Evidence map›Paper›PMID 29199489›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2018

Crystal structure of the human carbonic anhydrase II adduct with 1-(4-sulfamoylphenyl-ethyl)-2,4,6-triphenylpyridinium perchlorate, a membrane-impermeant, isoform selective inhibitor.

Vincenzo Alterio, Davide Esposito, Simona Maria Monti, Claudiu T Supuran, Giuseppina De Simone

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  6. Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020
    Article
  7. Article
  8. Benzothiazole derivatives as anticancer agents.Journal of enzyme inhibition and medicinal chemistry · 2020
    Review
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  10. Article
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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 2 institutions in 1 country.

Vincenzo Alterioa Istituto di Biostrutture e Bioimagini-CNR , Naples , Italy.
Davide Espositoa Istituto di Biostrutture e Bioimagini-CNR , Naples , Italy.
Simona Maria Montia Istituto di Biostrutture e Bioimagini-CNR , Naples , Italy.
Claudiu T Supuranb Neurofarba Department, Section of Pharmaceutical and Nutraceutical Sciences , Università degli Studi di Firenze , Sesto Fiorentino, Florence , Italy.
Giuseppina De Simonea Istituto di Biostrutture e Bioimagini-CNR , Naples , Italy.
Institute of Biostructure and Bioimaging · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyridinium containing sulfonamides have been largely investigated as carbonic anhydrase inhibitors (CAIs), showing interesting selectivity features. Nevertheless, only few structural studies are so far available on adducts that these compounds form with diverse CA isoforms. In this paper, we report the structural characterization of the adduct that a triphenylpyridinium derivative forms with hCA II, showing that the substitution of the pyridinium ring plays a key role in determining the conformation of the inhibitor in the active site and consequently the binding affinity to the enzyme. These findings open new perspectives on the basic structural requirements for designing sulfonamide CAIs with a selective inhibition profile.

Indexed as

Carbonic Anhydrase IICarbonic Anhydrase InhibitorsCrystallography, X-RayDose-Response Relationship, DrugHumansModels, MolecularMolecular StructurePyridinium CompoundsStructure-Activity RelationshipSulfonamides1-(4-sulfamoylphenylethyl)-2,4,6-triphenylpyridiniumCarbonic Anhydrase IICarbonic Anhydrase InhibitorsPyridinium CompoundsSulfonamidescarbonic anhydrasemembrane-impermeant inhibitorsX-ray crystallography

Identifiers

PMID29199489
PMCPMC7011996
OpenAlexW2771096172

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.