Evolution of the sarafotoxin/endothelin superfamily of proteins.
- G. Landan, A. Bdolah, Z. Wollberg, E. Kochva, D. Graur
- BiologyToxicon
- 1991
Lethal factors and enzymes in the secretion from Duvernoy's gland of three colubrid snakes.
- H. I. Rosenberg, A. Bdolah, E. Kochva
- MedicineThe Journal of experimental zoology
- 1985
At least two of the snake species examined have toxic secretions that may be important during feeding by killing or weakening and helping to subdue the struggling prey.
Accumulation of some secretory enzymes in venom glands of Vipera palaestinae.
- R. S. Brown, M. Brown, A. Bdolah, E. Kochva
- BiologyAmerican Journal of Physiology
- 1975
It is concluded that each of the enzymes is secreted at a rate independent of the other two; this pattern of secretion can best be described as nonparallel.
Sarafotoxins S6: several isotoxins from Atractaspis engaddensis (burrowing asp) venom that affect the heart.
- C. Takasaki, N. Tamiya, A. Bdolah, Z. Wollberg, E. Kochva
- Chemistry, BiologyToxicon
- 1988
SRTX‐d, a new native peptide of the endothelin/sarafotoxin family
- A. Bdolah, Z. Wollberg, G. Fleminger, E. Kochva
- Biology, ChemistryFEBS Letters
- 9 October 1989
A novel cardiotoxic polypeptide from the venom of Atractaspis engaddensis (burrowing asp): cardiac effects in mice and isolated rat and human heart preparations.
- Z. Wollberg, R. Shabo-Shina, S. Gitter
- Biology, ChemistryToxicon
- 1988
Sarafotoxins and endothelins: evolution, structure and function.
- E. Kochva, A. Bdolah, Z. Wollberg
- Biology, ChemistryToxicon
- 1 May 1993
Cloning and sequence analysis of cDNAs encoding precursors of sarafotoxins. Evidence for an unusual "rosary-type" organization.
- F. Ducancel, V. Matre, A. Ménez
- BiologyJournal of Biological Chemistry
- 15 February 1993
The evolutionary history of the sarafotoxin/endothelin/endothelin-like superfamily.
- G. Landan, A. Bdolah, Z. Wollberg, E. Kochva, D. Graur
- Biology, ChemistryJournal of Cardiovascular Pharmacology
- 1991
In several lineages, the peptides have independently accumulated identical amino acid replacements in position 2, which supports the hypothesis that residue 2 is crucial to biological activity.
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