ArticleThe EMBO journal2000
A region of the sulfonylurea receptor critical for a modulation of ATP-sensitive K(+) channels by G-protein betagamma-subunits.
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 7 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.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Delta Opioid Receptor Expression and Function in Primary Afferent Somatosensory Neurons.Handbook of experimental pharmacology · 2018Review
- Possible mechanism involved in the antinociceptive activity of dimer of paederosidic acid and paederosidic acid methyl ester in mice.CNS neuroscience & therapeutics · 2014Article
- Transdermal buprenorphine - a critical appraisal of its role in pain management.Journal of pain research · 2009Article
- Expansion of signal transduction by G proteins. The second 15 years or so: from 3 to 16 alpha subunits plus betagamma dimers.Biochimica et biophysica acta · 2007Article
- Identification of R(-)-isomer of efonidipine as a selective blocker of T-type Ca2+ channels.British journal of pharmacology · 2004Article
- Opioid receptor modulation of a metabolically sensitive ion channel in rat amygdala neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Expression of cAMP-regulated guanine nucleotide exchange factors in pancreatic beta-cells.Biochemical and biophysical research communications · 2000Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To determine the interaction site(s) of ATP-sensitive K(+) (K(ATP)) channels for G-proteins, sulfonylurea receptor (SUR2A or SUR1) and pore-forming (Kir6.2) subunits were reconstituted in the mammalian cell line, COS-7. Intracellular application of the G-protein betagamma2-subunits (G(betagamma)(2)) caused a reduction of ATP-induced inhibition of Kir6.2/SUR channel activities by lessening the ATP sensitivity of the channels. G(betagamma)(2) bound in vitro to both intracellular (loop-NBD) and C-terminal segments of SUR2A, each containing a nucleotide-binding domain (NBD). Furthermore, a single amino acid substitution in the loop-NBD of SUR (Arg656Ala in SUR2A or Arg665Ala in SUR1) abolished the G(betagamma)(2)-dependent alteration of the channel activities. These findings provide evidence that G(betagamma) modulates K(ATP) channels through a direct interaction with the loop-NBD of SUR.
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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.