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- W2077306192 abstract "Glycine receptors (GlyR's) are inhibitory ligand-gated receptors in the nicotinicoid receptor superfamily. GlyR's mediate neurotransmission in CNS and are typically activated by glycine. GlyR is implicated in pain signaling to the brain. In order to better understand the silencing electrical activity of the brain and also the structure and function of GlyR in its open state, ivermectin (IVM) sensitive GlyR channels are developed as IVM is shown to stabilize GlyR in its non-desensitizing state. Double mutant F207A/A288G in α1 human GlyR has been shown to increase IVM sensitivity and reduce/remove sensitivity for glycine. We are developing photo crosslinking methodologies linked with mass spectrometric analysis on systematically generated single Cys mutations in IVM sensitive GlyR to enable us to study state-dependent structure of GlyR in the open state. Studies on GlyR in its open state will provide distance constraints that can be used in computational models to better the structure in its open state (non-desensitizing) and can help perform comparative studies with a desensitizing GlyR." @default.
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- W2077306192 date "2014-01-01" @default.
- W2077306192 modified "2023-09-27" @default.
- W2077306192 title "Towards Structural and Functional Determination of a Non-Desensitizing α1 Glycine Receptor" @default.
- W2077306192 doi "https://doi.org/10.1016/j.bpj.2013.11.3049" @default.
- W2077306192 hasPublicationYear "2014" @default.
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