Evidence map›Paper›PMID 22942686›Full record

ReviewInternational journal of molecular sciences2012

Glutamine synthetase in legumes: recent advances in enzyme structure and functional genomics.

Marco Betti, Margarita García-Calderón, Carmen M Pérez-Delgado, Alfredo Credali, Guillermo Estivill, Francisco Galván, José M Vega, Antonio J Márquez

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
8.0field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 59 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Marco BettiDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Margarita García-CalderónDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Carmen M Pérez-DelgadoDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Alfredo CredaliDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Guillermo EstivillDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Francisco GalvánDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
José M VegaDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Antonio J MárquezDepartment of Vegetal Biochemistry and Molecular Biology, Faculty of Chemistry, University of Seville, Apartado 1203, Sevilla 41071, Spain.
Universidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamine synthetase (GS) is the key enzyme involved in the assimilation of ammonia derived either from nitrate reduction, N(2) fixation, photorespiration or asparagine breakdown. A small gene family is encoding for different cytosolic (GS1) or plastidic (GS2) isoforms in legumes. We summarize here the recent advances carried out concerning the quaternary structure of GS, as well as the functional relationship existing between GS2 and processes such as nodulation, photorespiration and water stress, in this latter case by means of proline production. Functional genomic analysis using GS2-minus mutant reveals the key role of GS2 in the metabolic control of the plants and, more particularly, in carbon metabolism.

Indexed as

AnimalsCrystallography, X-RayFabaceaeGenes, PlantGlutamate-Ammonia LigaseHumansModels, MolecularNitrogen FixationPlant ProteinsPlastidsProtein ConformationGlutamate-Ammonia LigasePlant Proteinsfunctional genomicsglutamine synthetaseLotus japonicusnitrogen metabolism

Identifiers

PMID22942686
PMCPMC3430217
OpenAlexW2065677195

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.