Evidence map›Paper›PMID 32143488›Full record

ArticleInternational journal of molecular sciences2020

Activation Effects of Carnosine- and Histidine-Containing Dipeptides on Human Carbonic Anhydrases: A Comprehensive Study.

Giulio Vistoli, Giancarlo Aldini, Laura Fumagalli, Clelia Dallanoce, Andrea Angeli, Claudiu T Supuran

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Carbonic Anhydrases II, IX, and XII in Reflux Esophagitis.Digestive diseases and sciences · 2022
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Coumarin carbonic anhydrase inhibitors from natural sources.Journal of enzyme inhibition and medicinal chemistry · 2020
    Review
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

6 authors at 2 institutions in 1 country.

Giulio VistoliDepartment of Pharmaceutical Sciences, University of Milan, Via Luigi Mangiagalli 25, 20133 Milan, Italy.
Giancarlo AldiniDepartment of Pharmaceutical Sciences, University of Milan, Via Luigi Mangiagalli 25, 20133 Milan, Italy.ORCID 0000-0002-2355-6744
Laura FumagalliDepartment of Pharmaceutical Sciences, University of Milan, Via Luigi Mangiagalli 25, 20133 Milan, Italy.ORCID 0000-0003-1917-3000
Clelia DallanoceDepartment of Pharmaceutical Sciences, University of Milan, Via Luigi Mangiagalli 25, 20133 Milan, Italy.ORCID 0000-0002-7383-1484
Andrea AngeliDepartment of Neurosciences, Psychology, Drug Research and Child Health, University of Florence Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy.ORCID 0000-0002-1470-7192
Claudiu T SupuranDepartment of Neurosciences, Psychology, Drug Research and Child Health, University of Florence Via U. Schiff 6, Sesto Fiorentino, 50019 Florence, Italy.ORCID 0000-0003-4262-0323
University of Milan · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-Carnosine (β-Ala-l-His) and several other histidine-containing peptides, including two N-methylated forms on the imidazole ring (l-anserine and l-balenine), two derivatives modified on the carboxyl function (carcinine and l-carnosinamide), two analogues differing in the length of the N-terminal residue (l-homocarnosine and Gly-l-His) and the N-acetyl derivatives, were investigated as activators of four isoforms of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1). The four human isoforms hCA I, II, VA and IX were activated in the low to high micromolar range, with a rather complex structure activity relationship. A performed computational study allowed us to rationalize these results and to propose a binding mode of these activators within the enzyme active site. Similarly to other CA activators, the here studied peptides could find relevant pharmacological applications such as in the management of CA deficiencies, for therapy memory and enhancing cognition or for artificial tissues engineering.

Indexed as

Carbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase IXCarbonic AnhydrasesCarbonic Anhydrase VCarnosineChelating AgentsDipeptidesHistidineHumansKineticsModels, MolecularProtein DomainsProtonsSoftwareCarbonic Anhydrase ICarbonic Anhydrase IICarbonic Anhydrase IXCarbonic AnhydrasesCarbonic Anhydrase VcarcinineCarnosineChelating AgentsDipeptidesHistidinehomocarnosineProtonsactivatorcarbonic anhydrasecarnosinedipeptidehistidineproton shuttling

Identifiers

PMID32143488
PMCPMC7084589
OpenAlexW3009702175

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.