Evidence map›Paper›PMID 32507980›Full record

ArticleMolecular diversity2021

Urease: a highly efficient biocatalyst for synthesis of polyhydroquinolines and polyhydroacridines from the ammonia formed in situ.

Gan Zhu, Yiqun Li

Abstract read
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In one paragraph

Article in Molecular diversity, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Gan ZhuDepartment of Chemistry, Jinan University, Guangzhou, 510632, China.
Yiqun LiDepartment of Chemistry, Jinan University, Guangzhou, 510632, China. tlyq@jnu.edu.cn.ORCID http://orcid.org/0000-0002-3303-1730
Jinan University · CN

Funding

Natural Science Foundation of Guangdong Province 2020A1515010399
6 · The paper itself

Abstract

Urease, a nickel-dependent enzyme, has a powerful catalytic activity to decompose urea into ammonia via hydrolysis reaction under mild condition. In the present work, urease was employed for the synthesis of two series of polyhydroquinoline and polyhydroacridine derivatives via one-pot condensation of the ammonia generated in situ from urea, aryl aldehydes, and dimedone or ethyl acetoacetate (i.e., Hantzsch-type reaction) in water under mild green condition. The valuable features of this enzymatic method are mild reaction conditions, short reaction times, wide substrate toleration, and high yield of products. The present work provides a novel enzymatic catalysis to synthesize polyhydroquinolines and polyhydroacridines and expands the application of urease in organic synthesis.

Indexed as

AmmoniaUreaseAcridinesBiocatalysisHydroxyquinolinesAcridinesAmmoniaHydroxyquinolinesUreaseMulticomponent reactionPolyhydroacridinePolyhydroquinolineSynthesisUrease

Identifiers

PMID32507980
OpenAlexW3033911141

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.