Evidence map›Paper›PMID 31416831›Full record

ArticleThe Journal of biological chemistry2019

The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates.

David Fernández-Justel, Rafael Peláez, José Luis Revuelta, Rubén M Buey

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. An IMPDH2 variant associated with neurodevelopmental disorder disrupts purine biosynthesis and somite organization.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. A journey into the regulatory secrets of theFrontiers in pharmacology · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.Protein science : a publication of the Protein Society · 2022
    Review
  16. Article
  17. IMPDH dysregulation in disease: a mini review.Biochemical Society transactions · 2022
    Review
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

David Fernández-JustelMetabolic Engineering Group, Departamento de Microbiología y Genética, Universidad de Salamanca, Campus Miguel de Unamuno, 37007 Salamanca, Spain.ORCID 0000-0001-5728-2756
Rafael PeláezLaboratorio de Química Orgánica y Farmacéutica, Departamento de Ciencias Farmacéuticas, Universidad de Salamanca, Campus Miguel de Unamuno, 37007 Salamanca, Spain.
José Luis RevueltaMetabolic Engineering Group, Departamento de Microbiología y Genética, Universidad de Salamanca, Campus Miguel de Unamuno, 37007 Salamanca, Spain revuelta@usal.es.
Rubén M BueyMetabolic Engineering Group, Departamento de Microbiología y Genética, Universidad de Salamanca, Campus Miguel de Unamuno, 37007 Salamanca, Spain ruben.martinez@usal.es.ORCID 0000-0003-1263-0221
Universidad de Salamanca · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

IMP dehydrogenase (IMPDH) is an essential enzyme that catalyzes the rate-limiting step in the

Indexed as

Protein ConformationAllosteric RegulationBacterial InfectionsBinding SitesCatalysisCrystallography, X-RayDinucleoside PhosphatesEremotheciumGuanine NucleotidesHumansIMP DehydrogenaseModels, MolecularNeoplasmsProtein DomainsScattering, Small AngleX-Ray DiffractionDinucleoside PhosphatesGuanine NucleotidesIMP Dehydrogenaseallosteric regulationBateman domainconformational changeconformational switchdinucleoside polyphosphatesIMP dehydrogenasemolecular sensorsmall-angle X-ray scattering (SAXS)structural biologyX-ray crystallography

Identifiers

PMID31416831
PMCPMC6779442
OpenAlexW2968697374

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.