Evidence map›Paper›PMID 34201208›Full record

ArticleInternational journal of molecular sciences2021

The Role of Anthocyanins, Deoxyanthocyanins and Pyranoanthocyanins on the Modulation of Tyrosinase Activity: An In Vitro and In Silico Approach.

Patrícia Correia, Hélder Oliveira, Paula Araújo, Natércia F Brás, Ana Rita Pereira, Joana Moreira, Victor de Freitas, Nuno Mateus, Joana Oliveira, Iva Fernandes

Open access · goldAbstract read
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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

3 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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 1 institution in 1 country.

Patrícia CorreiaLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-2983-4290
Hélder OliveiraLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-8256-2968
Paula AraújoLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.
Natércia F BrásLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-3130-9807
Ana Rita PereiraLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-9779-2678
Joana MoreiraLaboratório de Química Orgânica e Farmacêutica, Departamento de Ciências Químicas, Faculty of Pharmacy of the University of Porto, Rua Jorge Viterbo Ferreira nº 228, 4050-313 Porto, Portugal.
Victor de FreitasLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.
Nuno MateusLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-9318-9732
Joana OliveiraLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0002-9996-1463
Iva FernandesLAQV-REQUIMTE, Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, 4169-007 Porto, Portugal.ORCID 0000-0003-2297-0086
Universidade do Porto · PT

Funding

Fundação para a Ciência e a Tecnologia PTDC/QUI-OUT/29013/2017
6 · The paper itself

Abstract

Tyrosinase is the central enzyme involved in the highly complex process of melanin formation, catalyzing the rate-limiting steps of this biosynthetic pathway. Due to such a preponderant role, it has become a major target in the treatment of undesired skin pigmentation conditions and also in the prevention of enzymatic food browning. Numerous phenolic-based structures from natural sources have been pointed out as potential tyrosinase inhibitors, including anthocyanins. The aim of the present study was to individually assess the tyrosinase inhibitory activity of eight purified compounds with a variable degree of structural complexity: native anthocyanins, deoxyanthocyanins, and pyranoanthocyanins. The latter two, the groups of anthocyanin-related compounds with enhanced stability, were tested for the first time. Compounds

Indexed as

AgaricalesAnthocyaninsCatalysisComputer SimulationEnzyme InhibitorsHumansIn Vitro TechniquesMolecular Docking SimulationMolecular StructureMonophenol MonooxygenaseOxidation-ReductionStructure-Activity RelationshipAnthocyaninsEnzyme InhibitorsMonophenol Monooxygenaseanthocyaninsdeoxyanthocyaninsenzymatic inhibitionmolecular dockingpigmentationpyranoanthocyaninsstructure–activity relationshiptyrosinase

Identifiers

PMID34201208
PMCPMC8230073
OpenAlexW3167761970

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.