Evidence map›Paper›PMID 24291102›Full record

ReviewEuropean journal of pharmacology2014

Roles of subunit phosphorylation in regulating glutamate receptor function.

John Q Wang, Ming-Lei Guo, Dao-Zhong Jin, Bing Xue, Eugene E Fibuch, Li-Min Mao

Abstract readReview
In one paragraph

Review in European journal of pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

51 citing papers in PubMed, 90 citations in OpenAlex.

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  17. Regulation of KInternational journal of molecular sciences · 2022
    Review
  18. Review
  19. Article
  20. Review
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.

John Q WangDepartment of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA; Department of Anesthesiology, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA. Electronic address: wangjq@umkc.edu.
Ming-Lei GuoDepartment of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.
Dao-Zhong JinDepartment of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.
Bing XueDepartment of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.
Eugene E FibuchDepartment of Anesthesiology, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.
Li-Min MaoDepartment of Basic Medical Science, School of Medicine, University of Missouri-Kansas City, Kansas City, MO 64108, USA.
University of Missouri–Kansas City · US

Funding

REGULATION OF GENE EXPRESSION IN STRIATAL NEURONSR01MH061469 · NIMH · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 2001 to 2024
$7.9M
Metabotropic Glutamate Regulation of Amphetamine ActionR01DA010355 · NIDA · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 2003 to 2017
$4.6M
METABOTROPIC GLUTAMATE REGULATION OF AMPHETAMINE ACTIONR29DA010355 · NIDA · UNIVERSITY OF MISSOURI KANSAS CITY · PI WANG, QIANG · 1997 to 2001
$198k
NIDA NIH HHS IHR01DA010355NIDA NIH HHS R01 DA010355NIMH NIH HHS R01 MH061469NIMH NIH HHS R01MH061469
6 · The paper itself

Abstract

Protein phosphorylation is an important mechanism for regulating ionotropic glutamate receptors (iGluRs). Early studies have established that major iGluR subtypes, including α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptors and N-methyl-d-aspartate (NMDA) receptors, are subject to phosphorylation. Multiple serine, threonine, and tyrosine residues predominantly within the C-terminal regions of AMPA receptor and NMDA receptor subunits have been identified as sensitive phosphorylation sites. These distinct sites undergo either constitutive phosphorylation or activity-dependent phosphorylation induced by changing cellular and synaptic inputs. An increasing number of synapse-enriched protein kinases have been found to phosphorylate iGluRs The common kinases include protein kinase A, protein kinase C, Ca(2+)/calmodulin-dependent protein kinase II, Src/Fyn non-receptor tyrosine kinases, and cyclin dependent kinase-5. Regulated phosphorylation plays a well-documented role in modulating the biochemical, biophysical, and functional properties of the receptor. In the future, identifying the precise mechanisms how phosphorylation regulates iGluR activities and finding the link between iGluR phosphorylation and the pathogenesis of various brain diseases, including psychiatric and neurodegenerative diseases, chronic pain, stroke, Alzheimer's disease and substance addiction, will be hot topics and could contribute to the development of novel pharmacotherapies, by targeting the defined phosphorylation process, for suppressing iGluR-related disorders.

Indexed as

AnimalsBrain DiseasesHumansPhosphorylationProtein SubunitsProtein TransportReceptors, AMPAReceptors, N-Methyl-D-AspartateProtein SubunitsReceptors, AMPAReceptors, N-Methyl-D-AspartateAMPACaMKIICdk5Excitatory amino acidNMDAPKAPKCTyrosine kinase

Identifiers

PMID24291102
PMCPMC3966912
OpenAlexW2047470842

What Socratic 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 Socratic graph.