Bothrops atrox is responsible for the majority of snakebite accidents in the …

• Abstract
• Background
• Results
• Discussion
• Conclusion
• Methods
• Abbreviations
• References

Biology Articles » Zoology » Herpetology » Ontogenetic variations in the venom proteome of the Amazonian snake Bothrops atrox » References

References

- Ontogenetic variations in the venom proteome of the Amazonian snake Bothrops atrox

1. Hoge AR, Romao Hoge SAWL: Poisonous snakes of the world. Part I. Check list of the pit vipers viperoidea, crotalinae.

   Memorias do Instituto Butantã 1978, 42:79-310.

   Return to text

2. López-Lozano JL, Sousa MV, Ricart CAO, Cháves-Olortegui C, Sanchez EF, Muniz EG, Bührnheim PF, Morhy L: Ontogenetic variation of metalloproteinases and plasma coagulant activity in venoms of wild Bothrops atrox specimens from Amazonian rain forest.

   Toxicon 2002, 40:997-1006. PubMed Abstract | Publisher Full Text |

   Return to text

3. Kamiguti AS, Hay CRM, Zuzel M: Inhibition of collagen-induced platelet aggregation as the result of cleavage of α2β1-integrin by the snake venom metalloproteinase Jararhagin.

   Biochem J 1996, 320:635-641. PubMed Abstract | Publisher Full Text | PubMed Central Full Text |

   Return to text

4. Matsui T, Fujimura Y, Titani K: Snake venom proteases affecting hemostasis and thrombosis.

   Biochim et Biophys Acta 2000, 1477:146-156.

   Return to text

5. Saldarriaga MM, Otero R, Nuñez V, Toro MF, Díaz A, Gutierrez JM: Ontogenetic variability of Bothrops atrox and Bothrops asper snake venoms from Colombia.

   Toxicon 2003, 42:405-411. PubMed Abstract | Publisher Full Text |

   Return to text

6. Hati R, Mitra P, Sarker S, Bhattacharyya KK: Snake venom hemorrhagins.

   Critical Reviews in Toxicology 1999, 29:1-19. PubMed Abstract | Publisher Full Text |

   Return to text

7. Takeya H, Nishida S, Miyata T, Kawada SI, Saisaka Y, Morita T, Iwanaga S: Coagulation factor X activating enzyme from Russell's viper venom (RVV-X).

   J Biol Chem 1992, 267:14109-14417. PubMed Abstract | Publisher Full Text |

   Return to text

8. Silva MB, Schattner M, Ramos CRR, Junqueira-De-Azevedo ILM, Guarnieri MC, Lazzari MA, Sampaio CAM, Pozner RG, Ventura JS, Ho PL, Chudzinski-Tavassi AM: A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning.

   Biochem J 2003, 369:129-139. PubMed Abstract | Publisher Full Text | PubMed Central Full Text |

   Return to text

9. Stábeli RG, Oliveira EB: Isolation and partial characterization of the L-amino acid oxidase from Bothrops alternatus snake venom.

   Journal of Venomous Animal Toxins Including Tropical Diseases 2003, 9:420.

   Return to text

10. Yamazaki Y, Hyodo F, Morita T: Wide distribution of cysteine-rich secretory proteins in snake venoms: Isolation and cloning of novel snake venom cysteine-rich secretory proteins.

    Arch Biochem Biophys 2003, 412:133-141. PubMed Abstract | Publisher Full Text |

    Return to text

11. Junqueira De Azevedo ILM, Farsky SHP, Oliveira ML, Ho PL: Molecular cloning and expression of a functional snake venom vascular endothelium growth factor (VEGF) from the Bothrops insularis p it viper.

    J Biol Chem 2001, 276:39836-39842. PubMed Abstract | Publisher Full Text |

    Return to text

12. Kostiza T, Meier J: Nerve growth factors from snake venoms: chemical properties, mode of action and biological significance.

    Toxicon 1996, 34:787-806. PubMed Abstract | Publisher Full Text |

    Return to text

13. Serrano SMT, Shannon JD, Wang D, Camargo ACM, Fox JWA: multifaceted analysis of viperid snake venoms by two-dimensional gel electrophoresis: An approach to understanding venom proteomics.

    Proteomics 2005, 5:501-510. PubMed Abstract | Publisher Full Text |

    Return to text

14. Li ST, Wang JQ, Zhang XM, Ren Y, Wang N, Zhao K, Chen XS, Zhao CF, Li XL, Shao JM, Yin JN, West MB, Xu NZ, Liu SQ: Proteomic characterization of two snake venoms: Naja naja atra and Agkistrodon halys.

