Article in The Journal of general physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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.
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
14 authors.
James S LottiCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0003-4541-1359
Jed T SyrenneCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-5267-7967
Avery J BentonCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0001-9063-6712
Ahmad Al-MousawiDepartment for Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID 0009-0007-1884-0226
Lauren E CornelisonCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-5294-1385
Christopher J TrolinderCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0009-0002-4970-2209
Feng YiCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-0049-742X
Zhucheng ZhangDepartment for Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID 0009-0006-3814-5637
Cindee K Yates-HansenCenter for Biomolecular Structure and Dynamics, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0001-8116-2586
Levi J McClellandCenter for Biomolecular Structure and Dynamics, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-0868-8925
James BoscoCenter for Biomolecular Structure and Dynamics, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0009-0006-7141-8705
Andrew R RauCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-7983-6809
Rasmus P ClausenDepartment for Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0001-9466-9431
Kasper B HansenCenter for Structural and Functional Neuroscience, Division of Biological and Biomedical Sciences, University of Montana, Missoula, MT, USA.ORCID 0000-0002-3303-4819
Funding
Research Core (Developmental Research Project Program)P20GM103474 · NIGMS · MONTANA STATE UNIVERSITY - BOZEMAN · PI Ann Therese Bertagnolli · 2012 to 2026
$60.0M
X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Vivian Stojanoff · 2019 to 2026
$38.6M
Surveillance genome sequencing to detect SARS-CoV-2 virus variants in MontanaP30GM140963 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2021 to 2025
$6.9M
Structural and functional investigation of negative allosteric NMDA receptor modulationR01NS097536 · NINDS · UNIVERSITY OF MONTANA · PI Kasper Boe Hansen · 2016 to 2026
$3.4M
Brookhaven National Laboratory DE-SC0012704DOE Office of Biological and Environmental Research KP1607011NIGMS NIH HHS P20 GM103474NIGMS NIH HHS P20GM103474NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P30GM133893NIGMS NIH HHS P30 GM140963NIGMS NIH HHS P30GM140963NIH HHS R01NS097536NINDS NIH HHS R01 NS097536U.S. Department of Energy
6 · The paper itself
Abstract
NMDA-type ionotropic glutamate receptors mediate excitatory neurotransmission and synaptic plasticity, but aberrant signaling by these receptors is also implicated in brain disorders. Here, we present the binding site and the mechanism of action for UCM-101, a novel negative NMDA receptor modulator that produces full inhibition of NMDA receptor-mediated excitatory postsynaptic currents in hippocampal CA pyramidal neurons from juvenile mouse brain slices. UCM-101 has a 59-fold higher binding affinity at GluN1/2A compared with GluN1/2B receptors and inhibits diheteromeric GluN1/2A and triheteromeric GluN1/2A/2B receptors with IC50 values of 110 and 240 nM, respectively, in the presence of 1 µM glycine. The novel binding mode for UCM-101 is revealed in a high-resolution crystal structure of the GluN1/2A agonist binding domain heterodimer. UCM-101 and its analog TCN-213 inhibit NMDA receptors by negatively modulating co-agonist binding to the GluN1 subunit via an allosteric mechanism that is conserved with previously described GluN2A-selective antagonists, TCN-201 and MPX-004. Despite the shared mechanism of action, the structural determinants that mediate subunit selectivity for UCM-101 are distinct from those of TCN-201 and MPX-004. These findings provide detailed insights into the binding site and mechanism of action of a novel NMDA receptor modulator and open new avenues for the development of NMDA receptor ligands with therapeutic potential.
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.
Novel binding mode for negative allosteric NMDA receptor modulators. · full record | OpenQuestion