ReviewJournal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology2009
The domain and conformational organization in potassium voltage-gated ion channels.
Review in Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Kv1.1 channel dysfunction in parvalbumin-positive interneurons contributes to anxiety-like behaviors in young adult presenilin 1/2 conditional double knockout mice.Cell & bioscience · 2025Article
- Molecular Modulation of Threadfin Fish Brain to Hypoxia Challenge and Recovery Revealed by Multi-Omics Profiling.International journal of molecular sciences · 2025Article
- Potassium voltage-gated channel subfamily H member 2 (KCNH2) is a promising target for incretin secretagogue therapies.Signal transduction and targeted therapy · 2024Article
- Disruption of a Conservative Motif in the C-Terminal Loop of the KCNQ1 Channel Causes LQT Syndrome.International journal of molecular sciences · 2022Article
- Domain structure and conformational changes in rat KV2.1 ion channel.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2014Article
- Mechanisms of activation of voltage-gated potassium channels.Acta naturae · 2014Article
- Ion channels as drug targets in central nervous system disorders.Current medicinal chemistry · 2013Review
- Cytoplasmic domains and voltage-dependent potassium channel gating.Frontiers in pharmacology · 2012Article
- The evolutionarily conserved residue A653 plays a key role in HERG channel closing.The Journal of physiology · 2009Article
- Nanobiology for the pharmacology of cellular ion channels.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potassium ion channels play critical roles in cell function, providing the maintenance of the membrane, repolarization of action potentials, and the regulation of firing frequency. Mutations in genes that interfere with K(v) ion channel function cause severe inherited diseases, such as episodic ataxia type 1, deafness, epilepsy, or cardiac arrhythmia. Because of their critical role in the central nervous system, all ion channels are targets for multiple pharmacologically active compounds. Better understanding of the structure and function of K(v) channels may eventually contribute to a more effective design of drugs. In this review, we show the recent data about domain organization of eukaryotic potassium voltage-gated ion channels. We are giving special attention to the interaction between the domains and the corresponding conformational changes upon activation of the channel.
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What OpenQuestion holds
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.