Evidence map›Paper›PMID 35059457›Full record

ArticleBioMed research international2022

Molecular Docking, Synthesis, and Tyrosinase Inhibition Activity of Acetophenone Amide: Potential Inhibitor of Melanogenesis.

Yasir Nazir, Hummera Rafique, Sadia Roshan, Shazia Shamas, Zaman Ashraf, Muhammad Rafiq, Tehreem Tahir, Zia-Ur-Rahman Qureshi, Alvina Aslam, Muhammad Hassham Hassan Bin Asad

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
5.0field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

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  6. Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025
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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

10 authors at 7 institutions in 1 country.

Yasir NazirDepartment of Chemistry, Allama Iqbal Open University, Islamabad, Pakistan.
Hummera RafiqueDepartment of Chemistry, University of Gujrat, Gujrat 50700, Pakistan.
Sadia RoshanDepartment of Zoology, University of Gujrat, Gujrat 50700, Pakistan.
Shazia ShamasDepartment of Zoology, University of Gujrat, Gujrat 50700, Pakistan.
Zaman AshrafDepartment of Chemistry, Allama Iqbal Open University, Islamabad, Pakistan.ORCID https://orcid.org/0000-0002-6620-9080
Muhammad RafiqDepartment of Physiology and Biochemistry, Faculty of Bio-Sciences, Cholistan University of Veterinary and Animal Sciences, Bahawalpur 63100, Pakistan.
Tehreem TahirInstitute of Biochemistry, Biotechnology and Bioinformatics, Faculty of Science, The Islamia University of Bahawalpur, Bahawalpur 63100, Pakistan.
Zia-Ur-Rahman QureshiDepartment of Pharmacy, SBK Women University, Quetta, Pakistan.
Alvina AslamInstitute of Molecular Biology and Biotechnology (IMBB), University of Lahore, Punjab, Pakistan.
Muhammad Hassham Hassan Bin AsadDepartment of Pharmacy, COMSATS University Islamabad, Abbottabad Campus, 22060, Pakistan.ORCID https://orcid.org/0000-0002-2739-9416
University of Gujrat · PKAllama Iqbal Open University · PKCOMSATS University Islamabad · PKIslamia University of Bahawalpur · PKSardar Bahadur Khan Women's University · PKUniversity of Lahore · PKUniversity of Veterinary and Animal Sciences · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosinase and its related proteins are responsible for pigmentation disorders, and inhibiting tyrosinase is an established strategy to treat hyperpigmentation. The carbonyl scaffolds can be effective inhibitors of tyrosinase activity, and the fact that both benzoic and cinnamic acids are safe natural substances with such a scaffolded structure, it was speculated that hydroxyl-substituted benzoic and cinnamic acid derivatives may exhibit potent tyrosinase inhibitory activity. These moieties were incorporated into new chemotypes that displayed in vitro inhibitory effect against mushroom tyrosinase with a view to explore antimelanogenic ingredients. The most active compound, 2-((3-acetylphenyl)amino)-2-oxoethyl(E)-3-(2,4-dihydroxyphenyl)acrylate (5c), inhibited mushroom tyrosinase with an IC

Indexed as

Fungal ProteinsMolecular Docking SimulationMonophenol MonooxygenaseAgaricalesEnzyme InhibitorsEnzyme InhibitorsFungal ProteinsMonophenol Monooxygenase

Identifiers

PMID35059457
PMCPMC8766184
OpenAlexW4206248229

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.