Evidence map›Paper›PMID 28378791›Full record

ArticleScientific reports2017

Computationally Discovered Potentiating Role of Glycans on NMDA Receptors.

Anton V Sinitskiy, Nathaniel H Stanley, David H Hackos, Jesse E Hanson, Benjamin D Sellers, Vijay S Pande

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  11. Glutamate and Glycine Binding to the NMDA Receptor.Structure (London, England : 1993) · 2018
    Article
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  13. Article
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

6 authors at 1 institution in 1 country.

Anton V SinitskiyDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Nathaniel H StanleyStanford ChEM-H, Stanford University, Stanford, CA 94305, USA.
David H HackosDepartment of Neuroscience, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA.
Jesse E HansonDepartment of Neuroscience, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA.
Benjamin D SellersDepartment of Discovery Chemistry, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA.
Vijay S PandeDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Stanford University · US

Funding

Topology, nucleation, and the protein folding barrierR01GM062868 · NIGMS · STANFORD UNIVERSITY · PI PANDE, VIJAY S · 2002 to 2018
$5.5M
NIGMS NIH HHS R01 GM062868
6 · The paper itself

Abstract

N-methyl-D-aspartate receptors (NMDARs) are glycoproteins in the brain central to learning and memory. The effects of glycosylation on the structure and dynamics of NMDARs are largely unknown. In this work, we use extensive molecular dynamics simulations of GluN1 and GluN2B ligand binding domains (LBDs) of NMDARs to investigate these effects. Our simulations predict that intra-domain interactions involving the glycan attached to residue GluN1-N440 stabilize closed-clamshell conformations of the GluN1 LBD. The glycan on GluN2B-N688 shows a similar, though weaker, effect. Based on these results, and assuming the transferability of the results of LBD simulations to the full receptor, we predict that glycans at GluN1-N440 might play a potentiator role in NMDARs. To validate this prediction, we perform electrophysiological analysis of full-length NMDARs with a glycosylation-preventing GluN1-N440Q mutation, and demonstrate an increase in the glycine EC50 value. Overall, our results suggest an intramolecular potentiating role of glycans on NMDA receptors.

Indexed as

AnimalsBinding SitesGene ExpressionGlycineGlycosylationHumansKineticsMolecular Dynamics SimulationMutationNerve Tissue ProteinsOocytesPatch-Clamp TechniquesPolysaccharidesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandGlycineGRIN1 protein, humanNerve Tissue ProteinsNR2B NMDA receptorPolysaccharidesReceptors, N-Methyl-D-AspartateRecombinant Proteins

Identifiers

PMID28378791
PMCPMC5381272
OpenAlexW2594383381

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.