Mechanism of glutamate receptor desensitization
By Yu Sun, R. Olson, M. Horning, N. Armstrong, M. Mayer, Eric Gouaux. Nature, 2002
665 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/d6d6f0d061993008707603690e2cfb6a750f3caf
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- NMDA receptor subunits: function and pharmacology. (2007, background): “In AMPARs, this region forms a binding site for AMPAR-selective non-competitive antagonists of the GYKI family [39].”
- Ionotropic and metabotropic glutamate receptor structure and pharmacology (2005, neutral): “The binding site for cyclothiazide was identified at the dimer interface between AMPA receptor subunits (Sun et al. 2002).”
- Glutamate Receptor Ion Channels: Structure, Regulation, and Function (2010, background): “The specificity of cyclothiazide for flip splice variants arises from its interaction with Ser754, which is a larger Asn in flop variants and precludes tight cyclothiazide binding (Sun et al., 2002).”
- The voltage-gated potassium channels and their relatives (2002, background): “—seem to have an important dimer relationship between their sensor domain”
- Handbook of ion channels (2015, background): “CTZ also potentiates responses, possibly because it reduces the angle between LBDs in each dimer (Sun et al., 2002), in turn promoting linker separation.”