ArticleNature communications2013
A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed.
- Inhibitory effects of cannabidiol on voltage-dependent sodium currents.The Journal of biological chemistry · 2018Article
- Applications of sequence coevolution in membrane protein biochemistry.Biochimica et biophysica acta. Biomembranes · 2018Review
- A new mechanism of voltage-dependent gating exposed by KThe Journal of general physiology · 2017Article
- Atomic determinants of BK channel activation by polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Forces from the Portal Govern the Late-Stage DNA Transport in a Viral DNA Packaging Nanomotor.Biophysical journal · 2016Article
- Atomic basis for therapeutic activation of neuronal potassium channels.Nature communications · 2015Article
- Comparative sequence analysis suggests a conserved gating mechanism for TRP channels.The Journal of general physiology · 2015Article
- A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium Channels.The Journal of biological chemistry · 2015Article
- Atom-by-atom engineering of voltage-gated ion channels: magnified insights into function and pharmacology.The Journal of physiology · 2015Review
- Evolutionary imprint of activation: the design principles of VSDs.The Journal of general physiology · 2014Article
- Hydrogen bonds as molecular timers for slow inactivation in voltage-gated potassium channels.eLife · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Voltage-gated potassium channels elicit membrane hyperpolarization through voltage-sensor domains that regulate the conductive status of the pore domain. To better understand the inherent basis for the open-closed equilibrium in these channels, we undertook an atomistic scan using synthetic fluorinated derivatives of aromatic residues previously implicated in the gating of Shaker potassium channels. Here we show that stepwise dispersion of the negative electrostatic surface potential of only one site, Phe481, stabilizes the channel open state. Furthermore, these data suggest that this apparent stabilization is the consequence of the amelioration of an inherently repulsive open-state interaction between the partial negative charge on the face of Phe481 and a highly co-evolved acidic side chain, Glu395, and this interaction is potentially modulated through the Tyr485 hydroxyl. We propose that the intrinsic open-state destabilization via aromatic repulsion represents a new mechanism by which ion channels, and likely other proteins, fine-tune conformational equilibria.
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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.