ATP-dependent interaction of the cytosolic domains of Kir6.2 revealed by fluorescence resonance energy transfer

ATP-dependent interaction of the cytosolic domains of Kir6.2 revealed by fluorescence resonance energy transfer

Chi tiết về thư mục
Những tác giả chính:	Tsuboi, T, Lippiat, J, Ashcroft, F, Rutter, G
Định dạng:	Conference item
Được phát hành:	2003

Những quyển sách tương tự

ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer.
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Identification of residues contributing to the ATP binding site of Kir6.2.
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Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
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Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
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Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
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The N-terminus of Kir6.2 is involved in coupling to SUR1
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Functional coupling between Kir6.2 and SUR1 is prerequisite for [H-3]repaglinide, but not [H-3]glibenclamide, binding to pancreatic ATP-sensitive potassium (K-ATP) channels.
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Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes.
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