Title |
Diversity of metalloproteinases in Bothrops neuwiedi snake venom transcripts: evidences for recombination between different classes of SVMPs
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Published in |
BMC Genomic Data, November 2011
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DOI | 10.1186/1471-2156-12-94 |
Pubmed ID | |
Authors |
Ana M Moura-da-Silva, Maria Stella Furlan, Maria Cristina Caporrino, Kathleen F Grego, José Antonio Portes-Junior, Patrícia B Clissa, Richard H Valente, Geraldo S Magalhães |
Abstract |
Snake venom metalloproteinases (SVMPs) are widely distributed in snake venoms and are versatile toxins, targeting many important elements involved in hemostasis, such as basement membrane proteins, clotting proteins, platelets, endothelial and inflammatory cells. The functional diversity of SVMPs is in part due to the structural organization of different combinations of catalytic, disintegrin, disintegrin-like and cysteine-rich domains, which categorizes SVMPs in 3 classes of precursor molecules (PI, PII and PIII) further divided in 11 subclasses, 6 of them belonging to PII group. This heterogeneity is currently correlated to genetic accelerated evolution and post-translational modifications. |
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Unknown | 3 | 100% |
Demographic breakdown
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Scientists | 1 | 33% |
Members of the public | 1 | 33% |
Practitioners (doctors, other healthcare professionals) | 1 | 33% |
Mendeley readers
Geographical breakdown
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Brazil | 1 | 1% |
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Demographic breakdown
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Student > Master | 18 | 21% |
Researcher | 15 | 17% |
Student > Bachelor | 10 | 11% |
Student > Doctoral Student | 5 | 6% |
Other | 9 | 10% |
Unknown | 12 | 14% |
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Immunology and Microbiology | 2 | 2% |
Other | 7 | 8% |
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