ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structural basis for activation of voltage sensor domains in an ion channel TPC1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
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- Structural basis for inhibition of the lysosomal two-pore channel TPC2 by a small molecule antagonist.Structure (London, England : 1993) · 2024Article
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- 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
- Voltage-gating and cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Parallel adaptation in autopolyploid Arabidopsis arenosa is dominated by repeated recruitment of shared alleles.Nature communications · 2021Article
- Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins.International journal of molecular sciences · 2021Review
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- Stable Picodisc Assemblies from Saposin Proteins and Branched Detergents.Biochemistry · 2021Article
- Distinguishing Potassium Channel Resting State Conformations in Live Cells with Environment-Sensitive Fluorescence.ACS chemical neuroscience · 2020Article
- Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.eLife · 2020Article
- Resting state structure of the hyperdepolarization activated two-pore channel 3.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- DirectMX - One-Step Reconstitution of Membrane Proteins From Crude Cell Membranes Into Salipro Nanoparticles.Frontiers in bioengineering and biotechnology · 2020Article
- Why recombinant antibodies - benefits and applications.Current opinion in biotechnology · 2019Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Voltage-sensing domains (VSDs) couple changes in transmembrane electrical potential to conformational changes that regulate ion conductance through a central channel. Positively charged amino acids inside each sensor cooperatively respond to changes in voltage. Our previous structure of a TPC1 channel captured an example of a resting-state VSD in an intact ion channel. To generate an activated-state VSD in the same channel we removed the luminal inhibitory Ca
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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.