ArticleNature chemical biology2011
Contributions of counter-charge in a potassium channel voltage-sensor domain.
Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
69 citing papers in PubMed, 99 citations in OpenAlex.
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026Review
- Voltage sensors.Molecular pharmacology · 2025Review
- Genetic Code Expansion for Mechanistic Studies in Ion Channels: An (Un)natural Union of Chemistry and Biology.Chemical reviews · 2024Review
- Dual mechanisms contribute to enhanced voltage dependence of an electric fish potassium channel.Biophysical journal · 2024Article
- Article
- Ion currents through the voltage sensor domain of distinct families of proteins.Journal of biological physics · 2023Review
- Fifty years of gating currents and channel gating.The Journal of general physiology · 2023Review
- The role of Phe150 in human voltage-gated proton channel.iScience · 2022Article
- Role of a conserved ion-binding site tyrosine in ion selectivity of the Na+/K+ pump.The Journal of general physiology · 2022Article
- The 70-year search for the voltage-sensing mechanism of ion channels.The Journal of physiology · 2022Article
- Critical Role of E1623 Residue in S3-S4 Loop of Nav1.1 Channel and Correlation Between Nature of Substitution and Functional Alteration.Frontiers in molecular neuroscience · 2021Article
- Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Metal Bridge in S4 Segment Supports Helix Transition in Shaker Channel.Biophysical journal · 2020Article
- Structures Illuminate Cardiac Ion Channel Functions in Health and in Long QT Syndrome.Frontiers in pharmacology · 2020Review
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Helix breaking transition in the S4 of HCN channel is critical for hyperpolarization-dependent gating.eLife · 2019Article
- Opening TRPP2 (Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018Review
- Replacing voltage sensor arginines with citrulline provides mechanistic insight into charge versus shape.The Journal of general physiology · 2018Article
- Mutations in the voltage-sensing domain affect the alternative ion permeation pathway in the TRPM3 channel.The Journal of physiology · 2018Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-sensor domains couple membrane potential to conformational changes in voltage-gated ion channels and phosphatases. Highly coevolved acidic and aromatic side chains assist the transfer of cationic side chains across the transmembrane electric field during voltage sensing. We investigated the functional contribution of negative electrostatic potentials from these residues to channel gating and voltage sensing with unnatural amino acid mutagenesis, electrophysiology, voltage-clamp fluorometry and ab initio calculations. The data show that neutralization of two conserved acidic side chains in transmembrane segments S2 and S3, namely Glu293 and Asp316 in Shaker potassium channels, has little functional effect on conductance-voltage relationships, although Glu293 appears to catalyze S4 movement. Our results suggest that neither Glu293 nor Asp316 engages in electrostatic state-dependent charge-charge interactions with S4, likely because they occupy, and possibly help create, a water-filled vestibule.
Indexed as
Identifiers
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.