Evidence map›Paper›PMID 35741038›Full record

ReviewCells2022

Contribution of Model Organisms to Investigating the Far-Reaching Consequences of PRPP Metabolism on Human Health and Well-Being.

Eziuche A Ugbogu, Lilian M Schweizer, Michael Schweizer

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 22 citations in OpenAlex.

  1. 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.

Eziuche A UgboguSchool of Life Sciences, Heriot Watt University, Edinburgh EH14 4AS, UK.ORCID 0000-0003-3145-5473
Lilian M SchweizerSchool of Life Sciences, Heriot Watt University, Edinburgh EH14 4AS, UK.ORCID 0000-0002-4967-7958
Michael SchweizerInstitute of Biological Chemistry, Biophysics & Engineering (IB3), School of Engineering &Physical Sciences, Heriot Watt University, Edinburgh EH14 4AS, UK.ORCID 0000-0001-7458-5783
Heriot-Watt University · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

Phosphoribosyl pyrophosphate synthetase (PRS EC 2.7.6.1) is a rate-limiting enzyme that irreversibly catalyzes the formation of phosphoribosyl pyrophosphate (PRPP) from ribose-5-phosphate and adenosine triphosphate (ATP). This key metabolite is required for the synthesis of purine and pyrimidine nucleotides, the two aromatic amino acids histidine and tryptophan, the cofactors nicotinamide adenine dinucleotide (NAD

Indexed as

Phosphoribosyl PyrophosphateZebrafishAdenosine TriphosphateAnimalsHumansNADNeoplasm Recurrence, LocalRibose-Phosphate PyrophosphokinaseSaccharomyces cerevisiaeAdenosine TriphosphateNADPhosphoribosyl PyrophosphateRibose-Phosphate Pyrophosphokinaseageingcancercell signallingCMTX5CWI pathwayDanio rerioDFN2/DFNX1eukaryotic model organismshuman neuropathies: Arts syndromephosphoribosyl pyrophosphate synthetase (PRS/PRPS)Saccharomyces cerevisiae

Identifiers

PMID35741038
PMCPMC9221600
OpenAlexW4282834136

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.