ArticleThe Journal of general physiology2018
Replacing voltage sensor arginines with citrulline provides mechanistic insight into charge versus shape.
Article in The Journal of general physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026Review
- Genetic Code Expansion for Mechanistic Studies in Ion Channels: An (Un)natural Union of Chemistry and Biology.Chemical reviews · 2024Review
- Dual mechanisms contribute to enhanced voltage dependence of an electric fish potassium channel.Biophysical journal · 2024Article
- Article
- HIFs: New arginine mimic inhibitors of the Hv1 channel with improved VSD-ligand interactions.The Journal of general physiology · 2021Article
- Chemical biology of protein citrullination by the protein A arginine deiminases.Current opinion in chemical biology · 2021Review
- Mapping the interaction surface of scorpion β-toxins with an insect sodium channel.The Biochemical journal · 2021Article
- Site-specific incorporation of citrulline into proteins in mammalian cells.Nature communications · 2021Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Investigating an epileptogenic mutation.The Journal of general physiology · 2019Article
- Epilepsy-associated mutations in the voltage sensor of KCNQ3 affect voltage dependence of channel opening.The Journal of general physiology · 2019Article
- Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor.Nature communications · 2018Article
- Determining the molecular basis of voltage sensitivity in membrane proteins.The Journal of general physiology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Voltage-dependent activation of voltage-gated cation channels results from the outward movement of arginine-bearing helices within proteinaceous voltage sensors. The voltage-sensing residues in potassium channels have been extensively characterized, but current functional approaches do not allow a distinction between the electrostatic and steric contributions of the arginine side chain. Here we use chemical misacylation and in vivo nonsense suppression to encode citrulline, a neutral and nearly isosteric analogue of arginine, into the voltage sensor of the
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Registered trials
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