Production of recombinat Conkunitzin-S1 in Escherichia coli. (2006)
Bayrhuber, M., Graf, R., Ferber, M., Zweckstetter, M., Imperial, J., Garrett, J. E., ...
Imperial, J. S., Bansal, P. S., Daly, N. L., Craik, D. ., Sporning, A., ...
Using assay-directed fractionation of the venom from the vermivorous cone snail Conus planorbis, we isolated a new conotoxin, designated p114a, with potent activity at both nicotinic acetylcholine...
Imperial, J. S., Bansal, P. S., Daly, N. L., Craik, D. ., Sporning, A., ...
Using assay-directed fractionation of the venom from the vermivorous cone snail Conus planorbis, we isolated a new conotoxin, designated p114a, with potent activity at both nicotinic acetylcholine...
Identification of a novel pharmacophore for peptide toxins interacting with K+ channels (2005)
Verdier, L., Al-Sabi, A., Rivier, J. E. F., Olivera, B. M., Terlau, H., Carlomagno, T.
Identification of a novel pharmacore for peptide toxins interacting with K+ channels (2005)
Verdier, L., Al-Sabi, A., Rivier, J. E. F., Olivera, B. M., Terlau, H., Carlomagno, T.
kappa M-conotoxin RIIIK, structural and functional novelty in a K+ channel antagonist (2004)
Al-Sabi, A., Lennartz, D., Ferber, M., Gulyas, J., Rivier, J. E. F., Olivera, B. M., ...
Differential expression of c-jun, junB, and junD in rat hippocampal slices. (1994)
Schlingensiepen, R., Terlau, H., Brysch, W., Schlingensiepen, K. H.
CALCIUM-CHANNEL CHARACTERISTICS CONFERRED ON THE SODIUM-CHANNEL BY SINGLE MUTATIONS (1992)
Heinemann, S. H., Terlau, H., Stuehmer, W., Imoto, K., Numa, S.
A SINGLE MUTATION ALTERS THE SODIUM-CHANNEL TO A CALCIUM-PERMEABLE CHANNEL (1992)
Heinemann, S. H., Terlau, H., Stuehmer, W., Imoto, K., Numa, S.
EXTRACELLULAR K+ SPECIFICALLY MODULATES A RAT-BRAIN K+ CHANNEL (1992)
Pardo, L. A., Heinemann, S. H., Terlau, H., Ludewig, U., Lorra, C., Pongs, O., ...
DETERMINANTS OF SENSITIVITY TO TETRODOTOXIN AND SAXITOXIN OF SODIUM CHANNEL-II (1992)
Terlau, H., Heinemann, S. H., Stuehmer, W., Pusch, M., Conti, F., Imoto, K., ...
MAPPING THE SITE OF BLOCK BY TETRODOTOXIN AND SAXITOXIN OF SODIUM CHANNEL-II (1991)
Terlau, H., Heinemann, S. H., Stuehmer, W., Pusch, M., Conti, F., Imoto, K., ...
Extracellular K+ specifically modulates a rat brain K+ channel.
Pardo, L A, Heinemann, S H, Terlau, H, Ludewig, U, Lorra, C, Pongs, O, ...
Extracellular potassium concentration is actively maintained within narrow limits in all higher organisms. Slight variations in extracellular potassium levels can induce major alterations of...
Ludwig, J, Terlau, H, Wunder, F, Brüggemann, A, Pardo, L A, Marquardt, A, ...
We have cloned a mammalian (rat) homologue of Drosophila ether á go-go (eag) cDNA, which encodes a distinct type of voltage activated potassium (K) channel. The derived Drosophila and rat eag...
Terlau, H, Heinemann, S H, Stühmer, W, Pongs, O, Ludwig, J
1. Rat eag potassium channels (r-eag) were expressed in Xenopus oocytes. They gave rise to delayed rectifying K+ currents with a strong Cole-Moore effect. 2. Deletions in the N-terminal structure of...
Extracellular K+ specifically modulates a rat brain K+ channel.
Pardo, L A, Heinemann, S H, Terlau, H, Ludewig, U, Lorra, C, Pongs, O, ...
Extracellular potassium concentration is actively maintained within narrow limits in all higher organisms. Slight variations in extracellular potassium levels can induce major alterations of...
Ludwig, J, Terlau, H, Wunder, F, Brüggemann, A, Pardo, L A, Marquardt, A, ...
We have cloned a mammalian (rat) homologue of Drosophila ether á go-go (eag) cDNA, which encodes a distinct type of voltage activated potassium (K) channel. The derived Drosophila and rat eag...
Terlau, H, Heinemann, S H, Stühmer, W, Pongs, O, Ludwig, J
1. Rat eag potassium channels (r-eag) were expressed in Xenopus oocytes. They gave rise to delayed rectifying K+ currents with a strong Cole-Moore effect. 2. Deletions in the N-terminal structure of...
Imperial, JS, Bansal, PS, Alewood, PF, Daly, NL, Craik, DJ, Sporning, A, ...
Using assay-directed fractionation of the venom from the vermivorous cone snail Conus planorbis, we isolated a new conotoxin, designated p114a, with potent activity at both nicotinic acetylcholine...