Defining the structural relationship between kainate-receptor deactivation and desensitization
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Title
Defining the structural relationship between kainate-receptor deactivation and desensitization
Authors
Keywords
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Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 9, Pages 1054-1061
Publisher
Springer Nature
Online
2013-08-19
DOI
10.1038/nsmb.2654
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Related references
Note: Only part of the references are listed.- Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain
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- NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers
- (2011) William F. Borschel et al. Nature Communications
- Desensitization and models of receptor-channel activation
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- Dynamic visualization of membrane-inserted fraction of pHluorin-tagged channels using repetitive acidification technique
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- Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization
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- Ion-dependent gating of kainate receptors
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- A Nondesensitizing Kainate Receptor Point Mutant
- (2009) N. Nayeem et al. MOLECULAR PHARMACOLOGY
- A Transmembrane Accessory Subunit that Modulates Kainate-Type Glutamate Receptors
- (2009) Wei Zhang et al. NEURON
- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
- (2008) Berk Hess et al. Journal of Chemical Theory and Computation
- GluR6/KA2 Kainate Receptors Mediate Slow-Deactivating Currents
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- Structural and Single-Channel Results Indicate That the Rates of Ligand Binding Domain Closing and Opening Directly Impact AMPA Receptor Gating
- (2008) W. Zhang et al. JOURNAL OF NEUROSCIENCE
- Molecular Basis of Kainate Receptor Modulation by Sodium
- (2008) Andrew J.R. Plested et al. NEURON
- Structural Rearrangements of NR1/NR2A NMDA Receptors during Allosteric Inhibition
- (2008) Marc Gielen et al. NEURON
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