Evidence map›Paper›PMID 32746656›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2020

Sonia Del Prete, Silvia Bua, Claudiu T Supuran, Clemente Capasso

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Selected strategies to fight pathogenic bacteria.Journal of enzyme inhibition and medicinal chemistry · 2023
    Review
  7. Article
  8. Review
  9. The gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  10. Biological investigation ofJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  11. Antibiotics (Basel, Switzerland) · 2022
    Article
  12. Article
  13. Article
  14. Activation of the β-carbonic anhydrase from the protozoan pathogenJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  15. Anion inhibition studies of the α-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  16. An anion and small molecule inhibition study of the β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  17. An overview on the recently discovered iota-carbonic anhydrases.Journal of enzyme inhibition and medicinal chemistry · 2021
    Review
  18. Inhibition of the β-carbonic anhydrase from the protozoan pathogenJournal of enzyme inhibition and medicinal chemistry · 2021
    Article
  19. Selective Inhibition ofInternational journal of molecular sciences · 2021
    Article
  20. 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

4 authors at 2 institutions in 1 country.

Sonia Del PreteDepartment of Biology, Agriculture and Food Sciences, CNR, Institute of Biosciences and Bioresources, Napoli, Italy.ORCID https://orcid.org/0000-0001-5291-8823
Silvia BuaSection of Pharmaceutical and Nutraceutical Sciences, Department of NEUROFARBA, University of Florence, Firenze, Italy.
Claudiu T SupuranSection of Pharmaceutical and Nutraceutical Sciences, Department of NEUROFARBA, University of Florence, Firenze, Italy.ORCID https://orcid.org/0000-0003-4262-0323
Clemente CapassoDepartment of Biology, Agriculture and Food Sciences, CNR, Institute of Biosciences and Bioresources, Napoli, Italy.ORCID https://orcid.org/0000-0003-3314-2411
Institute of Biosciences and Bioresources · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes involved in biosynthetic processes, transport, supply, and balance of CO

Indexed as

Carbonic Anhydrase InhibitorsCarbonic AnhydrasesDose-Response Relationship, DrugEscherichia coliMolecular StructureRecombinant ProteinsStructure-Activity RelationshipSulfonamidesCarbonic Anhydrase InhibitorsCarbonic AnhydrasesRecombinant ProteinsSulfonamidesantibacterialsCarbonic anhydraseEscherichia coliinhibitorssulphonamides

Identifiers

PMID32746656
PMCPMC7470111
OpenAlexW3047296269

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.