Evidence map›Paper›PMID 27725765›Full record

ArticleScientific reports2016

The unravelling of the complex pattern of tyrosinase inhibition.

Batel Deri, Margarita Kanteev, Mor Goldfeder, Daniel Lecina, Victor Guallar, Noam Adir, Ayelet Fishman

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 169 citations in OpenAlex.

  1. Trial
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  8. Molecules (Basel, Switzerland) · 2026
    Article
  9. Untargeted UHPLC-HRMS Metabolomic Profiling ofAntioxidants (Basel, Switzerland) · 2025
    Article
  10. Article
  11. Review
  12. Genetic mutations disrupt the coordinated mode of tyrosinase's intra-melanosomal domain.Protein science : a publication of the Protein Society · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
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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

7 authors at 3 institutions in 2 countries.

Batel DeriDepartment of Biotechnology and Food Engineering, Technion-Israel Institute of Technology, Haifa, 3200003, Israel.
Margarita KanteevDepartment of Biotechnology and Food Engineering, Technion-Israel Institute of Technology, Haifa, 3200003, Israel.
Mor GoldfederDepartment of Biotechnology and Food Engineering, Technion-Israel Institute of Technology, Haifa, 3200003, Israel.
Daniel LecinaJoint BSC-CRG-IRB Research Program in Computational Biology, Barcelona Supercomputing Center, Jordi Girona 29, 08034 Barcelona, Spain.
Victor GuallarJoint BSC-CRG-IRB Research Program in Computational Biology, Barcelona Supercomputing Center, Jordi Girona 29, 08034 Barcelona, Spain.
Noam AdirSchulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa, 3200003, Israel.
Ayelet FishmanDepartment of Biotechnology and Food Engineering, Technion-Israel Institute of Technology, Haifa, 3200003, Israel.
Technion – Israel Institute of Technology · ILBarcelona Supercomputing Center · ESInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosinases are responsible for melanin formation in all life domains. Tyrosinase inhibitors are used for the prevention of severe skin diseases, in skin-whitening creams and to avoid fruit browning, however continued use of many such inhibitors is considered unsafe. In this study we provide conclusive evidence of the inhibition mechanism of two well studied tyrosinase inhibitors, KA (kojic acid) and HQ (hydroquinone), which are extensively used in hyperpigmentation treatment. KA is reported in the literature with contradicting inhibition mechanisms, while HQ is described as both a tyrosinase inhibitor and a substrate. By visualization of KA and HQ in the active site of TyrBm crystals, together with molecular modeling, binding constant analysis and kinetic experiments, we have elucidated their mechanisms of inhibition, which was ambiguous for both inhibitors. We confirm that while KA acts as a mixed inhibitor, HQ can act both as a TyrBm substrate and as an inhibitor.

Indexed as

Bacillus megateriumEnzyme InhibitorsHydroquinonesHyperpigmentationKineticsMelaninsMonophenol MonooxygenasePyronesSkinEnzyme InhibitorshydroquinoneHydroquinoneskojic acidMelaninsMonophenol MonooxygenasePyrones

Identifiers

PMID27725765
PMCPMC5057104
OpenAlexW2531874273

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.