Evidence map›Paper›PMID 34948458›Full record

ArticleInternational journal of molecular sciences2021

New Inhibitors of Laccase and Tyrosinase by Examination of Cross-Inhibition between Copper-Containing Enzymes.

Dinesh Chaudhary, Fangchen Chong, Trilok Neupane, Joonhyeok Choi, Jun-Goo Jee

Open access · goldAbstract readComparative Study
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-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

7 citing papers in PubMed, 10 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

5 authors at 1 institution in 1 country.

Dinesh ChaudharyResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Korea.
Fangchen ChongResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Korea.
Trilok NeupaneResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Korea.
Joonhyeok ChoiResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Korea.
Jun-Goo JeeResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Korea.
Kyungpook National University · KR

Funding

the 4TH BK21 project (Educational Research Group for Platform development of management of emerging infectious disease) of the Korean ministry of education 5199990614732the Bio & Medical Technology Development Program of the National Research Foundation (NRF) funded by the Ministry of Science & ICT 2017M3A9G8083382
6 · The paper itself

Abstract

Coppers play crucial roles in the maintenance homeostasis in living species. Approximately 20 enzyme families of eukaryotes and prokaryotes are known to utilize copper atoms for catalytic activities. However, small-molecule inhibitors directly targeting catalytic centers are rare, except for those that act against tyrosinase and dopamine-β-hydroxylase (DBH). This study tested whether known tyrosinase inhibitors can inhibit the copper-containing enzymes, ceruloplasmin, DBH, and laccase. While most small molecules minimally reduced the activities of ceruloplasmin and DBH, aside from known inhibitors, 5 of 28 tested molecules significantly inhibited the function of laccase, with the K

Indexed as

AgaricalesBiocatalysisCatalytic DomainCeruloplasminCheminformaticsCopperDopamine beta-HydroxylaseEnzyme InhibitorsFungal ProteinsFungiHumansLaccaseModels, MolecularProtein ConformationSmall Molecule LibrariesCeruloplasminCopperDopamine beta-HydroxylaseEnzyme InhibitorsFungal ProteinsLaccaseSmall Molecule Librariesceruloplasmincheminformaticsdopamine-β-hydroxylaselaccasetyrosinase

Identifiers

PMID34948458
PMCPMC8707586
OpenAlexW4200481871

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.