Evidence map›Paper›PMID 7685113›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain.

R Planells-Cases, W Sun, A V Ferrer-Montiel, M Montal

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

7 citing papers in PubMed, 60 citations in OpenAlex.

  1. Modulation of NMDA channel gating by CaScientific reports · 2016
    Article
  2. Molecular pharmacology of human NMDA receptors.Neurochemistry international · 2012
    Article
  3. An N-methyl-D-aspartate receptor channel blocker with neuroprotective activity.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  4. Article
  5. Alternative RNA splicing of the NMDA receptor NR1 mRNA in the neurons of the teleost electrosensory system.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  6. Article
  7. 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

4 authors at 1 institution in 1 country.

R Planells-CasesDepartment of Biology, University of California, San Diego, La Jolla 92093-0319.
W Sun
A V Ferrer-Montiel
M Montal
University of California, San Diego · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
MOLECULAR ANATOMY OF CHANNEL PROTEINS AND MENTAL ILLNESSK05MH000778 · NIMH · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI MONTAL, MAURICIO S · 1989 to 1993
–
MOLECULAR ANATOMY OF CHANNEL PROTEINS AND MENTAL ILLNESSR01MH044638 · NIMH · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI MONTAL, MAURICIO S · 1989 to 1991
–
NIGMS NIH HHS 5T32GM08326NIMH NIH HHS MH-00778NIMH NIH HHS MH-44638
6 · The paper itself

Abstract

A cDNA encoding a full-length N-methyl-D-aspartate (NMDA) receptor subunit 1, hNR1, was isolated from a human brain cDNA library. The hNR1 cDNA encodes an open reading frame of approximately 2.7 kb that shares high homology with the rat brain NMDA receptor subunit 1 and the mouse zeta 1 subunit. The hNR1 sequence, however, diverges from the rodent and murine homologs near the C terminus, suggesting that they represent alternatively spliced messages of the same gene. Oocytes injected with cRNA synthesized from the hNR1 cDNA express glutamate and NMDA-activated currents in the presence of glycine. Currents are blocked by the NMDA-receptor-specific antagonists 2-amino-5-phosphovaleric acid and 7-chlorokynurenate, and the open channel blockers MK-801 and phencyclidine, by Mg2+ ions in a voltage-dependent manner, and by Zn2+. Expressed hNR1 homomeric receptor channels exhibit the high Ca2+ permeability characteristic of neuronal NMDA receptors. Therefore, the cDNA clone hNR1 codes for a human brain NMDA receptor subunit cognate to the rodent and murine brain NR1 subunits.

Indexed as

2-Amino-5-phosphonovaleratealpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidAmino Acid SequenceAnimalsCloning, MolecularDizocilpine MaleateDNAFemaleFrontal LobeGene LibraryGlutamatesGlutamic AcidGlycineHumansIbotenic AcidKainic Acid2-Amino-5-phosphonovaleratealpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidDizocilpine MaleateDNAGlutamatesGlutamic AcidGlycineIbotenic AcidKainic AcidMacromolecular SubstancesN-MethylaspartateQuisqualic AcidReceptors, N-Methyl-D-AspartateRNA, Messenger

Identifiers

PMID7685113
PMCPMC46653
OpenAlexW2014408798

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.