Evidence map›Paper›PMID 30154947›Full record

ReviewOxidative medicine and cellular longevity2018

Protective Role of Carbonic Anhydrases III and VII in Cellular Defense Mechanisms upon Redox Unbalance.

Anna Di Fiore, Daria M Monti, Andrea Scaloni, Giuseppina De Simone, Simona M Monti

Open access · hybridAbstract readReview
In one paragraph

Review in Oxidative medicine and cellular longevity, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. α-CAs from Photosynthetic Organisms.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Identification of Time-Invariant Biomarkers for Non-Genotoxic Hepatocarcinogen Assessment.International journal of environmental research and public health · 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 3 institutions in 1 country.

Anna Di FioreInstitute of Biostructures and Bioimaging, National Research Council, 80134 Naples, Italy.ORCID 0000-0003-2924-5194
Daria M MontiDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0002-1136-0576
Andrea ScaloniProteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy.ORCID 0000-0001-9362-8515
Giuseppina De SimoneInstitute of Biostructures and Bioimaging, National Research Council, 80134 Naples, Italy.ORCID 0000-0001-9783-5431
Simona M MontiInstitute of Biostructures and Bioimaging, National Research Council, 80134 Naples, Italy.ORCID 0000-0001-9647-7089
Institute of Biostructure and Bioimaging · ITIstituto per il Sistema Produzione Animale in Ambiente Mediterraneo · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Under oxidative stress conditions, several constitutive cellular defense systems are activated, which involve both enzymatic systems and molecules with antioxidant properties such as glutathione and vitamins. In addition, proteins containing reactive sulfhydryl groups may eventually undergo reversible redox modifications whose products act as protective shields able to avoid further permanent molecular oxidative damage either in stressful conditions or under pathological circumstances. After the recovery of normal redox conditions, the reduced state of protein sulfhydryl groups is restored. In this context, carbonic anhydrases (CAs) III and VII, which are human metalloenzymes catalyzing the reversible hydration of carbon dioxide to bicarbonate and proton, have been identified to play an antioxidant role in cells where oxidative damage occurs. Both proteins are mainly localized in tissues characterized by a high rate of oxygen consumption, and contain on their molecular surface two reactive cysteine residues eventually undergoing S-glutathionylation. Here, we will provide an overview on the molecular and functional features of these proteins highlighting their implications into molecular processes occurring during oxidative stress conditions.

Indexed as

AnimalsAntioxidantsCarbonic Anhydrase IIICarbonic AnhydrasesHumansIsoenzymesOxidation-ReductionOxidative StressAntioxidantsCarbonic Anhydrase IIICarbonic AnhydrasesIsoenzymes

Identifiers

PMID30154947
PMCPMC6098850
OpenAlexW2885095741

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.