Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
Context-dependent inhibition of NMDA receptors has important therapeutic implications for treatment of neurological diseases. Here, the authors use structural biology and biophysics to describe the basis for pH-dependent inhibition for a class of allosteric NMDAR inhibitors, called the 93-series.
Saved in:
Main Authors: | Michael C. Regan, Zongjian Zhu, Hongjie Yuan, Scott J. Myers, Dave S. Menaldino, Yesim A. Tahirovic, Dennis C. Liotta, Stephen F. Traynelis, Hiro Furukawa |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2019
|
Subjects: | |
Online Access: | https://doaj.org/article/6b226358d0264cea8bca51d4ed185d0d |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Asynchronous release sites align with NMDA receptors in mouse hippocampal synapses
by: Shuo Li, et al.
Published: (2021) -
Structural basis of subtype-selective competitive antagonism for GluN2C/2D-containing NMDA receptors
by: Jue Xiang Wang, et al.
Published: (2020) -
Structural features in the glycine-binding sites of the GluN1 and GluN3A subunits regulate the surface delivery of NMDA receptors
by: Kristyna Skrenkova, et al.
Published: (2019) -
Analysis of the NMDA in Focal Cerebral Ischemia in Rats
by: Tirapelli,D. P. C, et al.
Published: (2012) -
Predicting regulatory elements in repetitive sequences using transcription factor binding sites
by: Horng,Jorng-Tzong, et al.
Published: (2000)