The muscarinic-gated K+ channel: Subunit stoichiometry and structural domains essential for G protein stimulation

The muscarinic-gated K+ channel: Subunit stoichiometry and structural domains essential for G protein stimulation

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Tucker, S, Pessia, M, Adelman, J
التنسيق:	Journal article
منشور في:	1996

مواد مشابهة

Muscarine-gated K+ channel: subunit stoichiometry and structural domains essential for G protein stimulation.
حسب: Tucker, S, وآخرون
منشور في: (1996)

Inhibitory interactions between two inward rectifier K+ channel subunits mediated by the transmembrane domains.
حسب: Tucker, S, وآخرون
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Inhibitory interactions between two inward rectifier K+ channel subunits mediated by the transmembrane domains.
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Subunit positional effects revealed by novel heteromeric inwardly rectifying K+ channels.
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Subunit positional effects revealed by novel heteromeric inwardly rectifying K+ channels.
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Membrane protein stoichiometry determined from the step-wise photobleaching of dye-labelled subunits.
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Gating and ATP-sensitivity of the cloned beta-cell K-ATP channel
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