani.
Abstract Background: In recent decades, snake venom disintegrins have received special attention due to their potential use in anticancer therapy. Disintegrins are small and cysteine-rich proteins present in snake venoms and can interact with specific integrins to inhibit their activities in cell-cell and cell-ECM interactions. These molecules, known to inhibit platelet aggregation, are also capable of interacting with certain cancer-related integrins, and may interfere in important processes involved in carcinogenesis. Therefore, disintegrin from Crotalus durissus collilineatus venom was isolated, structurally characterized and evaluated for its toxicity and ability to interfere with cell proliferation and migration in MDA-MB-231, a human breast cancer...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Crotalus durissus collilineatus; Non-RGD disintegrin; Cell migration; Cell adhesion; Human breast cancer; MDA-MB-231.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100319
Registros recuperados: 3
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