Extracellular Blockade of K+ Channels by Tea
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منابع مشابه
Extracellular Blockade of K+ Channels by Tea
TEA is a classical blocker of K(+) channels. From mutagenesis studies, it has been shown that external blockade by TEA is strongly dependent upon the presence of aromatic residue at Shaker position 449 which is located near the extracellular entrance to the pore (Heginbotham, L., and R. MacKinnon. 1992. Neuron. 8:483-491). The data suggest that TEA interacts simultaneously with the aromatic res...
متن کاملExtracellular Blockade of K Channels by TEA: Results from Molecular Dynamics Simulations of the KcsA Channel
TEA is a classical blocker of K channels. From mutagenesis studies, it has been shown that external blockade by TEA is strongly dependent upon the presence of aromatic residue at Shaker position 449 which is located near the extracellular entrance to the pore (Heginbotham, L., and R. MacKinnon. 1992. Neuron. 8:483– 491). The data suggest that TEA interacts simultaneously with the aromatic resid...
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Extracellular blockade of potassium channels by TEA + has long been an important tool in electrophysiology (Armstrong, 1969). It is known that the binding affi n-ity of TEA + for the external side is directly affected by the amino acid side chain at position 449 (Shaker) (Heginbotham and MacKinnon, 1992). If an aromatic side chain is present (Tyr or Phe), TEA + binding is strong, whereas there ...
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Tetraethylammonium (TEA1) is widely used for reversible blockade of K channels in many preparations. We noticed that intracellular perfusion of voltage-clamped squid giant axons with a solution containing K1 and TEA1 irreversibly decreased the potassium current when there was no K1 outside. Five minutes of perfusion with 20 mM TEA1, followed by removal of TEA1, reduced potassium current to <5% ...
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ROMK channels are regulated by internal pH (pH(i)) and extracellular K(+) (K(+)(o)). The mechanisms underlying this regulation were studied in these channels after expression in Xenopus oocytes. Replacement of the COOH-terminal portion of ROMK2 (Kir1.1b) with the corresponding region of the pH-insensitive channel IRK1 (Kir 2.1) produced a chimeric channel (termed C13) with enhanced sensitivity ...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 2001
ISSN: 0022-1295,1540-7748
DOI: 10.1085/jgp.118.2.207