ArticleThe EMBO journal2000
The molecular basis of the specificity of action of K(ATP) channel openers.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
54 citing papers in PubMed, 138 citations in OpenAlex.
- Nicorandil as a promising therapeutic option for ventricular arrhythmia: A case report and review of literature.World journal of cardiology · 2024Article
- Novel loss-of-function variants expand ABCC9-related intellectual disability and myopathy syndrome.Brain : a journal of neurology · 2024Article
- KThe Journal of pharmacology and experimental therapeutics · 2023Article
- CL-705G: a novel chemical Kir6.2-specific KFrontiers in pharmacology · 2023Article
- Article
- Omega-3 polyunsaturated fatty acid-induced vasodilation in mouse aorta and mesenteric arteries is not mediated by ATP-sensitive potassium channels.Frontiers in physiology · 2022Article
- ATP-sensitive potassium channels in zebrafish cardiac and vascular smooth muscle.The Journal of physiology · 2022Article
- Routes for Potassium Ions across Mitochondrial Membranes: A Biophysical Point of View with Special Focus on the ATP-Sensitive KBiomolecules · 2021Review
- The Pharmacology of ATP-Sensitive KHandbook of experimental pharmacology · 2021Article
- The Potential Involvement of an ATP-Dependent Potassium Channel-Opening Mechanism in the Smooth Muscle Relaxant Properties ofBiomolecules · 2019Article
- Structure-Activity Relationships, Pharmacokinetics, and Pharmacodynamics of the Kir6.2/SUR1-Specific Channel Opener VU0071063.The Journal of pharmacology and experimental therapeutics · 2019Article
- Genetic Discovery of ATP-Sensitive KCirculation. Arrhythmia and electrophysiology · 2019Review
- 2,2-Dimethyl-3,4-dihydro-2MedChemComm · 2019Article
- Altered KATP Channel Subunits Expression and Vascular Reactivity in Spontaneously Hypertensive Rats With Age.Journal of cardiovascular pharmacology · 2016Article
- Article
- KATP Channels in the Cardiovascular System.Physiological reviews · 2016Review
- Kir6.2 activation by sulfonylurea receptors: a different mechanism of action for SUR1 and SUR2A subunits via the same residues.Physiological reports · 2015Article
- Label-free cell phenotypic profiling decodes the composition and signaling of an endogenous ATP-sensitive potassium channel.Scientific reports · 2014Article
- Sarcolemmal ATP-sensitive potassium channels modulate skeletal muscle function under low-intensity workloads.The Journal of general physiology · 2014Article
- The unusual stoichiometry of ADP activation of the KATP channel.Frontiers in physiology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
K(ATP) channels incorporate a regulatory subunit of the ATP-binding cassette (ABC) transporter family, the sulfonylurea receptor (SUR), which defines their pharmacology. The therapeutically important K(+) channel openers (e.g. pinacidil, cromakalim, nicorandil) act specifically on the SUR2 muscle isoforms but, except for diazoxide, remain ineffective on the SUR1 neuronal/pancreatic isoform. This SUR1/2 dichotomy underpinned a chimeric strategy designed to identify the structural determinants of opener action, which led to a minimal set of two residues within the last transmembrane helix of SUR. Transfer of either residue from SUR2A to SUR1 conferred opener sensitivity to SUR1, while the reverse operation abolished SUR2A sensitivity. It is therefore likely that these residues form part of the site of interaction of openers with the channel. Thus, openers would target a region that, in other ABC transporters, is known to be tightly involved with the binding of substrates and other ligands. This first glimpse of the site of action of pharmacological openers should permit rapid progress towards understanding the structural determinants of their affinity and specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.