Evidence map›Paper›PMID 27983623›Full record

ReviewBiology2016

Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implications.

Victoria Bunik, Artem Artiukhov, Vasily Aleshin, Garik Mkrtchyan

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Review
  3. Changes in the brain [NADFrontiers in aging neuroscience · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. A comparative analysis of fruit fly and human glutamate dehydrogenases inFrontiers in cell and developmental biology · 2023
    Article
  15. Article
  16. Article
  17. Heliyon · 2022
    Article
  18. Article
  19. Article
  20. 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.

Victoria BunikA.N.Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow 19991, Russia. bunik@belozersky.msu.ru.
Artem ArtiukhovFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 19991, Russia. whitelord32br@gmail.com.
Vasily AleshinFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 19991, Russia. Aleshin_vasily@mail.ru.
Garik MkrtchyanFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 19991, Russia. g.v.mkrtchyan@gmail.com.
Lomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamate dehydrogenase (GDH) of animal cells is usually considered to be a mitochondrial enzyme. However, this enzyme has recently been reported to be also present in nucleus, endoplasmic reticulum and lysosomes. These extramitochondrial localizations are associated with moonlighting functions of GDH, which include acting as a serine protease or an ATP-dependent tubulin-binding protein. Here, we review the published data on kinetics and localization of multiple forms of animal GDH taking into account the splice variants, post-translational modifications and GDH isoenzymes, found in humans and apes. The kinetic properties of human GLUD1 and GLUD2 isoenzymes are shown to be similar to those published for GDH1 and GDH2 from bovine brain. Increased functional diversity and specific regulation of GDH isoforms due to alternative splicing and post-translational modifications are also considered. In particular, these structural differences may affect the well-known regulation of GDH by nucleotides which is related to recent identification of thiamine derivatives as novel GDH modulators. The thiamine-dependent regulation of GDH is in good agreement with the fact that the non-coenzyme forms of thiamine, i.e., thiamine triphosphate and its adenylated form are generated in response to amino acid and carbon starvation.

Indexed as

acetylationadenylated thiamine triphosphateglutamate dehydrogenase alternative splicingglutamate dehydrogenase isoenzymesglutamate dehydrogenase isoformsnucleotide-dependent regulation

Identifiers

PMID27983623
PMCPMC5192433
OpenAlexW2563521501

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.