Evidence map›Paper›PMID 36752373›Full record

ArticleIUCrJ2023

Comparison of the structure and activity of thioredoxin 2 and thioredoxin 1 from Acinetobacter baumannii.

Ye Ji Chang, Ji Hye Sung, Chang Sup Lee, Jun Hyuck Lee, Hyun Ho Park

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

5 authors at 3 institutions in 1 country.

Ye Ji ChangCollege of Pharmacy, Chung-Ang University, Seoul 06974, Republic of Korea.
Ji Hye SungCollege of Pharmacy, Chung-Ang University, Seoul 06974, Republic of Korea.ORCID 0000-0002-5971-6666
Chang Sup LeeCollege of Pharmacy and Research Institute of Pharmaceutical Science, Gyeongsang National University, Jinju 52828, Republic of Korea.
Jun Hyuck LeeUnit of Research for Practical Application, Korea Polar Research Institute, Incheon 21990, Republic of Korea.ORCID 0000-0002-4831-2228
Hyun Ho ParkCollege of Pharmacy, Chung-Ang University, Seoul 06974, Republic of Korea.ORCID 0000-0001-9928-0847
Chung-Ang University · KRGyeongsang National University · KRKorea Polar Research Institute · KR

Funding

Korea Polar Research Institute PM22030National Research Foundation of Korea 2018R1A4A1023822National Research Foundation of Korea 2021R1A2C3003331
6 · The paper itself

Abstract

Thioredoxin (Trx) is essential in a redox-control system, with many bacteria containing two Trxs: Trx1 and Trx2. Due to a Trx system's critical function, Trxs are targets for novel antibiotics. Here, a 1.20 Å high-resolution structure of Trx2 from Acinetobacter baumannii (abTrx2), an antibiotic resistant pathogenic superbug, is elucidated. By comparing Trx1 and Trx2, it is revealed that the two Trxs possess similar activity, although Trx2 contains an additional N-terminal zinc-finger domain and exhibits more flexible properties in solution. Finally, it is shown that the Trx2 zinc-finger domain might be rotatable and that proper zinc coordination at the zinc-finger domain is critical to abTrx2 activity. This study enhances understanding of the Trx system and will facilitate the design of novel antibiotics.

Indexed as

Acinetobacter baumanniiOxidation-ReductionThioredoxinsZincThioredoxinsZincAcinetobacter baumanniicrystal structureredox homeostasissuperbugsthioredoxinzinc-finger domains

Identifiers

PMID36752373
PMCPMC9980383
OpenAlexW4319460494

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.