Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Receptor stimulation causes slow inhibition of IRK1 inwardly rectifying K+ channels by direct protein kinase A-mediated phosphorylation.

Proceedings of the National Academy of Sciences of the United States of America - 11 Jun 1996

Wischmeyer E, Karschin A

Abstract excerpt

Strongly rectifying IRK-type inwardly rectifying K+ channels are involved in the control of neuronal excitability in the mammalian brain. Whole-cell patch-clamp experiments show that cloned rat IRK1 (Kir 2.1) channels, when heterologously expressed in mammalian COS-7 cells, are inhibited followin...

Topics

Animals
Cell Line
Cyclic AMP-Dependent Protein Kinases
Mutation
Phosphorylation
Potassium Channel Blockers
Potassium Channels
Potassium Channels, Inwardly Rectifying
Rats
Receptors, Serotonin
Serotonin Receptor Agonists

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Tumor Cells, Cultured

Source

Open in PubMed Open full text

Identifiers

PMID: 8650176
DOI: 10.1073/pnas.93.12.5819
PMCID: PMC39145

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8650176-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Receptor stimulation causes slow inhibition of IRK1 inwardly rectifying K+ channels by direct protein kinase A-mediated phosphorylation.PMID 8650176Read ↗

Beta subunit phosphorylation selectively increases fast desensitization and prolongs deactivation of alpha1beta1gamma2L and alpha1beta3gamma2L GABA(A) receptor currents.Semantic proximity Read ↗

Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation.Semantic proximity Read ↗

Receptor-coupled regulation of K+ channel N-type inactivation.Semantic proximity Read ↗

Differential ion current activation by human 5-HT(1A) receptors in Xenopus oocytes: evidence for agonist-directed trafficking of receptor signalling.Semantic proximity Read ↗

Conditional protein phosphorylation regulates BK channel activity in rat cerebellar Purkinje neurons.Semantic proximity Read ↗

Deficiency of the RIβ subunit of protein kinase A causes body tremor and impaired fear conditioning memory in rats.Semantic proximity Read ↗

Constitutive activity of serotonin 2C receptors at G protein-independent signaling: modulation by RNA editing and antidepressants.Semantic proximity Read ↗

Sequential phosphorylation mediates receptor- and kinase-induced inhibition of TREK-1 background potassium channels.Semantic proximity Read ↗

The Phosphodiesterase Inhibitor IBMX Blocks the Potassium Channel THIK-1 from the Extracellular Side.Semantic proximity Read ↗

Rapid signaling at the plasma membrane by a nuclear receptor for thyroid hormoneSemantic proximity Read ↗

Neuronal phenotype dependency of agonist-induced internalization of the 5-HT(1A) serotonin receptor.Semantic proximity Read ↗

Phosphorylation of Galpha11 protein contributes to agonist-induced desensitization of 5-HT2A receptor signaling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.