Evidence map›Paper›PMID 35454074›Full record

ReviewBiomolecules2022

In Search of Differential Inhibitors of Aldose Reductase.

Francesco Balestri, Roberta Moschini, Umberto Mura, Mario Cappiello, Antonella Del Corso

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.0field-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

27 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Review
  3. ExploringMolecules (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. An Investigation of 5-HalogenatedMedicines (Basel, Switzerland) · 2025
    Article
  14. Article
  15. Frontiers in molecular biosciences · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

Francesco BalestriBiochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy.
Roberta MoschiniBiochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy.ORCID 0000-0001-5227-2348
Umberto MuraBiochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy.ORCID 0000-0001-8280-6275
Mario CappielloBiochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy.ORCID 0000-0002-8864-5043
Antonella Del CorsoBiochemistry Unit, Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy.ORCID 0000-0003-3165-6128
University of Pisa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldose reductase, classified within the aldo-keto reductase family as AKR1B1, is an NADPH dependent enzyme that catalyzes the reduction of hydrophilic as well as hydrophobic aldehydes. AKR1B1 is the first enzyme of the so-called polyol pathway that allows the conversion of glucose into sorbitol, which in turn is oxidized to fructose by sorbitol dehydrogenase. The activation of the polyol pathway in hyperglycemic conditions is generally accepted as the event that is responsible for a series of long-term complications of diabetes such as retinopathy, cataract, nephropathy and neuropathy. The role of AKR1B1 in the onset of diabetic complications has made this enzyme the target for the development of molecules capable of inhibiting its activity. Virtually all synthesized compounds have so far failed as drugs for the treatment of diabetic complications. This failure may be partly due to the ability of AKR1B1 to reduce alkenals and alkanals, produced in oxidative stress conditions, thus acting as a detoxifying agent. In recent years we have proposed an alternative approach to the inhibition of AKR1B1, suggesting the possibility of a differential inhibition of the enzyme through molecules able to preferentially inhibit the reduction of either hydrophilic or hydrophobic substrates. The rationale and examples of this new generation of aldose reductase differential inhibitors (ARDIs) are presented.

Indexed as

Diabetes ComplicationsDiabetes MellitusAldehyde ReductaseEnzyme InhibitorsGlucoseHumansAKR1B1 protein, humanAldehyde ReductaseEnzyme InhibitorsGlucoseAKR1B1aldose reductasealdose reductase differential inhibitorsaldose reductase inhibitorsdiabetesinflammationoxidative stress

Identifiers

PMID35454074
PMCPMC9024650
OpenAlexW4220716011

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.