ArticleThe Journal of general physiology2014
Drug-induced ion channel opening tuned by the voltage sensor charge profile.
Article in The Journal of general physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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
24 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Carboxyl-group compounds activate voltage-gated potassium channels via a distinct mechanism.The Journal of general physiology · 2024Article
- Identification of PUFA interaction sites on the cardiac potassium channel KCNQ1.The Journal of general physiology · 2021Article
- Resin-acid derivatives bind to multiple sites on the voltage-sensor domain of the Shaker potassium channel.The Journal of general physiology · 2021Article
- Coupling stabilizers open KProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Optoelectronic control of single cells using organic photocapacitors.Science advances · 2019Article
- Mechanisms Underlying the Dual Effect of Polyunsaturated Fatty Acid Analogs on Kv7.1.Cell reports · 2018Article
- Biaryl sulfonamide motifs up- or down-regulate ion channel activity by activating voltage sensors.The Journal of general physiology · 2018Article
- Replacing voltage sensor arginines with citrulline provides mechanistic insight into charge versus shape.The Journal of general physiology · 2018Article
- Atom-by-atom tuning of the electrostatic potassium-channel modulator dehydroabietic acid.The Journal of general physiology · 2018Article
- A drug pocket at the lipid bilayer-potassium channel interface.Science advances · 2017Article
- Article
- Actions and Mechanisms of Polyunsaturated Fatty Acids on Voltage-Gated Ion Channels.Frontiers in physiology · 2017Review
- Atomic determinants of BK channel activation by polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Extracellular Linkers Completely Transplant the Voltage Dependence from Kv1.2 Ion Channels to Kv2.1.Biophysical journal · 2016Article
- Voltage-sensor conformation shapes the intra-membrane drug binding site that determines gambierol affinity in Kv channels.Neuropharmacology · 2016Article
- Reciprocal voltage sensor-to-pore coupling leads to potassium channel C-type inactivation.Scientific reports · 2016Article
- The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.PLoS computational biology · 2016Article
- In-Depth Study of the Interaction, Sensitivity, and Gating Modulation by PUFAs on KFrontiers in physiology · 2016Review
- Alkanols inhibit voltage-gated K(+) channels via a distinct gating modifying mechanism that prevents gate opening.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyunsaturated fatty acids modulate the voltage dependence of several voltage-gated ion channels, thereby being potent modifiers of cellular excitability. Detailed knowledge of this molecular mechanism can be used in designing a new class of small-molecule compounds against hyperexcitability diseases. Here, we show that arginines on one side of the helical K-channel voltage sensor S4 increased the sensitivity to docosahexaenoic acid (DHA), whereas arginines on the opposing side decreased this sensitivity. Glutamates had opposite effects. In addition, a positively charged DHA-like molecule, arachidonyl amine, had opposite effects to the negatively charged DHA. This suggests that S4 rotates to open the channel and that DHA electrostatically affects this rotation. A channel with arginines in positions 356, 359, and 362 was extremely sensitive to DHA: 70 µM DHA at pH 9.0 increased the current >500 times at negative voltages compared with wild type (WT). The small-molecule compound pimaric acid, a novel Shaker channel opener, opened the WT channel. The 356R/359R/362R channel drastically increased this effect, suggesting it to be instrumental in future drug screening.
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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.