Sulfonylurea receptors: ABC transporters that regulate ATP-sensitive K(+) channels.

No abstract is available for this paper.

• Publication year

  1999

• Venue

  Biochimica et Biophysica Acta

• Publication date

  1999-12-06

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0005-2736(99)00164-9PMID 10581362
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide.

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• The N-terminus of KIR6.2 limits spontaneous bursting and modulates the ATP-inhibition of KATP channels.

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

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• Alternative sulfonylurea receptor expression defines metabolic sensitivity of K‐ATP channels in dopaminergic midbrain neurons

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• Stoichiometry of sulfonylurea-induced ATP-sensitive potassium channel closure.

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• Direct Photoaffinity Labeling of the Kir6.2 Subunit of the ATP-sensitive K+ Channel by 8-Azido-ATP*

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• Involvement of the N‐terminus of Kir6.2 in coupling to the sulphonylurea receptor

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• Structural rearrangements underlying K+-channel activation gating.

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• Involvement of the N‐terminus of Kir6.2 in the inhibition of the KATP channel by ATP

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• ATP inhibition of KATP channels: control of nucleotide sensitivity by the N‐terminal domain of the Kir6.2 subunit

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• Two Regions of Sulfonylurea Receptor Specify the Spontaneous Bursting and ATP Inhibition of KATP Channel Isoforms*

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• Mg2+ and ATP dependence of KATP channel modulator binding to the recombinant sulphonylurea receptor, SUR2B

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• The structure of the potassium channel: molecular basis of K+ conduction and selectivity.

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• Toward understanding the assembly and structure of KATP channels.

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• Binding of KATP channel modulators in rat cardiac membranes

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• KATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit.

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