Evidence map›Paper›PMID 32545297›Full record

ArticleInternational journal of molecular sciences2020

The Effect of Substituted Benzene-Sulfonamides and Clinically Licensed Drugs on the Catalytic Activity of CynT2, a Carbonic Anhydrase Crucial for

Sonia Del Prete, Viviana De Luca, Silvia Bua, Alessio Nocentini, Vincenzo Carginale, Claudiu T Supuran, Clemente Capasso

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Novel Drug Screening Assay forJournal of medicinal chemistry · 2024
    Article
  5. Selected strategies to fight pathogenic bacteria.Journal of enzyme inhibition and medicinal chemistry · 2023
    Review
  6. Review
  7. Article
  8. Article
  9. Biological investigation ofJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  10. The gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  11. Article
  12. Article
  13. An anion and small molecule inhibition study of the β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  14. Anion inhibition studies of the α-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  15. Activation of the β-carbonic anhydrase from the protozoan pathogenJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  16. Selective Inhibition ofInternational journal of molecular sciences · 2021
    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 3 institutions in 1 country.

Sonia Del PreteInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.
Viviana De LucaInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.
Silvia BuaSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy.
Alessio NocentiniSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy.ORCID 0000-0003-3342-702X
Vincenzo CarginaleInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.ORCID 0000-0002-1842-494X
Claudiu T SupuranSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy.ORCID 0000-0003-4262-0323
Clemente CapassoInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.ORCID 0000-0003-3314-2411
Institute of Biosciences and Bioresources · ITUniversity of Florence · ITIstituto per il Sistema Produzione Animale in Ambiente Mediterraneo · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are relevant antimicrobial drug targets, and among them, enzymes represent a significant group, since most of them catalyze reactions essential for supporting the central metabolism, or are necessary for the pathogen vitality. Genomic exploration of pathogenic and non-pathogenic microorganisms has revealed genes encoding for a superfamily of metalloenzymes, known as carbonic anhydrases (CAs, EC 4.2.1.1). CAs catalyze the physiologically crucial reversible reaction of the carbon dioxide hydration to bicarbonate and protons. Herein, we investigated the sulfonamide inhibition profile of the recombinant

Indexed as

Anion Transport ProteinsAnti-Bacterial AgentsBenzeneCarbon DioxideCarbonic Anhydrase InhibitorsCarbonic AnhydrasesDrug Evaluation, PreclinicalEscherichia coli ProteinsHumansStructure-Activity RelationshipSulfonamidesAnion Transport ProteinsAnti-Bacterial AgentsBenzenecan protein, E coliCarbon DioxideCarbonic Anhydrase InhibitorsCarbonic Anhydrasescyanate permease, E coliEscherichia coli ProteinsSulfonamidesantibacterialscarbonic anhydraseEscherichia coliinhibitorsprotonographystopped-flow assaysulfonamides

Identifiers

PMID32545297
PMCPMC7312386
OpenAlexW3034403254

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.