Evidence map›Paper›PMID 29072105›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Synthesis and biological evaluation of histamine Schiff bases as carbonic anhydrase I, II, IV, VII, and IX activators.

Suleyman Akocak, Nabih Lolak, Daniela Vullo, Mustafa Durgun, 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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.0field-weighted citation impact, top 5% 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, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Isocoumarins: a new class of selective carbonic anhydrase IX and XII inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2022
    Article
  7. Activation studies with amino acids and amines of a β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Activation studies of the β-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2020
    Article
  12. A structure-based approach towards the identification of novel antichagasic compounds:Journal of enzyme inhibition and medicinal chemistry · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The first activation study of the β-carbonic anhydrases from the pathogenic bacteriaJournal of enzyme inhibition and medicinal chemistry · 2019
    Article
  18. Article
  19. Article
  20. Investigation of piperazines as human carbonic anhydrase I, II, IV and VII activators.Journal of enzyme inhibition and medicinal chemistry · 2018
    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 2 countries.

Suleyman Akocaka Department of Pharmaceutical Chemistry, Faculty of Pharmacy , Adiyaman University , Adiyaman , Turkey.
Nabih Lolaka Department of Pharmaceutical Chemistry, Faculty of Pharmacy , Adiyaman University , Adiyaman , Turkey.
Daniela Vullob NEUROFARBA Dept., Sezione di Scienze Farmaceutiche , Università degli Studi di Firenze , Florence , Italy.
Mustafa Durgunc Department of Chemistry, Faculty of Science and Literature , Harran University , Sanliurfa , Turkey.
Claudiu T Supuranb NEUROFARBA Dept., Sezione di Scienze Farmaceutiche , Università degli Studi di Firenze , Florence , Italy.
Adıyaman University · TRUniversity of Florence · ITHarran University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A series of 20 histamine Schiff base was synthesised by reaction of histamine, a well known carbonic anhydrase (CA, E.C 4.2.2.1.) activator pharmacophore, with substituted aldehydes. The obtained histamine Schiff bases were assayed as activators of five selected human (h) CA isozymes, the cytosolic hCA I, hCA II, and hCA VII, the membrane-anchored hCA IV and transmembrane hCA IX. Some of these compounds showed efficient activity (in the nanomolar range) against the cytosolic isoform hCA VII, which is a key CA enzyme involved in brain metabolism. Moderate activity was observed against hCA I and hCA IV (in the nanomolar to low micromolar range). The structure-activity relationship for activation of these isoforms with the new histamine Schiff bases is discussed in detail based on the nature of the aliphatic, aromatic, or heterocyclic moiety present in the aldehyde fragment of the molecule, which may participate in diverse interactions with amino acid residues at the entrance of the active site, where activators bind, and which is the most variable part among the different CA isoforms.

Indexed as

Biological AssayCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase IVCarbonic Anhydrase IXCarbonic AnhydrasesEnzyme ActivationHistamineHumansMolecular StructureProtein IsoformsSchiff Basescarbonic anhydrase 7, mouseCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase IVCarbonic Anhydrase IXCarbonic AnhydrasesHistamineProtein IsoformsSchiff BasesAlzheimer’s diseaseCarbonic anhydrase activatorshistamineisozymesSchiff bases

Identifiers

PMID29072105
PMCPMC6010137
OpenAlexW2766601154

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.