Evidence map›Paper›PMID 27213314›Full record

ReviewMolecules (Basel, Switzerland)2016

Flavin-Dependent Thymidylate Synthase as a New Antibiotic Target.

Michael Choi, Kalani Karunaratne, Amnon Kohen

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Megaplasmids associate withbioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Effect of 5-fluorouracil onFrontiers in microbiology · 2025
    Review
  4. Review
  5. Article
  6. Pathways of thymidine hypermodification.Nucleic acids research · 2022
    Article
  7. Article
  8. Riboswitches as Drug Targets for Antibiotics.Antibiotics (Basel, Switzerland) · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Structural Comparison ofMolecules (Basel, Switzerland) · 2019
    Article
  14. Article
  15. 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

3 authors.

Michael ChoiDepartment of Chemistry, The University of Iowa, Iowa City, IA 52242-1727, USA. michael-a-choi@uiowa.edu.
Kalani KarunaratneDepartment of Chemistry, The University of Iowa, Iowa City, IA 52242-1727, USA. kalaniudara-karunaratne@uiowa.edu.
Amnon KohenDepartment of Chemistry, The University of Iowa, Iowa City, IA 52242-1727, USA. amnon-kohen@uiowa.edu.

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
PREDOCTORAL TRAINING PROGRAM IN BIOTECHNOLOGYT32GM008365 · NIGMS · UNIVERSITY OF IOWA · PI KERNS, ROBERT JOHN · 1990 to 2021
$3.8M
Mechanistic Studies of Flavin Dependent Thymidylate SynthaseR01GM110775 · NIGMS · UNIVERSITY OF IOWA · PI QUINN, DANIEL M · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM110775NIGMS NIH HHS T32 GM007337NIGMS NIH HHS T32 GM008365
6 · The paper itself

Abstract

In humans de novo synthesis of 2'-deoxythymidine-5'-monophosphate (dTMP), an essential building block of DNA, utilizes an enzymatic pathway requiring thymidylate synthase (TSase) and dihydrofolate reductase (DHFR). The enzyme flavin-dependent thymidylate synthase (FDTS) represents an alternative enzymatic pathway to synthesize dTMP, which is not present in human cells. A number of pathogenic bacteria, however, depend on this enzyme in lieu of or in conjunction with the analogous human pathway. Thus, inhibitors of this enzyme may serve as antibiotics. Here, we review the similarities and differences of FDTS vs. TSase including aspects of their structure and chemical mechanism. In addition, we review current progress in the search for inhibitors of flavin dependent thymidylate synthase as potential novel therapeutics.

Indexed as

Anti-Bacterial AgentsBacteriaFlavinsHumansInfectionsKineticsMultienzyme ComplexesTetrahydrofolate DehydrogenaseThymidine MonophosphateThymidylate SynthaseAnti-Bacterial AgentsFlavinsMultienzyme ComplexesTetrahydrofolate DehydrogenaseThymidine MonophosphateThymidylate Synthasethymidylate synthase-dihydrofolate reductaseantibioticenzymeflavinmechanismthymidylate synthase

Identifiers

PMID27213314
PMCPMC4913046

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.