ArticleProceedings of the National Academy of Sciences of the United States of America2020
Resting state structure of the hyperdepolarization activated two-pore channel 3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. 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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Who cites it
11 citing papers in PubMed.
- Review
- Voltage sensors.Molecular pharmacology · 2025Review
- Structural basis for severe pain caused by mutations in the S4-S5 linkers of voltage-gated sodium channel NaProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Conformational rearrangements in the second voltage sensor domain switch PIPProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Characterization of Endo-Lysosomal Cation Channels Using Calcium Imaging.Handbook of experimental pharmacology · 2023Article
- Two-pore channels: going with the flows.Biochemical Society transactions · 2022Article
- Article
- Activation of endo-lysosomal two-pore channels by NAADP and PI(3,5)PCell calcium · 2022Review
- Molecular basis of multistep voltage activation in plant two-pore channel 1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- Highlighting membrane protein structure and function: A celebration of the Protein Data Bank.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Voltage-gated ion channels endow membranes with excitability and the means to propagate action potentials that form the basis of all neuronal signaling. We determined the structure of a voltage-gated sodium channel, two-pore channel 3 (TPC3), which generates ultralong action potentials. TPC3 is distinguished by activation only at extreme membrane depolarization (V
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Registered trials
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