Evidence map›Paper›PMID 26797606›Full record

ReviewInternational journal of molecular sciences2016

The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives.

Maria Giulia Lionetto, Roberto Caricato, Maria Elena Giordano, Trifone Schettino

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Substitution of ZnACS omega · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Carbonic Anhydrase and Biomarker Research: New Insights.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022
    Review
  18. Article
  19. Article
  20. Structural Contour Map of the Iota Carbonic Anhydrase from the DiatomInternational journal of molecular sciences · 2021
    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.

Maria Giulia LionettoDepartment of Biological and Environmental Science and Technologies (DiSTeBA), University of Salento, Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. giulia.lionetto@unisalento.it.
Roberto CaricatoDepartment of Biological and Environmental Science and Technologies (DiSTeBA), University of Salento, Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. roberto.caricato@unisalento.it.
Maria Elena GiordanoDepartment of Biological and Environmental Science and Technologies (DiSTeBA), University of Salento, Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. elena.giordano@unisalento.it.
Trifone SchettinoDepartment of Biological and Environmental Science and Technologies (DiSTeBA), University of Salento, Via Prov.le Lecce-Monteroni, 73100 Lecce, Italy. trifone.schettino@unisalento.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonic anhydrase is a ubiquitous metalloenzyme, which catalyzes the reversible hydration of CO₂ to HCO₃(-) and H⁺. Metals play a key role in the bioactivity of this metalloenzyme, although their relationships with CA have not been completely clarified to date. The aim of this review is to explore the complexity and multi-aspect nature of these relationships, since metals can be cofactors of CA, but also inhibitors of CA activity and modulators of CA expression. Moreover, this work analyzes new insights and perspectives that allow translating new advances in basic science on the interaction between CA and metals to applications in several fields of research, ranging from biotechnology to environmental sciences.

Indexed as

AnimalsBinding SitesBiocatalysisBiological AssayBiomarkersCadmiumCarbonic AnhydrasesCations, DivalentGene Expression RegulationHumansIronIsoenzymesModels, MolecularProtein BindingZincBiomarkersCadmiumCarbonic AnhydrasesCations, DivalentIronIsoenzymesZincbioassaybiomarkercarbonic anhydraseexpressioninhibitionmetals

Identifiers

PMID26797606
PMCPMC4730368

What OpenQuestion holds

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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.