Evidence map›Paper›PMID 26184158›Full record

ReviewInternational journal of molecular sciences2015

Thermostable Carbonic Anhydrases in Biotechnological Applications.

Anna Di Fiore, Vincenzo Alterio, Simona M Monti, Giuseppina De Simone, Katia D'Ambrosio

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Alpha Carbonic Anhydrase fromInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Comparison of Carbonic Anhydrases for COInternational journal of molecular sciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Biocatalytic COInternational journal of molecular sciences · 2020
    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

5 authors at 1 institution in 1 country.

Anna Di FioreIstituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy. anna.difiore@cnr.it.
Vincenzo AlterioIstituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy. vincenzo.alterio@cnr.it.
Simona M MontiIstituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy. marmonti@unina.it.
Giuseppina De SimoneIstituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy. gdesimon@unina.it.
Katia D'AmbrosioIstituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy. katia.dambrosio@cnr.it.
Institute of Biostructure and Bioimaging · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbonic anhydrases are ubiquitous metallo-enzymes which catalyze the reversible hydration of carbon dioxide in bicarbonate ions and protons. Recent years have seen an increasing interest in the utilization of these enzymes in CO2 capture and storage processes. However, since this use is greatly limited by the harsh conditions required in these processes, the employment of thermostable enzymes, both those isolated by thermophilic organisms and those obtained by protein engineering techniques, represents an interesting possibility. In this review we will provide an extensive description of the thermostable carbonic anhydrases so far reported and the main processes in which these enzymes have found an application.

Indexed as

BacteriaCalcium CarbonateCarbon DioxideCarbonic AnhydrasesKineticsProtein EngineeringProtein Structure, TertiaryCalcium CarbonateCarbon DioxideCarbonic Anhydrasescarbonic anhydrasesCO2 capture processprotein engineeringthermostable enzyme

Identifiers

PMID26184158
PMCPMC4519908
OpenAlexW1598850776

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.