Evidence map›Paper›PMID 28856935›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

The use of dimethylsulfoxide as a solvent in enzyme inhibition studies: the case of aldose reductase.

Livia Misuri, Mario Cappiello, Francesco Balestri, Roberta Moschini, Vito Barracco, Umberto Mura, Antonella Del-Corso

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Cytological profiling of trypanocidal principles fromPhytomedicine plus : international journal of phytotherapy and phytopharmacology · 2025
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  6. Long-term cell fate and functional maintenance of human hepatocyte through stepwise culture configuration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
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  11. Review
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  13. Intra-site differential inhibition of multi-specific enzymes.Journal of enzyme inhibition and medicinal chemistry · 2020
    Review
  14. Article
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.

Livia Misuria Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Mario Cappielloa Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Francesco Balestria Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Roberta Moschinia Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Vito Barraccoa Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Umberto Muraa Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
Antonella Del-Corsoa Department of Biology, Biochemistry Unit , University of Pisa , Pisa , Italy.
University of Pisa · ITRegione Toscana

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldose reductase (AR) is an enzyme devoted to cell detoxification and at the same time is strongly involved in the aetiology of secondary diabetic complications and the amplification of inflammatory phenomena. AR is subjected to intense inhibition studies and dimethyl sulfoxide (DMSO) is often present in the assay mixture to keep the inhibitors in solution. DMSO was revealed to act as a weak but well detectable AR differential inhibitor, acting as a competitive inhibitor of the L-idose reduction, as a mixed type of non-competitive inhibitor of HNE reduction and being inactive towards 3-glutathionyl-4-hydroxynonanal transformation. A kinetic model of DMSO action with respect to differently acting inhibitors was analysed. Three AR inhibitors, namely the flavonoids neohesperidin dihydrochalcone, rutin and phloretin, were used to evaluate the effects of DMSO on the inhibition studies on the reduction of L-idose and HNE.

Indexed as

Aldehyde ReductaseDimethyl SulfoxideDose-Response Relationship, DrugEnzyme InhibitorsHumansRecombinant ProteinsSolventsStructure-Activity RelationshipAldehyde ReductaseDimethyl SulfoxideEnzyme InhibitorsRecombinant ProteinsSolventsaldose reductasealdose reductase differential inhibitorsDimethyl sulfoxide

Identifiers

PMID28856935
PMCPMC6009938
OpenAlexW2750773993

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.