Evidence map›Paper›PMID 33430028›Full record

ArticleInternational journal of molecular sciences2021

Effect of Sulfonamides and Their Structurally Related Derivatives on the Activity of ι-Carbonic Anhydrase from

Viviana De Luca, Andrea Petreni, Alessio Nocentini, Andrea Scaloni, Claudiu T Supuran, Clemente Capasso

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Comparative study on Antibacterial efficacy of a series of chromone sulfonamide derivatives against drug-resistant and MDR-isolates.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  3. Article
  4. Review
  5. The gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  6. Dithiocarbamates effectively inhibit the α-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  7. Article
  8. An overview on the recently discovered iota-carbonic anhydrases.Journal of enzyme inhibition and medicinal chemistry · 2021
    Review
  9. An anion and small molecule inhibition study of the β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  10. Anion inhibition studies of the α-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  11. 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

6 authors at 3 institutions in 1 country.

Viviana De LucaInstitute of Biosciences and Bioresources, CNR, via Pietro Castellino 111, 80131 Napoli, Italy.
Andrea PetreniSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, 50019 Florence, Italy.
Alessio NocentiniSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, 50019 Florence, Italy.ORCID 0000-0003-3342-702X
Andrea ScaloniProteomics & Mass Spectrometry Laboratory, ISPAAM, CNR, via Argine 1085, 80147 Napoli, Italy.
Claudiu T SupuranSection of Pharmaceutical and Nutraceutical Sciences, Department of Neurofarba, University of Florence, Via U. Schiff 6, 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
University of Florence · ITIstituto per il Sistema Produzione Animale in Ambiente Mediterraneo · ITInstitute of Biosciences and Bioresources · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonic anhydrases (CAs) are essential metalloenzymes in nature, catalyzing the carbon dioxide reversible hydration into bicarbonate and proton. In humans, breathing and many other critical physiological processes depend on this enzymatic activity. The CA superfamily function and inhibition in pathogenic bacteria has recently been the object of significant advances, being demonstrated to affect microbial survival/virulence. Targeting bacterial CAs may thus be a valid alternative to expand the pharmacological arsenal against the emergence of widespread antibiotic resistance. Here, we report an extensive study on the inhibition profile of the recently discovered ι-CA class present in some bacteria, including

Indexed as

Amino Acid SequenceBenzeneBurkholderiaCarbonic Anhydrase InhibitorsCarbonic AnhydrasesHumansMolecular StructureRespirationStructure-Activity RelationshipSulfonamidesBenzeneCarbonic Anhydrase InhibitorsCarbonic AnhydrasesSulfonamidesCarbonic anhydrasesinhibitorkinetic constantsmetalloenzymesulfonamides

Identifiers

PMID33430028
PMCPMC7827628
OpenAlexW3118704054

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.