Evidence map›Paper›PMID 28718686›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Kinetic study on the inhibition of xanthine oxidase by acylated derivatives of flavonoids synthesised enzymatically.

Maria Elisa Melo Branco de Araújo, Yollanda Edwirges Moreira Franco, Thiago Grando Alberto, Marcia Cristina Fernandes Messias, Camila Wielewski Leme, Alexandra Christine Helena Frankland Sawaya, Patricia de Oliveira Carvalho

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. 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
1.3field-weighted citation impact, top 20% 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, 23 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

7 authors at 2 institutions in 1 country.

Maria Elisa Melo Branco de Araújoa Laboratory of Multidisciplinary Research , São Francisco University , Bragança Paulista , Brazil.
Yollanda Edwirges Moreira Francoa Laboratory of Multidisciplinary Research , São Francisco University , Bragança Paulista , Brazil.
Thiago Grando Albertoa Laboratory of Multidisciplinary Research , São Francisco University , Bragança Paulista , Brazil.
Marcia Cristina Fernandes Messiasa Laboratory of Multidisciplinary Research , São Francisco University , Bragança Paulista , Brazil.
Camila Wielewski Lemeb Department of Biochemistry , Institute of Biology, State University of Campinas (UNICAMP) , Campinas , Brazil.
Alexandra Christine Helena Frankland Sawayac Department of Plant Biology , Institute of Biology, State University of Campinas (UNICAMP) , Campinas , Brazil.
Patricia de Oliveira Carvalhoa Laboratory of Multidisciplinary Research , São Francisco University , Bragança Paulista , Brazil.
Universidade São Francisco · BRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Studies have reported that flavonoids inhibit xanthine oxidase (XO) activity; however, poor solubility and stability in lipophilic media limit their bioavailability and applications. This study evaluated the kinetic parameters of XO inhibition and partition coefficients of flavonoid esters biosynthesised from hesperidin, naringin, and rutin via enzymatic acylation with hexanoic, octanoic, decanoic, lauric, and oleic acids catalysed by Candida antarctica lipase B (CALB). Quantitative determination by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) showed higher conversion yields (%) for naringin and rutin esters using acyl donors with 8C and 10C. Rutin decanoate had higher partition coefficients (0.95), and naringin octanoate and naringin decanoate showed greater inhibitory effects on XO (IC

Indexed as

AcylationDose-Response Relationship, DrugEnzyme InhibitorsFlavonoidsFungal ProteinsKineticsLipaseMolecular StructureStructure-Activity RelationshipXanthine OxidaseEnzyme InhibitorsFlavonoidsFungal ProteinsLipaselipase B, Candida antarcticaXanthine OxidaseAcylationflavonoidslipasexanthine oxidase

Identifiers

PMID28718686
PMCPMC6445226
OpenAlexW2739058777

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.