Evidence map›Paper›PMID 32404369›Full record

ArticleThe Journal of biological chemistry2020

The ThiL enzyme is a valid antibacterial target essential for both thiamine biosynthesis and salvage pathways in

Hyung Jun Kim, Hyunjung Lee, Yunmi Lee, Inhee Choi, Yoonae Ko, Sangchul Lee, Soojin Jang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. 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
0.8field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. Review
  6. Chemical genetic interactions elucidate pathways controlling tuberculosis antibiotic efficacy during infection.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Metabolic Reprogramming ofJournal of proteome research · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Characterization of anBiochemistry · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. The Involvement of Thiamine Uptake in the Virulence ofPathogens (Basel, Switzerland) · 2022
    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

7 authors at 1 institution in 1 country.

Hyung Jun KimDiscovery Biology Department, Antibacterial Resistance Laboratory, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Hyunjung LeeDiscovery Biology Department, Antibacterial Resistance Laboratory, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Yunmi LeeDiscovery Biology Department, Antibacterial Resistance Laboratory, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Inhee ChoiTranslation Research Department, Medicinal Chemistry, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Yoonae KoTranslation Research Department, Medicinal Chemistry, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Sangchul LeeTranslation Research Department, Medicinal Chemistry, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea.
Soojin JangDiscovery Biology Department, Antibacterial Resistance Laboratory, Institut Pasteur Korea, Seongnam-si, Gyeonggi-do, Republic of Korea soojin.jang@ip-korea.org.
Institut Pasteur Korea · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thiamine pyrophosphate (TPP) is an essential cofactor for various pivotal cellular processes in all living organisms, including bacteria. Thiamine biosynthesis occurs in bacteria but not in humans; therefore, the enzymes in this pathway are attractive targets for antibiotic development. Among these enzymes, thiamine monophosphate kinase (ThiL) catalyzes the final step of this pathway, phosphorylating thiamine monophosphate to produce TPP. Here, we extensively investigated ThiL in

Indexed as

Bacterial ProteinsPhosphotransferases (Phosphate Group Acceptor)Anti-Bacterial AgentsEnzyme InhibitorsPseudomonas aeruginosaThiamineAnti-Bacterial AgentsBacterial ProteinsEnzyme InhibitorsPhosphotransferases (Phosphate Group Acceptor)Thiaminethiamin-phosphate kinaseantibacterial targetbacterial metabolismbacterial pathogenesisdrug targetinfectionPaThiLPseudomonas aeruginosathiaminethiamine monophosphate kinasevirulence

Identifiers

PMID32404369
PMCPMC7380198
OpenAlexW3025599489

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.