Evidence map›Paper›PMID 29540480›Full record

ArticleThe Journal of biological chemistry2018

Structural basis for the catalytic mechanism and α-ketoglutarate cooperativity of glutamate dehydrogenase.

Prem Prakash, Narayan S Punekar, Prasenjit Bhaumik

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.5field-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

13 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  6. Quantifying Reductive Amination in Nonenzymatic Amino Acid Synthesis.Angewandte Chemie (International ed. in English) · 2022
    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

3 authors at 1 institution in 1 country.

Prem PrakashFrom the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai-400076, India.
Narayan S PunekarFrom the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai-400076, India.
Prasenjit BhaumikFrom the Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Powai, Mumbai-400076, India pbhaumik@iitb.ac.in.
Indian Institute of Technology Bombay · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamate dehydrogenase (GDH) is a key enzyme connecting carbon and nitrogen metabolism in all living organisms. Despite extensive studies on GDHs from both prokaryotic and eukaryotic organisms in the last 40 years, the structural basis of the catalytic features of this enzyme remains incomplete. This study reports the structural basis of the GDH catalytic mechanism and allosteric behavior. We determined the first high-resolution crystal structures of glutamate dehydrogenase from the fungus

Indexed as

Allosteric RegulationAmmoniaAspergillus nigerCatalytic DomainCrystallography, X-RayFungal ProteinsGlutamate DehydrogenaseGlutamatesNADPStructure-Activity Relationshipalpha-ketoglutamic acidAmmoniaFungal ProteinsGlutamate DehydrogenaseGlutamatesNADPallosteric regulationAspergillus nigercooperativitycrystal structuredehydrogenaseenzyme catalysisenzyme mechanismfungal GDHglutamate dehydrogenasereaction mechanism

Identifiers

PMID29540480
PMCPMC5925808
OpenAlexW2790688800

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.