Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites

Publikation: Bidrag til tidsskrift › Letter › Forskning › fagfællebedømt

Standard

Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites. / Maolanon, Alex R.; Risgaard, Rune; Wang, Shuang Yan; Snoep, Yoran; Papangelis, Athanasios; Yi, Feng; Holley, David; Barslund, Anne F.; Svenstrup, Niels; Hansen, Kasper B.; Clausen, Rasmus P.

I: ACS Chemical Neuroscience, Bind 8, Nr. 8, 16.08.2017, s. 1681-1687.

Publikation: Bidrag til tidsskrift › Letter › Forskning › fagfællebedømt

Harvard

Maolanon, AR, Risgaard, R, Wang, SY, Snoep, Y, Papangelis, A, Yi, F, Holley, D, Barslund, AF, Svenstrup, N, Hansen, KB & Clausen, RP 2017, 'Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites', ACS Chemical Neuroscience, bind 8, nr. 8, s. 1681-1687. https://doi.org/10.1021/acschemneuro.7b00117

APA

Maolanon, A. R., Risgaard, R., Wang, S. Y., Snoep, Y., Papangelis, A., Yi, F., Holley, D., Barslund, A. F., Svenstrup, N., Hansen, K. B., & Clausen, R. P. (2017). Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites. ACS Chemical Neuroscience, 8(8), 1681-1687. https://doi.org/10.1021/acschemneuro.7b00117

Vancouver

Maolanon AR, Risgaard R, Wang SY, Snoep Y, Papangelis A, Yi F o.a. Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites. ACS Chemical Neuroscience. 2017 aug. 16;8(8):1681-1687. https://doi.org/10.1021/acschemneuro.7b00117

Author

Maolanon, Alex R. ; Risgaard, Rune ; Wang, Shuang Yan ; Snoep, Yoran ; Papangelis, Athanasios ; Yi, Feng ; Holley, David ; Barslund, Anne F. ; Svenstrup, Niels ; Hansen, Kasper B. ; Clausen, Rasmus P. / Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites. I: ACS Chemical Neuroscience. 2017 ; Bind 8, Nr. 8. s. 1681-1687.

Bibtex

@article{87a3ff83757b40e7acf4832ae6f9292d,
title = "Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites",
abstract = "A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.",
keywords = "d -cycloserine, d -serine, Ionotropic glutamate receptor, NMDA, subtype selectivity, superagonist",
author = "Maolanon, {Alex R.} and Rune Risgaard and Wang, {Shuang Yan} and Yoran Snoep and Athanasios Papangelis and Feng Yi and David Holley and Barslund, {Anne F.} and Niels Svenstrup and Hansen, {Kasper B.} and Clausen, {Rasmus P.}",
year = "2017",
month = aug,
day = "16",
doi = "10.1021/acschemneuro.7b00117",
language = "English",
volume = "8",
pages = "1681--1687",
journal = "ACS Chemical Neuroscience",
issn = "1948-7193",
publisher = "American Chemical Society",
number = "8",

}

RIS

TY - JOUR

T1 - Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites

AU - Maolanon, Alex R.

AU - Risgaard, Rune

AU - Wang, Shuang Yan

AU - Snoep, Yoran

AU - Papangelis, Athanasios

AU - Yi, Feng

AU - Holley, David

AU - Barslund, Anne F.

AU - Svenstrup, Niels

AU - Hansen, Kasper B.

AU - Clausen, Rasmus P.

PY - 2017/8/16

Y1 - 2017/8/16

N2 - A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.

AB - A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.

KW - d -cycloserine

KW - d -serine

KW - Ionotropic glutamate receptor

KW - NMDA

KW - subtype selectivity

KW - superagonist

U2 - 10.1021/acschemneuro.7b00117

DO - 10.1021/acschemneuro.7b00117

M3 - Letter

C2 - 28514141

AN - SCOPUS:85027413593

VL - 8

SP - 1681

EP - 1687

JO - ACS Chemical Neuroscience

JF - ACS Chemical Neuroscience

SN - 1948-7193

IS - 8

ER -

ID: 183858151