Evidence map›Paper›PMID 36446640›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2023

An overview: metal-based inhibitors of urease.

Wei Yang, Zhiyun Peng, Guangcheng Wang

Open access · goldAbstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

9 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Discovery ofFuture medicinal chemistry · 2025
    Article
  6. Review
  7. Article
  8. A review for non-antibiotic treatment ofFrontiers in microbiology · 2024
    Review
  9. 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

3 authors at 1 institution in 1 country.

Wei YangClinical Trails Center, The Affiliated Hospital of Guizhou Medical University, Guiyang, China.
Zhiyun PengClinical Trails Center, The Affiliated Hospital of Guizhou Medical University, Guiyang, China.
Guangcheng WangState Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Provincial Key Laboratory of Pharmaceutics, Guizhou Medical University, Guiyang, China.ORCID 0000-0001-9104-337X
Guiyang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Urease is a kind of nickel-dependent metalloenzyme, which exists in the biological world widely, and can catalyse the hydrolysis of urea into ammonia and carbon dioxide to provide a nitrogen source for organisms. Urease has important uses in agriculture and medicine because it can catalyse the production of ammonia. Therefore, in this review, metal-based inhibitors of urease will be summarised according to different transition metal ions. Including the urease inhibition, structure-activity relationship, and molecular docking. Importantly, among these reviewed effective urease inhibitors, most of copper metal complexes exhibited stronger urease inhibition with IC

Indexed as

MetalloproteinsUreaseAmmoniaMetalsMolecular Docking SimulationAmmoniaMetalloproteinsMetalsUreasemetal-based urease inhibitormolecular dockingReviewstructure–activity relationshipUrease

Identifiers

PMID36446640
PMCPMC11003495
OpenAlexW4310570698

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.