Evidence map›Paper›PMID 33615947›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2021

Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase.

Alessio Nocentini, Andrea Angeli, Fabrizio Carta, Jean-Yves Winum, Raivis Zalubovskis, Simone Carradori, Clemente Capasso, William A Donald, Claudiu T Supuran

Open access · goldAbstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
8.1field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Carbonic Anhydrase Inhibitors in Oncology.Sub-cellular biochemistry · 2026
    Review
  4. Review
  5. Review
  6. Human Carbonic Anhydrase Inhibitors.ACS medicinal chemistry letters · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Cloning, expression, and purification of an α-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2024
    Article
  11. Article
  12. Article
  13. Sulfonamide-Based Inhibition of the β-Carbonic Anhydrase fromInternational journal of molecular sciences · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 1,2,3-Benzoxathiazine-2,2-dioxides - effective inhibitors of human carbonic anhydrases.Journal of enzyme inhibition and medicinal chemistry · 2023
    Article

3 more citing papers are in PubMed but not listed here.

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

9 authors at 6 institutions in 6 countries.

Alessio NocentiniNeurofarba Department, Pharmaceutical and Nutraceutical Section, University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0003-3342-702X
Andrea AngeliNeurofarba Department, Pharmaceutical and Nutraceutical Section, University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0002-1470-7192
Fabrizio CartaNeurofarba Department, Pharmaceutical and Nutraceutical Section, University of Florence, Florence, Italy.
Jean-Yves WinumIBMM, Univ. Montpellier, CNRS, ENSCM, Montpellier, France.
Raivis ZalubovskisLatvian Institute of Organic Synthesis, Riga, Latvia.
Simone CarradoriDepartment of Pharmacy, "G. d'Annunzio" University of Chieti-Pescara, Chieti, Italy.ORCID https://orcid.org/0000-0002-8698-9440
Clemente CapassoInstitute of Biosciences and Bioresources, National Research Council, Napoli, Italy.ORCID https://orcid.org/0000-0003-3314-2411
William A DonaldSchool of Chemistry, University of New South Wales, Sydney, Australia.
Claudiu T SupuranNeurofarba Department, Pharmaceutical and Nutraceutical Section, University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0003-4262-0323
University of Florence · ITÉcole Nationale Supérieure de Chimie de Montpellier · FRNational Academies of Sciences, Engineering, and Medicine · USRiga Technical University · LVUniversity of Chieti-Pescara · ITUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inorganic anions inhibit the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) generally by coordinating to the active site metal ion. Cyanate was reported as a non-coordinating CA inhibitor but those erroneous results were subsequently corrected by another group. We review the anion CA inhibitors (CAIs) in the more general context of drug design studies and the discovery of a large number of inhibitor classes and inhibition mechanisms, including zinc binders (sulphonamides and isosteres, dithiocabamates and isosteres, thiols, selenols, benzoxaboroles, ninhydrins, etc.); inhibitors anchoring to the zinc-coordinated water molecule (phenols, polyamines, sulfocoumarins, thioxocoumarins, catechols); CAIs occluding the entrance to the active site (coumarins and derivatives, lacosamide), as well as compounds that bind outside the active site. All these new chemotypes integrated with a general procedure for obtaining isoform-selective compounds (the tail approach) has resulted, through the guidance of rigorous X-ray crystallography experiments, in the development of highly selective CAIs for all human CA isoforms with many pharmacological applications.

Indexed as

Drug DesignAnionsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesCoordination ComplexesCrystallography, X-RayHumansIsoenzymesModels, MolecularZincAnionsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesCoordination ComplexesIsoenzymesZinccarbonic anhydrasecyanateinhibition mechanismsinhibitorsulphonamide

Identifiers

PMID33615947
PMCPMC7901698
OpenAlexW3133227992

What OpenQuestion holds

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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.