Publications by authors named "Tonya L Ebersole"
Article Synopsis
- iGluR channels, like GluA2, control synaptic activity by opening and closing in response to glutamate binding, but the mechanism behind gate opening is not fully understood.
- Substituting a key alanine residue (Ala-621) in the pore helix of the channel with glycine led to a channel that is more active and sensitive to glutamate, while mutation of another residue (Met-629) reduced activity, highlighting the roles of these residues in channel function.
- iGluRs and potassium channels have similar structural features, but iGluRs utilize a less flexible alanine as a hinge at a critical position to keep their activity low until activated by a ligand, differentiating them from potassium channels
