Evidence map›Paper›PMID 34482770›Full record

ReviewJournal of enzyme inhibition and medicinal chemistry2021

An overview on the recently discovered iota-carbonic anhydrases.

Alessio Nocentini, Claudiu T Supuran, Clemente Capasso

Open access · goldAbstract readReview
In one paragraph

Review in Journal of enzyme inhibition and medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026
    Review
  9. Article
  10. Article
  11. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  12. Article
  13. Article
  14. Unusual regulation of the COApplied and environmental microbiology · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

Alessio NocentiniDepartment of NEUROFARBA, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence, Firenze, Italy.ORCID 0000-0003-3342-702X
Claudiu T SupuranDepartment of NEUROFARBA, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence, Firenze, Italy.ORCID 0000-0003-4262-0323
Clemente CapassoDepartment of Biology, Agriculture and Food Sciences, Institute of Biosciences and Bioresources, CNR, Napoli, Italy.ORCID 0000-0003-3314-2411
University of Florence · ITInstitute of Biosciences and Bioresources · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) have been studied for decades and have been classified as a superfamily of enzymes which includes, up to date, eight gene families or classes indicated with the Greek letters α, β, γ, δ, ζ, η, θ, ι. This versatile enzyme superfamily is involved in multiple physiological processes, catalysing a fundamental reaction for all living organisms, the reversible hydration of carbon dioxide to bicarbonate and a proton. Recently, the ι-CA (LCIP63) from the diatom

Indexed as

BiocatalysisBurkholderiaCarbonic AnhydrasesCyanobacteriaEukaryotaCarbonic AnhydrasesbacteriaCA classesCarbonic anhydrasescatalytic pockethydratase activity

Identifiers

PMID34482770
PMCPMC8425729
OpenAlexW3196986287

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.