Evidence map›Paper›PMID 30197036›Full record

ArticleStructure (London, England : 1993)2018

Trypanosomatid Deoxyhypusine Synthase Activity Is Dependent on Shared Active-Site Complementation between Pseudoenzyme Paralogs.

Gustavo A Afanador, Diana R Tomchick, Margaret A Phillips

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Polyamine Metabolism inMedical sciences (Basel, Switzerland) · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Flexible NADInternational journal of molecular sciences · 2020
    Article
  16. Article
  17. Article
  18. Polyamines in protozoan pathogens.The Journal of biological chemistry · 2018
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Gustavo A AfanadorDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Diana R TomchickDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Margaret A PhillipsDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: margaret.phillips@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

TRYPANSOMIASIS--MOLECULAR APPROACHES TO CHEMOTHERAPYR01AI034432 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI PHILLIPS, MARGARET A. · 1995 to 2024
$4.9M
Polyamine and trypanothione metabolism in Trypanosoma bruceiR37AI034432 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI PHILLIPS, MARGARET A. · 2009 to 2018
$4.0M
NIAID NIH HHS R01 AI034432NIAID NIH HHS R37 AI034432
6 · The paper itself

Abstract

Trypanosoma brucei is a neglected tropical disease endemic to Africa. The polyamine spermidine is essential for post-translational hypusine modification of eukaryotic initiation factor 5A (eIF5A), which is catalyzed by deoxyhypusine synthase (TbDHS). In trypanosomatids, deoxyhypusine synthase (DHS) activity is dependent on heterotetramer formation between two paralogs, DHSc and DHSp, both with minimal activity on their own due to missing catalytic residues. We determined the X-ray structure of TbDHS showing a single functional shared active site is formed at the DHSc/DHSp heterodimer interface, with deficiencies in one subunit complemented by the other. Each heterodimer contains two NAD

Indexed as

AnimalsCatalytic DomainCrystallography, X-RayHumansModels, MolecularNADOxidoreductases Acting on CH-NH Group DonorsProtein MultimerizationProtozoan ProteinsSpecies SpecificitySubstrate SpecificityTrypanosoma brucei bruceideoxyhypusine synthaseNADOxidoreductases Acting on CH-NH Group DonorsProtozoan Proteinsdeoxyhypusine synthaseeIF5AhypusinepolyaminespseudoenzymeTrypanosoma bruceitrypanosomatids

Identifiers

PMID30197036
PMCPMC6221947
OpenAlexW2891642030

What OpenQuestion holds

Textmetadata
LicenceTDM
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.