Evidence map›Paper›PMID 32408533›Full record

ArticleMolecules (Basel, Switzerland)2020

Crystal Structure of a Tetrameric Type II β-Carbonic Anhydrase from the Pathogenic Bacterium

Andrea Angeli, Marta Ferraroni, Mariana Pinteala, Stelian S Maier, Bogdan C Simionescu, Fabrizio Carta, Sonia Del Prete, Clemente Capasso, Claudiu T Supuran

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Activation of the β-carbonic anhydrase from the protozoan pathogenJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  5. 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

9 authors at 3 institutions in 2 countries.

Andrea AngeliNEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, Università degli Studi di Firenze, 50019 Sesto Fiorentino (Florence), Italy.ORCID 0000-0002-1470-7192
Marta FerraroniDepartment of Chemistry "Ugo Schiff", Via della Lastruccia 13, Università degli Studi di Firenze, I-50019 Sesto Fiorentino (Florence), Italy.ORCID 0000-0001-7258-738X
Mariana PintealaCentre of Advanced Research in Bionanoconjugates and Biopolymers Department, "Petru Poni" Institute of Macromolecular Chemistry, 700487 Iasi, Romania.ORCID 0000-0002-4021-982X
Stelian S MaierCentre of Advanced Research in Bionanoconjugates and Biopolymers Department, "Petru Poni" Institute of Macromolecular Chemistry, 700487 Iasi, Romania.
Bogdan C SimionescuCentre of Advanced Research in Bionanoconjugates and Biopolymers Department, "Petru Poni" Institute of Macromolecular Chemistry, 700487 Iasi, Romania.
Fabrizio CartaNEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, Università degli Studi di Firenze, 50019 Sesto Fiorentino (Florence), Italy.ORCID 0000-0002-1141-6146
Sonia Del PreteIstituto di Bioscienze e Biorisorse, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.
Clemente CapassoIstituto di Bioscienze e Biorisorse, CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.ORCID 0000-0003-3314-2411
Claudiu T SupuranNEUROFARBA Department, Sezione di Scienze Farmaceutiche, Via Ugo Schiff 6, Università degli Studi di Firenze, 50019 Sesto Fiorentino (Florence), Italy.ORCID 0000-0003-4262-0323
University of Florence · ITInstitute of Biosciences and Bioresources · ITGheorghe Asachi Technical University of Iași · RO

Funding

Romanian Ministry of Research and Innovation, CNCS-UEFISCDI PN-III-P4-ID-PCCF-2016-0050
6 · The paper itself

Abstract

Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate and proton. Currently, CA inhibitors are widely used as antiglaucoma, anticancer, and anti-obesity drugs and for the treatment of neurological disorders. Recently, the potential use of CA inhibitors to fight infections caused by protozoa, fungi, and bacteria has emerged as a new research line. In this article, the X-ray crystal structure of β-CA from

Indexed as

Bacterial ProteinsCarbonic Anhydrase IIBurkholderia pseudomalleiCarbonic Anhydrase InhibitorsCatalytic DomainCrystallography, X-RayProtein Structure, QuaternaryBacterial ProteinsCarbonic Anhydrase IICarbonic Anhydrase InhibitorsBurkholderia pseudomalleicrystal structuretype II CAβ-Carbonic Anhydrase

Identifiers

PMID32408533
PMCPMC7287614
OpenAlexW3024876342

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.