Evidence map›Paper›PMID 24352816›Full record

ReviewNeurochemical research2014

The discovery of human of GLUD2 glutamate dehydrogenase and its implications for cell function in health and disease.

Pullanipally Shashidharan, Andreas Plaitakis

Abstract readReview
In one paragraph

Review in Neurochemical research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 24% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026
    Review
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  7. Mitochondrial Differentiation during Spermatogenesis: Lessons fromInternational journal of molecular sciences · 2024
    Review
  8. A comparative analysis of fruit fly and human glutamate dehydrogenases inFrontiers in cell and developmental biology · 2023
    Article
  9. Article
  10. Biomedicines · 2021
    Review
  11. Review
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  14. Novel genetic features of human and mouse Purkinje cell differentiation defined by comparative transcriptomics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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

2 authors at 2 institutions in 2 countries.

Pullanipally ShashidharanDepartment of Neurology, Icahn School of Medicine at Mount Sinai, Box 1137, One Gustave L Levy Place, New York, NY, 10029, USA, pullani.shashi@mssm.edu.
Andreas Plaitakis
Icahn School of Medicine at Mount Sinai · USUniversity of Crete · GR

Funding

BRAIN TORSIN-A AND CHILDHOOD ONSET DYSTONIAR01NS043038 · NINDS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SHASHIDHARAN, PULLANIPALLY · 2002 to 2012
$3.2M
NINDS NIH HHS NS43038NINDS NIH HHS R01 NS043038
6 · The paper itself

Abstract

While the evolutionary changes that led to traits unique to humans remain unclear, there is increasing evidence that enrichment of the human genome through DNA duplication processes may have contributed to traits such as bipedal locomotion, higher cognitive abilities and language. Among the genes that arose through duplication in primates during the period of increased brain development was GLUD2, which encodes the hGDH2 isoform of glutamate dehydrogenase expressed in neural and other tissues. Glutamate dehydrogenase GDH is an enzyme central to the metabolism of glutamate, the main excitatory neurotransmitter in mammalian brain involved in a multitude of CNS functions, including cognitive processes. In nerve tissue GDH is expressed in astrocytes that wrap excitatory synapses, where it is thought to play a role in the metabolic fate of glutamate removed from the synaptic cleft during excitatory transmission. Expression of GDH rises sharply during postnatal brain development, coinciding with nerve terminal sprouting and synaptogenesis. Compared to the original hGDH1 (encoded by the GLUD1 gene), which is potently inhibited by GTP generated by the Krebs cycle, hGDH2 can function independently of this energy switch. In addition, hGDH2 can operate efficiently in the relatively acidic environment that prevails in astrocytes following glutamate uptake. This adaptation is thought to provide a biological advantage by enabling enhanced enzyme catalysis under intense excitatory neurotransmission. While the novel protein may help astrocytes to handle increased loads of transmitter glutamate, dissociation of hGDH2 from GTP control may render humans vulnerable to deregulation of this enzyme's function. Here we will retrace the cloning and characterization of the novel GLUD2 gene and the potential implications of this discovery in the understanding of mechanisms that permitted the brain and other organs that express hGDH2 to fine-tune their functions in order to meet new challenging demands. In addition, the potential role of gain-of-function of hGDH2 variants in human neurodegenerative processes will be considered.

Indexed as

AnimalsAstrocytesBrainGlutamate DehydrogenaseHumansMutagenesis, Site-DirectedProtein IsoformsGLUD2 protein, humanGlutamate DehydrogenaseProtein Isoforms

Identifiers

PMID24352816
PMCPMC3944346
OpenAlexW2073347469

What OpenQuestion 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 OpenQuestion graph.