Evidence map›Paper›PMID 41320924›Full record

ArticleJournal of the American Chemical Society2025

Atomistic Mechanism of Calcium-Mediated Inward Rectification of the MthK Potassium Channel by Solid-State NMR and MD Simulations.

Carl Öster, Reinier de Vries, Juan Li, Denis Qoraj, Sascha Lange, Chaowei Shi, Wojciech Kopec, Bert L de Groot, Adam Lange

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Carl ÖsterResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.ORCID 0000-0002-8723-4533
Reinier de VriesComputational Biomolecular Dynamics Group, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.ORCID 0000-0002-3143-6830
Juan LiResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.
Denis QorajResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.ORCID 0009-0008-6944-4175
Sascha LangeResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.
Chaowei ShiResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.ORCID 0000-0002-0024-1096
Wojciech KopecComputational Biomolecular Dynamics Group, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.ORCID 0000-0001-8801-9563
Bert L de GrootComputational Biomolecular Dynamics Group, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Adam LangeResearch Unit Molecular Biophysics, Leibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin 13125, Germany.ORCID 0000-0002-7534-5973

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inward rectification is a fundamental but poorly understood phenomenon in potassium channel physiology. Despite its physiological importance, the exact mechanism has remained elusive. In this work, we uncover a previously unrecognized calcium-mediated gating mechanism in the MthK potassium channel that sheds new light on this essential process. By combining state-of-the-art proton-detected solid-state NMR spectroscopy with atomistic molecular dynamics simulations, we reveal that divalent calcium ions bind below the selectivity filter, physically obstructing the outward flow of potassium ions whereas inward flow is still possible─analogous to a molecular ball check valve. Second, the binding of Ca

Indexed as

CalciumMolecular Dynamics SimulationPotassium ChannelsNuclear Magnetic Resonance, BiomolecularPotassiumCalciumPotassiumPotassium Channels

Identifiers

PMID41320924
PMCPMC12703655

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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.