ArticleProceedings of the National Academy of Sciences of the United States of America2022
Molecular basis of multistep voltage activation in plant two-pore channel 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Review
- Structural basis for inhibition of the lysosomal two-pore channel TPC2 by a small molecule antagonist.Structure (London, England : 1993) · 2024Article
- Article
- Conformational rearrangements in the second voltage sensor domain switch PIPProceedings of the National Academy of Sciences of the United States of America · 2023Article
- HPCA1 is required for systemic reactive oxygen species and calcium cell-to-cell signaling and plant acclimation to stress.The Plant cell · 2022Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Electrophysiology and fluorescence to investigate cation channels and transporters in isolated plant vacuoles.Stress biology · 2022Review
- Major vacuolar TPC1 channel in stress signaling: what matters, KStress biology · 2022Review
- Voltage- and CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
- Commented on byVoltage- and Ca2022
Authors and funding
6 authors.
Funding
Abstract
Voltage-gated ion channels confer excitability to biological membranes, initiating and propagating electrical signals across large distances on short timescales. Membrane excitation requires channels that respond to changes in electric field and couple the transmembrane voltage to gating of a central pore. To address the mechanism of this process in a voltage-gated ion channel, we determined structures of the plant two-pore channel 1 at different stages along its activation coordinate. These high-resolution structures of activation intermediates, when compared with the resting-state structure, portray a mechanism in which the voltage-sensing domain undergoes dilation and in-membrane plane rotation about the gating charge-bearing helix, followed by charge translocation across the charge transfer seal. These structures, in concert with patch-clamp electrophysiology, show that residues in the pore mouth sense inhibitory Ca
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Registered trials
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