Evidence map›Paper›PMID 15052410›Full record

ReviewCellular and molecular life sciences : CMLS2004

Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate.

R H H van den Heuvel, B Curti, M A Vanoni, A Mattevi

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.4field-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

29 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Deciphering guanidine assimilation and riboswitch-based gene regulation in cyanobacteria for synthetic biology applications.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  4. Review
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  9. Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023
    Article
  10. A Reduced FJournal of bacteriology · 2022
    Article
  11. Article
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  16. Article
  17. Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017
    Review
  18. Article
  19. 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

4 authors at 3 institutions in 2 countries.

R H H van den HeuvelDepartment of Genetics and Microbiology, University of Pavia, Italy.
B Curti
M A Vanoni
A Mattevi
University of Milan · ITUniversity of Pavia · ITUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamate synthase is a multicomponent iron-sulfur flavoprotein belonging to the class of N-terminal nucleophile amidotransferases. It catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. In recent years the X-ray structures of the ferredoxin-dependent glutamate synthase and of the a subunit of the NADPH-dependent glutamate synthase have become available. Thanks to X-ray crystallography, it is now known that the ammonia reaction intermediate is transferred via an intramolecular tunnel from the amidotransferase domain to the synthase domain over a distance of about 32A. Although ammonia channeling is a recurrent theme for N-terminal nucleophile and triad-type amidotransferases, the molecular mechanisms of ammonia transfer and its control are different for each known amidotransferase. This review focuses on the intriguing mechanism of action and self-regulation of glutamate synthase with a special focus on the structural data.

Indexed as

Signal TransductionCatalytic DomainGlutamate SynthaseGlutamic AcidGlutamineLigandsModels, MolecularOxidation-ReductionProtein ConformationGlutamate SynthaseGlutamic AcidGlutamineLigands

Identifiers

PMID15052410
PMCPMC11138638
OpenAlexW2026226194

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.