Identification of the high-affinity tolbutamide site on the SUR1 subunit of the K(ATP) channel.

Identification of the high-affinity tolbutamide site on the SUR1 subunit of the K(ATP) channel.

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ATP-sensitive potassium channels (K(ATP)) are formed from four pore-forming Kir6.2 subunits complexed with four regulatory sulfonylurea receptor subunits (SUR1 in pancreatic beta-cells, SUR2A in heart). The sensitivity of the channel to different sulfonylureas depends on the SUR isoform. In particul...

Bibliografski detalji
Glavni autori:	Ashfield, R, Gribble, F, Ashcroft, S, Ashcroft, F
Format:	Journal article
Jezik:	English
Izdano:	1999

Slični predmeti

Identification of the high affinity tolbutamide site on the SUR1 subunit of the K-ATP channel
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The ATP- and tolbutamide-sensitivity of the ATP-sensitive K-channel from human pancreatic B cells.
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Interaction of MgATP with the sulphonylurea subunit activates ATP sensitive K-channels receptor
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Regulation of K-ATP channels by nucleotides and drugs
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Nucleotide modulation of pinacidil stimulation of the cloned K(ATP) channel Kir6.2/SUR2A.
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MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit.
od: Gribble, F, i dr.
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Protein kinase C does not influence the tolbutamide sensitivity of K-ATP currents
od: Proks, P, i dr.
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ATP modulation of ATP-sensitive potassium channel ATP sensitivity varies with the type of SUR subunit.
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Thiol reagents and ATP do not interact with C717 in the SUR1 subunit of the beta-cell K-ATP channel
od: Trapp, S, i dr.
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Modulation of tolbutamide sensitivity of K-ATP currents in mouse pancreatic beta-cells by intracellular nucleotides and magnesium
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Expression of the cloned beta-cell ATP-sensitive potassium channel in Xenopus oocytes
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The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide.
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A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.
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Differential sensitivity of beta-cell and extrapancreatic K(ATP) channels to gliclazide.
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Mechanism of K-ATP channel inhibition by ATP
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The Kir6.2-F333I mutation differentially modulates K-ATP channels composed of SUR1 or SUR2 subunits
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The Kir6.2-F333I mutation differentially modulates K ATP channels composed of SUR1 and SUR2 subunits
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Tissue-specific effects of sulfonylureas: lessons from studies of cloned K(ATP) channels.
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Activation and inhibition of K-ATP currents by guanine nucleotides is mediated by different channel subunits.
od: Trapp, S, i dr.
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Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
od: Dabrowski, M, i dr.
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The Yin and Yang of the K(ATP) channel.
od: Ashcroft, F
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The antimalarial agent mefloquine inhibits ATP-sensitive K-channels.
od: Gribble, F, i dr.
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Interaction of the cytosolic domains of the Kir6.2 subunit of the K(ATP) channel is modulated by sulfonylureas.
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Overlapping distribution of K(ATP) channel-forming Kir6.2 subunit and the sulfonylurea receptor SUR1 in rodent brain.
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The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.
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Analysis of the differential modulation of sulphonylurea block of beta-cell and cardiac ATP-sensitive K+ (K(ATP)) channels by Mg-nucleotides.
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A universally conserved residue in the SUR1 subunit of the K ATP channel is essential for translating nucleotide binding at SUR1 into channel opening
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