    Biochem J 2004, 384:119-127. PubMed Abstract | Publisher Full Text | PubMed Central Full Text |

    Return to text

15. Shevchenko A, Wilm M, Vorm O, Mann M: Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels.

    Anal Chem 1996, 68:850-858. PubMed Abstract | Publisher Full Text |

    Return to text

16. Havlis J, Thomas H, Sebela M, Shevchenko A: Fast-response proteomics by accelerated in-gel digestion of proteins.

    Anal Chem 2003, 75:1300-1306. PubMed Abstract | Publisher Full Text |

    Return to text

17. Shevchenko A, Jensen ON, Podtelejnikov AV, Sagliocco F, Wilm M, Vorm O, Mortensen P, Shevchenko A, Boucherie H, Mann M: Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels.

    Proc Natl Acad Sci USA 1996, 93:14440-14445. PubMed Abstract | Publisher Full Text | PubMed Central Full Text |

    Return to text

18. Liska AJ, Shevchenko A: Expanding organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications.

    Proteomics 2003, 3:19-28. PubMed Abstract | Publisher Full Text |

    Return to text

19. Shevchenko A, Sunyaev S, Loboda A, Bork P, Ens W, Standing KG: Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching.

    Anal Chem 2001, 73:1917-1926. PubMed Abstract | Publisher Full Text |

    Return to text

20. Habermann B, Oegema J, Sunyaev S, Shevchenko A: The power and the limitations of cross-species protein identification by mass spectrometry-driven sequence similarity searches.

    Mol Cell Proteomics 2004, 3:238-249. PubMed Abstract | Publisher Full Text |

    Return to text

21. Theakston RDG, Reid HA: Development of simple standard assays procedures for the characterization of snake venoms.

    Bull World Health Organization 1983, 61:949-956.

    Return to text

22. Martins M, Gordo M: Bothrops atrox (common lancehead) diet.

    Herpetology Reviews 1993, 24:151-152.

    Return to text

23. Mackessy SP: Venom ontogeny in the pacific rattlesnakes Crotalus viridis viridis and C. v. oreganus.

    Copeia 1988, 1:92-101. Publisher Full Text |

    Return to text

24. Andrade DV, Abe AS: Relationship of venom ontogeny and diet in Bothrops Herpetologica.

    1999, 55:200-204.

    Return to text

25. Daltry JC, Wuster W, Thorpe RS: Diet and snake evolution.

    Nature 1996, 379:537-540. PubMed Abstract | Publisher Full Text |

    Return to text

26. Martins M, Oliveira ME: Natural history of snakes in forest of the Manaus region, Central Amazonia, Brazil.

    Herpetol Nat History 1998, 6:78-150.

    Return to text

27. Sanchez JC, Rouge V, Pisteur M, Ravier F, Tonella L, Moosmayer M, Wilkins MR, Hochstrasser DF: Improved and simplified in-gel sample application using reswelling of dry immobilized pH gradients.

    Electrophoresis 1997, 18:324-327. PubMed Abstract | Publisher Full Text |

    Return to text

28. Blum H, Bier H, Gross HJ: Improved silver staining of plant proteins, RNA and DNA in polyacrilamide gels.

    Electrophoresis 1987, 8:93-95. Publisher Full Text |

    Return to text

29. Thomas H, Havlis J, Peychl J, Shevchenko A: Dried-droplet probe preparation on AnchorChip trade mark targets for navigating the acquisition of matrix-assisted laser desorption/ionization time-of-flight spectra by fluorescence of matrix/analyte crystals.

    Rapid Commun Mass Spectrom 2004, 18:923-930. PubMed Abstract | Publisher Full Text |

    Return to text

30. Shevchenko A, Chernushevich I, Wilm M, Mann M: "De novo " sequencing of peptides recovered from in-gel digested proteins by nanoelectrospray tandem mass spectrometry.

    Mol Biotechnol 2002, 20:107-118. PubMed Abstract | Publisher Full Text |

    Return to text

31. Shevchenko A, Sunyaev S, Liska A, Bork P: Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes.

    Methods Mol Biol 2003, 211:221-234. PubMed Abstract |

    Return to text

32. Biemann K: Contributions of mass spectrometry to peptide and protein structure.

    Biomed Environ Mass Spectrom 1988, 16:99-111. PubMed Abstract | Publisher Full Text |

    Return to text