Evidence map›Paper›PMID 28936885›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Psychoactive substances belonging to the amphetamine class potently activate brain carbonic anhydrase isoforms VA, VB, VII, and XII.

Andrea Angeli, Fabio Vaiano, Francesco Mari, Elisabetta Bertol, Claudiu T Supuran

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Carbon dioxide and MAPK signalling: towards therapy for inflammation.Cell communication and signaling : CCS · 2023
    Review
  3. Article
  4. Activation studies with amino acids and amines of a β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Coumarin carbonic anhydrase inhibitors from natural sources.Journal of enzyme inhibition and medicinal chemistry · 2020
    Review
  14. Article
  15. The first activation study of the β-carbonic anhydrases from the pathogenic bacteriaJournal of enzyme inhibition and medicinal chemistry · 2019
    Article
  16. Article
  17. Investigation of piperazines as human carbonic anhydrase I, II, IV and VII activators.Journal of enzyme inhibition and medicinal chemistry · 2018
    Article
  18. Dioxygen, an unexpected carbonic anhydrase ligand.Journal of enzyme inhibition and medicinal chemistry · 2018
    Article
  19. 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

5 authors at 1 institution in 1 country.

Andrea Angelia Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche e Nutraceutiche , Università degli Studi di Firenze , Florence , Italy.
Fabio Vaianob Forensic Toxicology Division, Department of Health Sciences , University of Florence , Florence , Italy.
Francesco Marib Forensic Toxicology Division, Department of Health Sciences , University of Florence , Florence , Italy.
Elisabetta Bertolb Forensic Toxicology Division, Department of Health Sciences , University of Florence , Florence , Italy.
Claudiu T Supurana Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche e Nutraceutiche , Università degli Studi di Firenze , Florence , Italy.
University of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identifying possible new biological activities of psychoactive substances belonging to various chemical classes may lead to a better understanding of their mode of action and side effects. We report here that amines structurally related to amphetamine, a widely used psychoactive substance, such as amphetamine, methamphetamine, phentermine, mephentermine, and chlorphenteramine, potently activate several carbonic anhydrase (CA, EC 4.2.1.1) isoforms involved in important physiological functions. Of the 11 investigated human (h) isoforms, the widespread hCA I and II, the secreted hCA VI, as well as the cytosolic hCA XIII, and membrane-bound hCA IX and XIV were poorly activated by these amines, whereas the extracellular hCA IV, the mitochondrial enzymes hCA VA/VB, the cytosolic hCA VII, and the transmembrane isoform hCA XII were potently activated. Some of these enzymes are abundant in the brain, raising the possibility that some of the cognitive effects of such psychoactive substances might be related to their activation of these enzymes.

Indexed as

AmphetamineBrainCarbonic AnhydrasesDose-Response Relationship, DrugEnzyme ActivationHumansIsoenzymesModels, MolecularMolecular StructurePsychotropic DrugsStructure-Activity RelationshipAmphetamineCarbonic AnhydrasesIsoenzymesPsychotropic DrugsactivatoramphetamineCarbonic anhydrasemethamphetaminephentermine

Identifiers

PMID28936885
PMCPMC6009978
OpenAlexW2756712334

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.