Evidence map›Paper›PMID 32015122›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Conformational spread and dynamics in allostery of NMDA receptors.

Ryan J Durham, Nabina Paudyal, Elisa Carrillo, Nidhi Kaur Bhatia, David M Maclean, Vladimir Berka, Drew M Dolino, Alemayehu A Gorfe, Vasanthi Jayaraman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024
    Article
  4. Article
  5. Article
  6. d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  7. Review
  8. Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  9. Allosteric Competition and Inhibition in AMPA Receptors.bioRxiv : the preprint server for biology · 2023
    Article
  10. Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. AFrontiers in genetics · 2021
    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

9 authors at 2 institutions in 1 country.

Ryan J DurhamCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.ORCID 0000-0003-2739-8437
Nabina PaudyalCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.
Elisa CarrilloCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.
Nidhi Kaur BhatiaCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.
David M MacleanDepartment of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, NY 14642.ORCID 0000-0001-8294-6075
Vladimir BerkaCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.
Drew M DolinoCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030.
Alemayehu A GorfeMD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, University of Texas Health Science Center at Houston, Houston, TX 77030.
Vasanthi JayaramanCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, Houston, TX 77030; vasanthi.jayaraman@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USUniversity of Rochester Medical Center · US

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
Dynamics Of Ligand Gated Ion ChannelsR35GM122528 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI Vasanthi Jayaraman · 2017 to 2026
$6.2M
Decoding the structures and lipid binding specificity of small GTPase membrane anchorsR01GM124233 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI GORFE, ALEMAYEHU A., HANCOCK, JOHN F · 2018 to 2021
$1.3M
3D structure and function of Acid Sensing Ion channelsK99NS094761 · NINDS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MACLEAN, DAVID MALCOM · 2015 to 2016
$173k
Agonist induced conformational changes in the NMDA receptorF31GM130035 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DURHAM, RYAN JAMES · 2018 to 2020
$96k
NIGMS NIH HHS F31 GM130035NIGMS NIH HHS R01 GM124233NIGMS NIH HHS R35 GM122528NIGMS NIH HHS T32 GM008280NINDS NIH HHS K99 NS094761
6 · The paper itself

Abstract

Allostery can be manifested as a combination of repression and activation in multidomain proteins allowing for fine tuning of regulatory mechanisms. Here we have used single molecule fluorescence resonance energy transfer (smFRET) and molecular dynamics simulations to study the mechanism of allostery underlying negative cooperativity between the two agonists glutamate and glycine in the NMDA receptor. These data show that binding of one agonist leads to conformational flexibility and an increase in conformational spread at the second agonist site. Mutational and cross-linking studies show that the dimer-dimer interface at the agonist-binding domain mediates the allostery underlying the negative cooperativity. smFRET on the transmembrane segments shows that they are tightly coupled in the unliganded and single agonist-bound form and only upon binding both agonists the transmembrane domain explores looser packing which would facilitate activation.

Indexed as

Allosteric RegulationAnimalsBinding SitesDimerizationGlutamic AcidGlycineMolecular Dynamics SimulationProtein BindingProtein ConformationProtein DomainsRatsReceptors, N-Methyl-D-AspartateGlutamic AcidGlycineReceptors, N-Methyl-D-AspartateallosteryFRETMD simulationsNMDA receptors

Identifiers

PMID32015122
PMCPMC7035515
OpenAlexW3004039649

What OpenQuestion holds

Textmetadata
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.