Zobrazeno 1 - 10
of 19
pro vyhledávání: '"R S, Rogowski"'
Publikováno v:
Journal of Toxicology: Toxin Reviews. 21:293-317
The long α-neurotoxin, α-Bungarotoxin (Bgtx), from the venom of the Taiwan banded krait, Bungarus multicinctus, is a high affinity competitive antagonist of skeletal muscle-type nicotinic acetylcholine receptors (nAChRs) and of certain homo-oligome
Autor:
Mordecai P. Blaustein, David J. Weber, K. C. Klenk, R. S. Rogowski, Donald R. Matteson, T.C. Tenenholz
Publikováno v:
Proteins: Structure, Function, and Genetics. 38:441-449
The Pandinotoxins, PiTX-K alpha and PiTX-K beta, are members of the Charybdotoxin family of scorpion toxins that can be used to characterize K+ channels. PiTX-K alpha differs from PiTX-K beta, another peptide from Pandinus imperator, by one residue (
Publikováno v:
Proteins. 38(4)
The Pandinotoxins, PiTX-K alpha and PiTX-K beta, are members of the Charybdotoxin family of scorpion toxins that can be used to characterize K+ channels. PiTX-K alpha differs from PiTX-K beta, another peptide from Pandinus imperator, by one residue (
Autor:
Shun Ichi Yamaguchi, Mordecai P. Blaustein, Michael A. Rogawski, R. S. Rogowski, Tushar G. Kokate, B. Y. Kim, K. N. Juhng
Publikováno v:
Epilepsy research. 34(2-3)
The scorpion venom peptide toxins tityustoxin-K(alpha) (TsTx-K(alpha)) and pandinustoxin-K(alpha) (PiTx-K(alpha)) are novel, highly potent and selective blockers of voltage-activated K+ channels. PiTx-K(alpha) preferentially blocks rapidly inactivati
Autor:
R S Rogowski, Robert G. Bryant, K S Whitley, S A Wise, J O Simpson, Thomas S. Gates, Roberto J. Cano, Jeffrey A. Hinkley
Publikováno v:
Smart Structures and Materials 1998: Industrial and Commercial Applications of Smart Structures Technologies.
Reported herein is an overview of the research being conducted within the Materials Division at NASA Langley Research Center on the development of smart material technologies for advanced airframe systems. The research is a part of the Aircraft Morph
Publikováno v:
Biochemistry. 36(10)
PiTX-K alpha, a 35-residue peptide recently isolated from the venom of Pandinus imperator, blocks the rapidly inactivating (A-type) K+ channel(s) in rat brain synaptosomes and the cloned Kv 1.2 potassium channel at very low toxin concentrations (6 nM
Autor:
R S, Rogowski, J H, Collins, T J, O'Neill, T A, Gustafson, T R, Werkman, M A, Rogawski, T C, Tenenholz, D J, Weber, M P, Blaustein
Publikováno v:
Molecular pharmacology. 50(5)
Three 35-amino acid peptide K+ channel toxins (pandinotoxins) were purified from the venom of the scorpion Pandinus imperaton the toxins are designated pandinotoxin (PiTX)-K alpha, PiTX-K beta, and PiTX-K gamma. In an 86Rb tracer flux assay on rat br
Publikováno v:
Annals of the New York Academy of Sciences. 779
Publikováno v:
The Journal of physiology. 485
1. The kinetic properties of the internal Na+ (Na+i)- dependent 45Ca2+ influx and external Na+ (Na+o)-dependent 45Ca2+ efflux were determined in isolated rat brain nerve terminals (synaptosomes) under conditions which the concentrations of internal N
Publikováno v:
Molecular pharmacology. 44(2)
The interaction between two nonhomologous K+ channel toxins, Tityus serrulatus (scorpion) toxin tityustoxin-K alpha (TsTX-K alpha) and Dendroaspis angusticeps (snake) toxin dendrotoxin (alpha-DTX), was investigated on K+ currents in B82 fibroblast ce