Evidence map›Paper›PMID 22269804›Full record

ReviewNeurochemistry international2012

Pharmacological modulation of NMDA receptor activity and the advent of negative and positive allosteric modulators.

Daniel T Monaghan, Mark W Irvine, Blaise Mathias Costa, Guangyu Fang, David E Jane

Abstract readReview
In one paragraph

Review in Neurochemistry international, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

  1. Pooled it
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  6. Discovery of GluN2A subtype-selectiveActa pharmaceutica Sinica. B · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Daniel T MonaghanDepartment of Pharmacology and Experimental Neuroscience, University of Nebraska Medical Center, Omaha, NE, USA. dtmonagh@unmc.edu
Mark W Irvine
Blaise Mathias Costa
Guangyu Fang
David E Jane
University of Bristol · GBUniversity of Nebraska Medical Center · US

Funding

Development and Pharmacology of Positive Allosteric Modulators of NMDA ReceptorsR01MH060252 · NIMH · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JANE, DAVID EDWARD, MONAGHAN, DANIEL T · 2001 to 2017
$4.0M
Biotechnology and Biological Sciences Research Council BB/F012519/1Medical Research Council G0601509Medical Research Council G0601812NIMH NIH HHS MH60252NIMH NIH HHS R01 MH060252
6 · The paper itself

Abstract

The NMDA receptor (NMDAR) family of l-glutamate receptors are well known to have diverse roles in CNS function as well as in various neuropathological and psychiatric conditions. Until recently, the types of agents available to pharmacologically regulate NMDAR function have been quite limited in terms of mechanism of action and subtype selectivity. This has changed significantly in the past two years. The purpose of this review is to summarize the many drug classes now available for modulating NMDAR activity. Previously, this included competitive antagonists at the l-glutamate and glycine binding sites, high and low affinity channel blockers, and GluN2B-selective N-terminal domain binding site antagonists. More recently, we and others have identified new classes of NMDAR agents that are either positive or negative allosteric modulators (PAMs and NAMs, respectively). These compounds include the pan potentiator UBP646, the GluN2A-selective potentiator/GluN2C and GluN2D inhibitor UBP512, the GluN2D-selective potentiator UBP551, the GluN2C/GluN2D-selective potentiator CIQ as well as the new NMDAR-NAMs such as the pan-inhibitor UBP618, the GluN2C/GluN2D-selective inhibitor QZN46 and the GluN2A inhibitors UBP608 and TCN201. These new agents do not bind within the l-glutamate or glycine binding sites, the ion channel pore or the N-terminal regulatory domain. Collectively, these new allosteric modulators appear to be acting at multiple novel sites on the NMDAR complex. Importantly, these agents display improved subtype-selectivity and as NMDAR PAMs and NAMs, they represent a new generation of potential NMDAR therapeutics.

Indexed as

Allosteric RegulationAnimalsHumansModels, MolecularReceptors, N-Methyl-D-AspartateReceptors, N-Methyl-D-Aspartate

Identifiers

PMID22269804
PMCPMC3360989
OpenAlexW2007906244

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.