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The Journal of Biological Chemistry|July 5, 1989
Identification and properties of very high affinity brain membrane-binding sites for a neurotoxic phospholipase from the taipan venomG Lambeau, J Barhanin, H Schweitz, et al.
The Journal of Biological Chemistry|July 15, 1992
A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps)H Schweitz, P Vigne, D Moinier, et al.
FEBS Letters|November 24, 1999
MIT(1), a black mamba toxin with a new and highly potent activity on intestinal contractionH Schweitz, P Pacaud, S Diochot, et al.
Biochimica Et Biophysica Acta|September 21, 1979
The sodium channel in non-impulsive cells. Interaction with specific neurotoxinsG Romey, Y Jacques, H Schweitz, et al.
Biochemistry|May 20, 1975
Structure-function relationship in the binding of snake neurotoxins to the torpedo membrane receptorR Chicheportiche, J P Vincent, C Kopeyan, et al.
The Journal of Biological Chemistry|June 10, 1981
Structure-function relationships of sea anemone toxin II from Anemonia sulcataJ Barhanin, M Hugues, H Schweitz, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 15, 1991
Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channelJ R de Weille, H Schweitz, P Maes, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1994
Calcicludine, a venom peptide of the Kunitz-type protease inhibitor family, is a potent blocker of high-threshold Ca2+ channels with a high affinity for L-type channels in cerebellar granule neuronsH Schweitz, C Heurteaux, P Bois, et al.
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