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Volume 33, Number 6, June 1995

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Neurotoxins from animal venoms as tools for neuroscience research.
pp. 713-713(1)
Author: Gopalakrishnakone, P.

Mechanism of action of crotoxin, a phospholipase A2 neurotoxin.
pp. 714-714(1)
Authors: Bon, C.; Choumet, V.; delot, E.; Faure, G.; Robbe-Vincent, A.; Saliou, B.

Engineering of toxic proteins.
pp. 714-714(1)
Authors: Menez, A.; Ducancel, F.; Boulain, J.; Vita, C.; Tremeau, O.

Apamin as a molecular probe to detect subtypes of small conductance, calcium-activated potassium channels.
pp. 714-715(2)
Authors: Strong, P.N.; Wadsworth, J.D.F.; Brewster, B.B.; Doorty, K.B.

Presynaptic snake neurotoxins produce tetanic fade during neuromuscular blockade.
pp. 715-716(2)
Authors: Nicholson, G.M.; Wilson, H.I.

Sea anemone neurotoxins--investigative tools and therapeutics.
pp. 715-715(1)
Authors: Elyakov, G.B.; Kozlovskaya, E.P.

Botulinum toxin: from menace to medicine.
pp. 716-716(1)
Author: Melling, J.

Modification of sodium channel gating by an Australian funnel-web spider toxin.
pp. 716-716(1)
Authors: Nicholson, G.M.; Little, M.J.; Willow, M.; Howden, M.E.H.; Narahashi, T.

Tandem mass spectrometry of conus peptides.
pp. 717-717(1)
Authors: Krishnamurthy, T.; Prabhakaran, M.; Long, S.R.

Effect of neurotoxin MPTP on the energy-related enzymes in brain of mice.
pp. 717-717(1)
Authors: Mangat, H.K.; Mann, H.

Ciguatoxins, a group of polyether neurotoxins which interact with sodium channels.
pp. 717-718(2)
Authors: Legrand, A.; Benoit, E.; Chinain, M.; Pauillac, S.; Molgo, J.

Mapping of the α-neurotoxin-binding site of the nicotinic acetylcholine receptor.
pp. 717-717(1)
Authors: Hucho, F.; Machold, J.; Utkin, Y.N.; Tsetlin, V.I.

Adrenergic nerve stimulation by venom of the scorpion Buthotus hottentota.
pp. 718-719(2)
Authors: Gwee, M.C.E.; Cheah, L.S.; Gopalakrishnakone, P.

Stimulation of non-adrenergic non-cholinergic (NANC) nerve by the venom of the scorpion Buthotus hottentota.
pp. 718-718(1)
Authors: Gwee, M.C.E.; Cheah, L.S.; Gopalakrishnakone, P.

Neurotoxins for the investigation of the membrane cytoskeleton interaction.
pp. 719-719(1)
Authors: Skibo, G.; Berezovskaya, O.; Rusakov, D.

Does the specific crotoxin inhibitor from Crotalus durissus terrificus serum behave as a soluble crotoxin acceptor?
pp. 720-720(1)
Authors: Perales, J.; Villela, C.; Domont, G.; Choumet, V.; Saliou, B.; Moussatche, H.; Bon, C.; Faure, G.

Inhibition of synaptosomal uptake of choline and GABA by sea anemone cytolysins.
pp. 720-720(1)
Authors: Khoo, H.E.; Lim, J.P.C.; Tan, C.H.

Pharmacological activity of four fractions isolated from the venom of the scorpion Buthus martensi karsch.
pp. 720-721(2)
Authors: Gong, J.P.; Kini, R.M.; Gwee, M.C.E.; Gopalakrishnakone, P.

Mechanism of action of Lophozozymus pictor toxin.
pp. 720-720(1)
Authors: Lau, C.O.; Li, Q.T.; Khoo, H.E.; Yuen, R.; Tan, C.H.

Neurotoxic effects of the venom on Bungarus caeruleus in the isolated chick biventer cervicis muscle.
pp. 721-721(1)
Authors: Alok, K.; Gwee, M.C.E.; Gopalakrishnakone, P.

The use of snake venom in neurology in China.
pp. 722-722(1)
Authors: Yang, J.H.; Li, F.Y.

The potencies of synthetic analogues of saxitoxin and the absolute stereoselectivity of decarbamoyl saxitoxin
pp. 723-737(15)
Authors: Strichartz, G.R.; Hall, S.; Magnani, B.; Hong, C.Y.; Kishi, Y.; debin, J.A.

Arthropod venom citrate inhibits phospholipase A2
pp. 763-770(8)
Authors: Fenton, A.W.; West, P.R.; Odell, G.V.; Hudiburg, S.M.; Ownby, C.L.; Mills, J.N.; Scroggins, B.T.; Shannon, S.B.

Anions and the anomalous gel filtration behavior of notexin and scutoxin
pp. 779-789(11)
Authors: Francis, B.; Schmidt, J.; Yang, Y.; Orlando, R.; Kaiser, I.I.

Interaction of palytoxin with red cells: structure-function studies
pp. 799-807(9)
Authors: Tosteson, M.T.; Scriven, D.R.L.; Bharadwaj, A.K.; Kishi, Y.; Tosteson, D.C.

Ability of six Latin American antivenoms to neutralize the venom of mapana equis (Bothrops atrox) from Antioquia and Choco (Colombia)
pp. 809-815(7)
Authors: Otero, R.; Nunez, V.; Osorio, R.G.; Gutierrez, J.M.; Giraldo, C.A.; Posada, L.E.

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