Evidence map›Paper›PMID 20091669›Full record

ReviewProtein science : a publication of the Protein Society2010

Pyrroline-5-carboxylate synthase and proline biosynthesis: from osmotolerance to rare metabolic disease.

Isabel Pérez-Arellano, Francisco Carmona-Alvarez, Ana I Martínez, Jesús Rodríguez-Díaz, Javier Cervera

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Proline Tagging for Stress Tolerance in Plants.International journal of genomics · 2025
    Review
  16. Article
  17. LysineFrontiers in molecular neuroscience · 2025
    Review
  18. Targeting the glutamine-arginine-proline metabolism axis in cancer.Journal of enzyme inhibition and medicinal chemistry · 2024
    Review
  19. Transcriptomic Profile of Tef (Plants (Basel, Switzerland) · 2024
    Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 1 country.

Isabel Pérez-ArellanoMolecular Recognition Laboratory, Centro de Investigación Príncipe Felipe, Valencia, Spain.
Francisco Carmona-Alvarez
Ana I Martínez
Jesús Rodríguez-Díaz
Javier Cervera
Centro de Investigacion Principe Felipe · ESCentre for Biomedical Network Research on Rare Diseases · ESCentro de Investigación Biomédica en Red · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyrroline-5-carboxylate synthase (P5CS) is a bifunctional enzyme that exhibits glutamate kinase (GK) and gamma-glutamyl phosphate reductase (GPR) activities. The enzyme is highly relevant in humans because it belongs to a combined route for the interconversion of glutamate, ornithine and proline. The deficiency of P5CS activity in humans is associated with a rare, inherited metabolic disease. It is well established that some bacteria and plants accumulate proline in response to osmotic stress. The alignment of P5CSs from different species and analysis of the solved structures of GK and GPR reveal high sequence and structural conservation. The information acquired from different mutant enzymes with increased osmotolerant properties, together with the position of the insertion found in the longer human isoform, permit the delimitation of the regulatory site of GK and P5CS and the proposal of a model of P5CS architecture. Additionally, the GK moiety of the human enzyme has been modeled and the known clinical mutations and polymorphisms have been mapped.

Indexed as

Amino Acid SequenceAnimalsBacteriaHumansMetabolic DiseasesOrnithine-Oxo-Acid TransaminaseOsmotic FragilityOsmotic PressurePlantsProlineProtein ConformationSequence AlignmentOrnithine-Oxo-Acid TransaminaseProline

Identifiers

PMID20091669
PMCPMC2866264
OpenAlexW2138492495

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.