3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1.
ATP-sensitive potassium (K(ATP)) channels conduct potassium ions across cell membranes and thereby couple cellular energy metabolism to membrane electrical activity. Here, we report the heterologous expression and purification of a functionally active K(ATP) channel complex composed of pore-forming...
المؤلفون الرئيسيون: | Mikhailov, M, Campbell, J, De Wet, H, Shimomura, K, Zadek, B, Collins, R, Sansom, MS, Ford, R, Ashcroft, F |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2005
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مواد مشابهة
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Phentolamine block of KATP channels is mediated by Kir6.2.
حسب: Proks, P, وآخرون
منشور في: (1997) -
Pyridine nucleotide regulation of the KATP channel Kir6.2/SUR1 expressed in Xenopus oocytes.
حسب: Dabrowski, M, وآخرون
منشور في: (2003) -
Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.
حسب: Proks, P, وآخرون
منشور في: (1999) -
Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
حسب: Antcliff, J, وآخرون
منشور في: (2005) -
Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
حسب: Dabrowski, M, وآخرون
منشور في: (2004)