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Article

Parametrisation of the free energy of ATP binding to wild-type and mutant Kir6.2 potassium channels.

Biophysical chemistry - 1 Jan 2013

Moran Oscar, Grottesi Alessandro, Chadburn Andrew J, Tammaro Paolo

Abstract excerpt

ATP-sensitive K(+) (K(ATP)) channels, comprised of pore-forming Kir6.x and regulatory SURx subunits, play important roles in many cellular functions; because of their sensitivity to inhibition by intracellular ATP, K(ATP) channels provide a link between cell metabolism and membrane electrical act...

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Source

Identifiers

PMID: 23219002
DOI: 10.1016/j.bpc.2012.10.006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23219002-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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