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- W2970337145 abstract "Significance A large family of membrane proteins, voltage-gated ion channels, regulate a vast array of physiological functions in essentially all life forms. How these molecules sense membrane potential and respond by creating ionic conduction is incompletely understood. The voltage sensors of these channels contain a “hydrophobic gasket,” a ring of hydrophobic amino acids near the center of the membrane, separating internal and external aqueous solutions. Although voltage-gated proton channels, H V 1, resemble voltage-sensing domains of other channels, they differ fundamentally. On depolarization, H V 1 conducts protons, whereas other voltage sensors open a physically distinct pore. We identify Val 109 , Phe 150 , Val 177 , and Val 178 as the hH V 1 hydrophobic gasket. Replacement with less hydrophobic amino acids accelerated channel opening and caused proton-selective leak through closed channels." @default.
- W2970337145 created "2019-09-05" @default.
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- W2970337145 date "2019-08-28" @default.
- W2970337145 modified "2023-10-14" @default.
- W2970337145 title "Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels" @default.
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- W2970337145 doi "https://doi.org/10.1073/pnas.1905462116" @default.
- W2970337145 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6754559" @default.
- W2970337145 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31462498" @default.
- W2970337145 hasPublicationYear "2019" @default.
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