NMDA Receptor Transmembrane Domain: Structure and Divalent Ion Selectivity
During a synaptic signal, NMDA receptors are the only ionotropic glutamate receptor subfamily that besides glutamate require glycine and membrane depolarization to allow ion permeation. The depolarization is necessary to release Mg2+ of the channel of NMDA receptors. Of the ions that permeate these...
Main Author: | Veras, Lea |
---|---|
Format: | Others |
Published: |
Research Showcase @ CMU
2014
|
Online Access: | http://repository.cmu.edu/dissertations/1036 http://repository.cmu.edu/cgi/viewcontent.cgi?article=2075&context=dissertations |
Similar Items
-
All atom NMDA receptor transmembrane domain model development and simulations in lipid bilayers and water.
by: Samaneh Mesbahi-Vasey, et al.
Published: (2017-01-01) -
The molecular mechanism underlying divalent ions permeation and block of NMDA receptors
by: Yu-Chang Chou, et al.
Published: (2011) -
Properties of slow voltage-dependent divalent cation block in native neuronal NMDA receptors
by: Kim, Nam-Kyung
Published: (2011) -
Structural and Functional Insights into the Transmembrane Domain Association of Eph Receptors
by: Amita R. Sahoo, et al.
Published: (2021-08-01) -
Syndecan Transmembrane Domain Specifically Regulates Downstream Signaling Events of the Transmembrane Receptor Cytoplasmic Domain
by: Jisun Hwang, et al.
Published: (2021-07-01)