Výsledky vyhledávání - "MESH: Viper Venoms/pharmacology"

Targeting α1 inserted domain (I) of α1β1 integrin by Lebetin 2 from M. lebetina transmediterranea venom decreased tumorigenesis and angiogenesis

Autor: Zaineb Abdelkafi-Koubaa, Mohamed El Ayeb, Erij Messadi, Najet Srairi Abid, Maram Morjen, Jed Jebali, Houcemeddine Othman, José Luis, Naziha Marrakchi

Publikováno v: International Journal of Biological Macromolecules
International Journal of Biological Macromolecules, 2018, 117, pp.790-799. ⟨10.1016/j.ijbiomac.2018.05.230⟩
International Journal of Biological Macromolecules, Elsevier, 2018, 117, pp.790-799. ⟨10.1016/j.ijbiomac.2018.05.230⟩

International audience; Through the recent development of knowledge in biotechnology and bioinformatics, snake venoms are widely used to develop new drugs to treat diseases such as hypertension and cancer. We have previously reported that Lebetin 2 i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90e51ea875cbc6ee35aa79287c5c9f3b
https://doi.org/10.1016/j.ijbiomac.2018.05.230

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Lebetin 2, a Snake Venom-Derived Natriuretic Peptide, Attenuates Acute Myocardial Ischemic Injury through the Modulation of Mitochondrial Permeability Transition Pore at the Time of Reperfusion

Autor: Elise Belaidi, Naziha Marrakchi, Jessica Morand, Mohamed Elayeb, Diane Godin-Ribuot, Bochra Tourki, Erij Messadi, Philippe Mateo

Publikováno v: PLoS ONE
PLoS ONE, Vol 11, Iss 9, p e0162632 (2016)
PLoS ONE, 2016, 11 (9), pp.e0162632. ⟨10.1371/journal.pone.0162632.s006⟩
PLoS ONE, Public Library of Science, 2016, 11 (9), pp.e0162632. ⟨10.1371/journal.pone.0162632.s006⟩

International audience; Cardiac ischemia is one of the leading causes of death worldwide. It is now well established that natriuretic peptides can attenuate the development of irreversible ischemic injury during myocardial infarction. Lebetin 2 (L2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d04d2741249654873641e73a1e25644
http://europepmc.org/articles/PMC5019389

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Lebein, a snake venom disintegrin, suppresses human colon cancer cells proliferation and tumor-induced angiogenesis through cell cycle arrest, apoptosis induction and inhibition of VEGF expression

Autor: Ons, Zakraoui, Cezary, Marcinkiewicz, Zohra, Aloui, Houcemeddine, Othman, Renaud, Grépin, Meriam, Haoues, Makram, Essafi, Najet, Srairi-Abid, Ammar, Gasmi, Habib, Karoui, Gilles, Pagès, Khadija, Essafi-Benkhadir

Publikováno v: Molecular Carcinogenesis
Molecular Carcinogenesis, Wiley, 2016, 56, pp.18-35. ⟨10.1002/mc.22470⟩

Lebein, is an heterodimeric disintegrin isolated from Macrovipera lebetina snake venom that was previously characterized as an inhibitor of ADP-induced platelet aggregation. In this study, we investigated the effect of Lebein on the p53-dependent gro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0f26039872eae3cfc403bba0d6257ac7
https://hal.archives-ouvertes.fr/hal-01356511

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Expression of a functional recombinant C-type lectin-like protein lebecetin in the human embryonic kidney (HEK) cells

Autor: Jed Jebali, José Luis, Assou el Battari, Amine Bazaa, Maram Morjen, Naziha Marrakchi, Sylvie Mathieu, Charlotte Jeanneau, Ali Gargouri, Mohamed El Ayeb

Publikováno v: Biotechnology Progress
Biotechnology Progress, Wiley, 2012, 28 (6), pp.1560-1565. ⟨10.1002/btpr.1632⟩

International audience; Lebecetin is an anticoagulant C-type lectin-like protein (CLPs) that was previously isolated from Macrovipera lebetinavenom and described to consist of two subunits (alpha and beta). It was reported to potently prevent platele

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a337b80447a0b2269b6934173480a9
https://hal-riip.archives-ouvertes.fr/pasteur-00733000

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Lebecetin, a C-lectin protein from the venom of Macrovipera lebetina that inhibits platelet aggregation and adhesion of cancerous cells

Autor: Sarray, Sameh, Srairi, Najet, Luis, José, Marvaldi, Jacques, El Ayeb, Mohamed, Marrakchi, Naziha

Publikováno v: Pathophysiology of Haemostasis and Thrombosis
Pathophysiology of Haemostasis and Thrombosis, Karger, 2001, 31 (3-6), pp.173-176. ⟨10.1159/000048060⟩
Pathophysiology of Haemostasis and Thrombosis, 2001, 31 (3-6), pp.173-176. ⟨10.1159/000048060⟩

International audience; A novel C-lectin protein, lebecetin, was purified and characterized from the venom of Macrovipera lebetina. It is a disulfide-linked heterodimer of 15 and 16 kD. The subunits are homologous to each other and to the other snake

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::8fa32a5f585417f59e0925129c466bac
https://pubmed.ncbi.nlm.nih.gov/11910182

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[Effect of Macrovipera lebetina and Cerastes cerastes venoms on adherence to integrins of cancerous cells (IGR39, HT29-D4 and IGROV1)]

Autor: Marrakchi, N, Sarray, S, Marvaldi, J, EL Ayeb, M, Luis, J

Publikováno v: Archives de l'Institut Pasteur de Tunis
Archives de l'Institut Pasteur de Tunis, 2002, 79 (1-4), pp.3--9

In this work, we provide experimental arguments in favor of the fact that components from Macrovipera lebetina and Cerastes cerastes venoms bind to IGR39 melanoma cells but not to HT29D4 cells that derive from carcinoma adenome. Furthermore, Macrovip

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f4f8046bcef43ab7d7c27c40052819e6
https://hal.archives-ouvertes.fr/hal-01975005

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Further characterization and thrombolytic activity in a rat model of a fibrinogenase from Vipera lebetina venom

Autor: Mohamed Elayeb, Habib Karoui, Ahmed Chabchoub, Koussay Dellagi, Ammar Gasmi, S. Guermazi

Publikováno v: Thrombosis Research
Thrombosis Research, Elsevier, 1997, 86 (3), pp.233-242. ⟨10.1016/S0049-3848(97)00066-2⟩

International audience; Vipera lebetina fibrinogenase (VIF) was shown to render fibrinogen incoagulable and to solubilize fibrin. The fibrinogenolytic activity of this enzyme was found to be 33 mg fibrinogen/min/mg protein. The study of the specifici

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fed4758c0c499d929c2598423f49aeb7
https://pubmed.ncbi.nlm.nih.gov/9175244

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