Evidence map›Paper›PMID 30315107›Full record

ArticleThe Journal of biological chemistry2018

Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD.

Francisco Del Caño-Ochoa, Araceli Grande-García, María Reverte-López, Marco D'Abramo, Santiago Ramón-Maiques

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Crystal structure of Methanococcus jannaschii dihydroorotase with substrate bound.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Structural Analysis ofMolecules (Basel, Switzerland) · 2021
    Article
  11. Review
  12. Article
  13. Complexed Crystal Structure ofBioinorganic chemistry and applications · 2021
    Article
  14. Article
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 2 countries.

Francisco Del Caño-OchoaFrom the Department of Genome Dynamics and Function, Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid 28049, Spain.ORCID 0000-0003-3093-3103
Araceli Grande-Garcíathe Structural Biology Programme, Spanish National Cancer Research Centre (CNIO), Madrid 28029, Spain, and.ORCID 0000-0003-2619-5013
María Reverte-LópezFrom the Department of Genome Dynamics and Function, Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid 28049, Spain.
Marco D'Abramothe Department of Chemistry, Sapienza University of Rome, Rome 00185, Italy.
Santiago Ramón-MaiquesFrom the Department of Genome Dynamics and Function, Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Madrid 28049, Spain, santiago.ramon@cbm.csic.es.ORCID 0000-0001-9674-8088
Centro de Biología Molecular Severo Ochoa · ESSapienza University of Rome · ITSpanish National Cancer Research Centre · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dihydroorotase (DHOase) domain of the multifunctional protein carbamoyl-phosphate synthetase 2, aspartate transcarbamoylase, and dihydroorotase (CAD) catalyzes the third step in the

Indexed as

Aspartate CarbamoyltransferaseCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)CatalysisCatalytic DomainDihydroorotaseHumansMolecular Dynamics SimulationMutagenesisMutationPhenylalanineProtein ConformationProtein DomainsAspartate CarbamoyltransferaseCAD trifunctional enzymeCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)DihydroorotasePhenylalanineconformational changeenzyme kineticsenzyme mechanismmetalloenzymemolecular dynamicsmultifunctional enzymenucleoside/nucleotide biosynthesispyrimidinesite-directed mutagenesisX-ray crystallography

Identifiers

PMID30315107
PMCPMC6295737
OpenAlexW2897131628

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.