ArticleThe EMBO journal2009
Coupling of activation and inactivation gate in a K+-channel: potassium and ligand sensitivity.
Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
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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
52 citing papers in PubMed.
- Article
- Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023Article
- Direct Detection of Bound Ammonium Ions in the Selectivity Filter of Ion Channels by Solid-State NMR.Journal of the American Chemical Society · 2022Article
- Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Informing NMR experiments with molecular dynamics simulations to characterize the dominant activated state of the KcsA ion channel.The Journal of chemical physics · 2021Article
- NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Exploring KFrontiers in molecular biosciences · 2021Article
- Conformational equilibrium shift underlies altered KNature communications · 2020Article
- Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020Review
- Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Selectivity Filter Gate Controls Voltage-Gated Calcium Channel Calcium-Dependent Inactivation.Neuron · 2019Article
- Identifying coupled clusters of allostery participants through chemical shift perturbations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Inverted allosteric coupling between activation and inactivation gates in KProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- The gating cycle of a KeLife · 2017Article
- Key role of segment IS4 in Cav1.2 inactivation: link between activation and inactivation.Pflugers Archiv : European journal of physiology · 2017Article
- Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potassium (K(+))-channel gating is choreographed by a complex interplay between external stimuli, K(+) concentration and lipidic environment. We combined solid-state NMR and electrophysiological experiments on a chimeric KcsA-Kv1.3 channel to delineate K(+), pH and blocker effects on channel structure and function in a membrane setting. Our data show that pH-induced activation is correlated with protonation of glutamate residues at or near the activation gate. Moreover, K(+) and channel blockers distinctly affect the open probability of both the inactivation gate comprising the selectivity filter of the channel and the activation gate. The results indicate that the two gates are coupled and that effects of the permeant K(+) ion on the inactivation gate modulate activation-gate opening. Our data suggest a mechanism for controlling coordinated and sequential opening and closing of activation and inactivation gates in the K(+)-channel pore.
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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.