Scorpion toxins specific for Na+-channels.
- L. Possani, B. Becerril, M. Delepierre, J. Tytgat
- BiologyEuropean Journal of Biochemistry
- 1 September 1999
A classification containing 10 different groups of toxins is proposed in this review, based on functional and structural features of the known toxins, and the limited success obtained in the search for the site through which these peptides bind to the channels.
Scorpion venom components as potential candidates for drug development
- E. Ortiz, G. Gurrola, E. F. Schwartz, L. Possani
- Biology, ChemistryToxicon
- 26 November 2014
Current views on scorpion toxins specific for K+-channels.
- R. C. Rodríguez de la Vega, L. Possani
- BiologyToxicon
- 15 June 2004
Scorpion venom components that affect ion-channels function.
- V. Quintero-Hernández, J. M. Jiménez-Vargas, G. Gurrola, H. Valdivia, L. Possani
- BiologyToxicon
- 15 December 2013
Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones)
- E. F. Schwartz, E. Diego-García, R. C. Rodríguez de la Vega, L. Possani
- BiologyBMC Genomics
- 16 May 2007
This report contains the first transcriptome analysis of genes transcribed by the venomous gland of a scorpion, and provides the first sketch of cellular components, molecular functions, biological processes and some unique sequences of the scorpion venom gland.
Peptides and genes coding for scorpion toxins that affect ion-channels.
- L. Possani, E. Merino, M. Corona, F. Bolivar, B. Becerril
- BiologyBiochimie
- 10 September 2000
Scorpionism and serotherapy in Mexico.
- M. Dehesa-Dávila, L. Possani
- MedicineToxicon
- 1 September 1994
Mapping the Binding Site of a Humanether-a-go-go-related Gene-specific Peptide Toxin (ErgTx) to the Channel's Outer Vestibule*
- L. Pardo-López, Mei Zhang, Jie Liu, M. Jiang, L. Possani, G. Tseng
- Biology, ChemistryJournal of Biological Chemistry
- 10 May 2002
This study proposes that the long S5-P linker of the HERG channel forms an amphipathic α-helix that, together with the P-S6 linker, forms a hydrophobic ErgTx binding site, which paves the way for future mutant cycle analysis of interacting residues in the Ergtx·HERG complex, which will yield information about the topology of HERG's outer vestibule.
Rate dependency of delayed rectifier currents during the guinea‐pig ventricular action potential
- M. Rocchetti, A. Besana, G. Gurrola, L. Possani, A. Zaza
- Biology, MedicineJournal of Physiology
- 1 August 2001
In spite of its complexity, the behaviour of IKr was accurately predicted by a numerical model based entirely on known kinetic properties of the current, and may be increased at fast heart rates, but this may occur through completely different mechanisms.
Triabin, a Highly Potent Exosite Inhibitor of Thrombin (*)
- C. Noeske-Jungblut, B. Haendler, P. Donner, A. Alagón, L. Possani, W. Schleuning
- Biology, ChemistryJournal of Biological Chemistry
- 1 December 1995
Triabin, a new thrombin inhibitor, has been purified from the saliva of Triatoma pallidipennis, a blood-sucking triatomine bug, and results indicate that the inhibitor is directed toward the anion-binding exosite ofThrombin.
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