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.

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Autores principales:	Michael C. Regan, Zongjian Zhu, Hongjie Yuan, Scott J. Myers, Dave S. Menaldino, Yesim A. Tahirovic, Dennis C. Liotta, Stephen F. Traynelis, Hiro Furukawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6b226358d0264cea8bca51d4ed185d0d
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spelling	oai:doaj.org-article:6b226358d0264cea8bca51d4ed185d0d2021-12-02T17:33:11ZStructural elements of a pH-sensitive inhibitor binding site in NMDA receptors10.1038/s41467-019-08291-12041-1723https://doaj.org/article/6b226358d0264cea8bca51d4ed185d0d2019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-08291-1https://doaj.org/toc/2041-1723Context-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.Michael C. ReganZongjian ZhuHongjie YuanScott J. MyersDave S. MenaldinoYesim A. TahirovicDennis C. LiottaStephen F. TraynelisHiro FurukawaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Michael C. Regan Zongjian Zhu Hongjie Yuan Scott J. Myers Dave S. Menaldino Yesim A. Tahirovic Dennis C. Liotta Stephen F. Traynelis Hiro Furukawa Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
description	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.
format	article
author	Michael C. Regan Zongjian Zhu Hongjie Yuan Scott J. Myers Dave S. Menaldino Yesim A. Tahirovic Dennis C. Liotta Stephen F. Traynelis Hiro Furukawa
author_facet	Michael C. Regan Zongjian Zhu Hongjie Yuan Scott J. Myers Dave S. Menaldino Yesim A. Tahirovic Dennis C. Liotta Stephen F. Traynelis Hiro Furukawa
author_sort	Michael C. Regan
title	Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
title_short	Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
title_full	Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
title_fullStr	Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
title_full_unstemmed	Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
title_sort	structural elements of a ph-sensitive inhibitor binding site in nmda receptors
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/6b226358d0264cea8bca51d4ed185d0d
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Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors

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