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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.
Biochemistry|March 7, 1989
NMR studies of toxin III from the sea anemone Radianthus paumotensis and comparison of its secondary structure with related toxinsJ H Pease, N V Kumar, H Schweitz, et al.
FEBS Letters|July 3, 1989
Charybdotoxin blocks dendrotoxin-sensitive voltage-activated K+ channelsH Schweitz, C E Stansfeld, J N Bidard, et al.
The Journal of Biological Chemistry|June 25, 1984
Crystallization and preliminary x-ray investigation of a protein neurotoxin from the sea anemone Anthopleura xanthogrammicaC D Smith, L DeLucas, S E Ealick, et al.
Journal of Molecular Biology|October 8, 1998
A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysisJ Boisbouvier, J P Albrand, M Blackledge, et al.
The Journal of Biological Chemistry|October 20, 1995
Kalicludines and kaliseptine. Two different classes of sea anemone toxins for voltage sensitive K+ channelsH Schweitz, T Bruhn, E Guillemare, et al.
Biochemistry|September 1, 1981
Purification and pharmacological properties of eight sea anemone toxins from Anemonia sulcata, Anthopleura xanthogrammica, Stoichactis giganteus, and Actinodendron plumosumH Schweitz, J P Vincent, J Barhanin, et al.
Brain Research|August 21, 1989
Analogies and differences in the mode of action and properties of binding sites (localization and mutual interactions) of two K+ channel toxins, MCD peptide and dendrotoxin IJ N Bidard, C Mourre, G Gandolfo, et al.
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